|
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 ... |
869-1949 |
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: 1491.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 869 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 948
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 949 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1028
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1029 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1108
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1109 KEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1188
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1189 LRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1268
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1269 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE 1348
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1349 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQR 1428
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1429 LEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALS 1508
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1509 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1588
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1589 NMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1668
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1669 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAL 1748
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1749 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1828
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1829 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1908
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1039738673 1909 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1949
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-792 |
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: 1440.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVGLDQVTGMTET 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD---------------------VDRIVGLDQVTGMTET 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 659 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14920 540 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14920 620 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-792 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1323.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP-GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQKPRQLKDKADF 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQtiqrasfydsvsglheppvdrivgldqvtgm 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE------------------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 656 tETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 735
Cdd:cd01377 527 -SGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKG 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 736 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01377 606 FPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-792 |
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: 1225.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVGLDQVTG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD---------------------VDRIVGLDKVAG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 655 MTETAFGsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd14932 540 MGESLHG-AFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQ 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 735 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14932 619 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-792 |
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: 1198.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVGLDQVTGMTET 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD---------------------VDRIIGLDQVAGMSET 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 659 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14919 537 ALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14919 617 RVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-792 |
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: 1194.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVGLDQVTGMTET 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD---------------------VDRIVGLDQMAKMTES 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 659 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14921 540 SLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14921 620 RIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-792 |
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: 1175.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN----IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVGLDQVTG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD---------------------VDRIVGLDKVSG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 655 MTEtaFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd15896 540 MSE--MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 735 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd15896 618 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-792 |
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: 1160.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASS---------HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 250 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 330 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKpRQL 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiqrasfydsvsglheppvdRIVGL 649
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA----------------------EIVGM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 650 DQVTgMTETAFGSayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 729
Cdd:cd14911 535 AQQA-LTDTQFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGI 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 730 RICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14911 612 RICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-792 |
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: 1142.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQETMEAMHIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVGLDQVTGMTET 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD---------------------VEGIVGLEQVSSLGDG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 659 AFGSayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14930 539 PPGG--RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPN 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14930 617 RILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-792 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1104.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 247 RINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDN 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 566 PRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRAsfydsvsglheppvdr 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAA---------------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 646 ivgldqvtgMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 725
Cdd:pfam00063 537 ---------ANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGV 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 726 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:pfam00063 608 LEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-804 |
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: 1015.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIP 318
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGgCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 319 GQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGMNVMEFTRAIL 397
Cdd:smart00242 235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 398 TPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQ 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 558 GSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsg 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN------------ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 638 lheppvdrivgldqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVL 717
Cdd:smart00242 538 ---------------------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVL 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 718 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLA 797
Cdd:smart00242 591 HQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLA 670
|
....*..
gi 1039738673 798 HLEEERD 804
Cdd:smart00242 671 ELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1482 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 917.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 36 VWIPSERHGFEAASIKEERGDEVMVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 191 VIQYLAHVASSHkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 271 AVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKV 349
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 350 VSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATY 429
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 430 ERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 510 DFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQKPRQLKDKadFCIIHYAGKVDYK 587
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 588 ADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppvdrivgldqvtgmtetafgsaykTK 667
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI----------------------------------------ES 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 668 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 747
Cdd:COG5022 601 KGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQ 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 748 RYEILTPNA----IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLA 823
Cdd:COG5022 681 RYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYL 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 824 RKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEEL--LKVKEKQTKVEGELEEMER 901
Cdd:COG5022 761 RRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIikLQKTIKREKKLRETEEVEF 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 902 KHQqlleeknilAEQLQAETELFAEAEEMRARLaaKKQELEEilhdlesrveeeeernQILQNEKKKMQAHIQDLEEQLD 981
Cdd:COG5022 841 SLK---------AEVLIQKFGRSLKAKKRFSLL--KKETIYL----------------QSAQRVELAERQLQELKIDVKS 893
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 982 EEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSS--QLAEEEEKAKNLAKIRNKQEVmISD 1059
Cdd:COG5022 894 ISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESKLKET-SEE 972
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1060 LEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQVDELKV---------QLTKKEEELQGALARGDDETLHK 1127
Cdd:COG5022 973 YEDLLKKSTILVREGNKANSELKNfkkELAELSKQYGALQESTKQLKElpvevaelqSASKIISSESTELSILKPLQKLK 1052
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1128 NNALKVARELQAQIAELQEDFESEKASRNKAEKQK--RDLSEELEALKTELEDT-------LDTTAAQQELRTKREQEVA 1198
Cdd:COG5022 1053 GLLLLENNQLQARYKALKLRRENSLLDDKQLYQLEstENLLKTINVKDLEVTNRnlvkpanVLQFIVAQMIKLNLLQEIS 1132
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1199 ELKKALEDETKNHEAQIQ------DMRQRHATALEELS-----EQLEQAKRFKANLEKNKQGLETDNKELACEVK-VLQQ 1266
Cdd:COG5022 1133 KFLSQLVNTLEPVFQKLSvlqlelDGLFWEANLEALPSpppfaALSEKRLYQSALYDEKSKLSSSEVNDLKNELIaLFSK 1212
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1267 VKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDN--VSTLLEEAEKKGIKFAKDA----AGLESQLQD 1340
Cdd:COG5022 1213 IFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNekLLSLLNSIDNLLSSYKLEEevlpATINSLLQY 1292
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1341 TQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQsQLADTKKKVDDDLGTIesleeakKKLLK 1420
Cdd:COG5022 1293 INVGLFNALRTKASSLRWKSATEVNYNSEELDDWCREFEISDVDEELEELI-QAVKVLQLLKDDLNKL-------DELLD 1364
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1421 DVEALSQRLEEKVLA-YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK--QKKFDQLLAEEK 1482
Cdd:COG5022 1365 ACYSLNPAEIQNLKSrYDPADKENNLPKEILKKIEALLIKQELQLSLEGKDetEVHLSEIFSEEK 1429
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-792 |
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: 861.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQDKDNFQETMEA 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 333 MHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 570 KDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdeiqtiqrasfydsvsglheppvdrivgl 649
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 650 dqvtgmtetafgsayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 729
Cdd:cd00124 519 ----------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAV 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 730 RICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd00124 571 RIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-792 |
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: 782.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVA------SSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 491 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR-- 567
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 568 -QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfyDSVSglheppvdri 646
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGS-------DSTE---------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 647 vglDQVTGMTETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 726
Cdd:cd14927 539 ---DPKSGVKEK------RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVL 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 727 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14927 610 EGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-792 |
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: 771.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSH--KGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKAD 574
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 --FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfYDSVSGlheppvdrivgldqv 652
Cdd:cd14913 477 ahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT----------FATADA--------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 653 tgmtETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14913 532 ----DSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRIC 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 733 RQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14913 608 RKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 750.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLK---DKA 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppvdrivgldqvT 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQ---------------------------S 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 654 GMTETAFGSAYKtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14909 530 GGGEQAKGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICR 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 734 QGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14909 609 KGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-792 |
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: 739.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK---A 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdRFVAELWKDEiqtiqrasfydsvsglheppvdrivgldqvt 653
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFKE------------------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 654 gmtETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14934 523 ---EEAPAGSKKQKRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRIC 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 733 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14934 600 RKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-792 |
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: 720.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGrkDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 418 DFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 497 EEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK--FQKPRQLKDKad 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhqssdrfvaelwkdeiqtiqRASfydsvsglheppvdrivgldqvtg 654
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVL--------------------KAS------------------------ 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 655 mtetafgsayKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd01380 506 ----------KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAA 572
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 735 GFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01380 573 GFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-792 |
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: 713.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK--A 573
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppvdrivgldqvt 653
Cdd:cd14929 472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIST---------------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 654 gMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14929 524 -DSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICR 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 734 QGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14929 603 EGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-792 |
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: 705.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK-- 572
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKpe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglhEPPVDRIVGldqv 652
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGA--------------DAPIEKGKG---- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 653 tgmtetafgsayKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 731
Cdd:cd14917 539 ------------KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRI 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 732 CRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14917 607 CRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-792 |
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: 689.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 181 GAGKTENTKKVIQYLAHVASSHKGRKDHN--IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKAD-- 574
Cdd:cd14918 402 EYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqraSFYDSVSGlheppvdrivgldqvtg 654
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF----------STYASAEA----------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 655 mtETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd14918 532 --DSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 735 GFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14918 610 GFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 687.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK 572
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrASFYDSVSGlheppvdrivgld 650
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF---------STYASADTG------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 651 qvtgmtETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 730
Cdd:cd14916 534 ------DSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIR 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 731 ICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14916 608 ICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-792 |
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: 686.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKA 573
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvSGLHeppvdrivgldq 651
Cdd:cd14912 478 EahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF----------------SGAQ------------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 652 vTGMTETAFGSAYK--TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 728
Cdd:cd14912 530 -TAEGASAGGGAKKggKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 729 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14912 609 IRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-792 |
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: 682.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHN---IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKA 573
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRASFYDSVSGlheppvdrivgldq 651
Cdd:cd14923 477 EahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKGG-------------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 652 vtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 731
Cdd:cd14923 543 -------------KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRI 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 732 CRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14923 610 CRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-792 |
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: 681.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK- 572
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKv 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvSGlheppvdrivgldQ 651
Cdd:cd14910 478 eAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF----------------SG-------------A 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 652 VTGMTETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 730
Cdd:cd14910 529 AAAEAEEGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIR 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 731 ICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14910 609 ICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-792 |
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: 670.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEaasgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK 572
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvSGLHeppvdrivgld 650
Cdd:cd14915 477 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLF----------------SGGQ----------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 651 qvTGMTETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 729
Cdd:cd14915 530 --TAEAEGGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGI 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 730 RICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14915 608 RICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-792 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 643.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 337 GFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 496 QEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADF 575
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiqrasfydsvsglhEPPVDRIVGLDQVTGM 655
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT-------------------YPDLLALTGLSISLGG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 656 TETAFGsaykTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 735
Cdd:cd14883 530 DTTSRG----TSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEG 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 736 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14883 605 FPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-792 |
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: 642.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 499 YQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlkDKAdFCII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER---GGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELwkdeiqtiqrasfYDSVSGLHeppvdrivglDQVTGMTET 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQL-------------FASKMLDA----------SRKALPLTK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 659 AFGSAyktkkGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd01383 520 ASGSD-----SQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPT 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 739 RIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01383 595 RMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-792 |
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: 641.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER-----VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 339 SHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---RDYVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 496 QEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQKPRQLKD--K 572
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppvdrivgldqv 652
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDL--------------------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 653 tgmtetafgsaykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd01378 526 -------------DSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVR 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 733 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01378 593 RAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-792 |
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: 608.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDK 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppvdrivgldqv 652
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM--------------------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 653 tgMTETAFGSAyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd01381 520 --GSETRKKSP---------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIR 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 733 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01381 589 KAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-792 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 603.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVA--SSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGgrAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDNFQETMEAM 333
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGRD-YVQ 409
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIVTPDgIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRql 569
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvsglhePPVDRivgl 649
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF---------------------PPLPR---- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 650 dqvtgmteTAFGSAYKtkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 729
Cdd:cd01384 521 --------EGTSSSSK-----FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 730 RICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 792
Cdd:cd01384 588 RISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-792 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 572.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV-GRDYVQKAQT 413
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKA 573
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvsglhePPVDrivgLDQVT 653
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF---------------------PPSE----GDQKT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 654 GMTetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14872 522 SKV----------------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 734 QGFPNRIVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14872 586 TGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-792 |
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: 570.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQETMEAMHIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRAILTPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 486 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 566 PRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiqrasfydsvsg 637
Cdd:cd01382 450 PRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESS--------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 638 lheppvdrivgldqvtgmTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVL 717
Cdd:cd01382 515 ------------------TNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQIL 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 718 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01382 577 SQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-792 |
8.11e-174 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 545.14 E-value: 8.11e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGeaaseaieqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 244 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 324 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 401
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 402 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 481
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 482 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQ--- 555
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAsfg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 556 ----------EQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdeiQT 625
Cdd:cd14890 477 rksgsggtrrGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------RS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 626 IQRASfydsvsglheppvdrivgldqvtgmtetafgsayktkkgmfrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHE 705
Cdd:cd14890 544 IREVS-------------------------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNET 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 706 KRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIG 785
Cdd:cd14890 581 KAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIG 655
|
....*..
gi 1039738673 786 QSKIFFR 792
Cdd:cd14890 656 SSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-792 |
1.52e-173 |
|
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: 543.96 E-value: 1.52e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHkgrkdhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlkDKAD 574
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRAsfydsvsglheppvdrivgldqvtg 654
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKA------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 655 mTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd01387 521 -PPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 735 GFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 792
Cdd:cd01387 600 GYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-792 |
1.54e-171 |
|
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: 539.66 E-value: 1.54e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLahVASSHKGrkdHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG--SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrQLKD 571
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 572 KAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL----------WKdeiqtIQRAsFYDSVSGLHEP 641
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWA-----VLRA-FFRAMAAFREA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 642 PVDRIVGLDQVTGM----TETAFGSAYKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVL 717
Cdd:cd01385 542 GRRRAQRTAGHSLTlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 718 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-792 |
4.09e-168 |
|
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: 529.35 E-value: 4.09e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLsgAGEHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGSHSKFQK----PRqlK 570
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR--T 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 571 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiQRASFYDSVSglheppvdrivgld 650
Cdd:cd14903 461 SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK------EKVESPAAAS-------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 651 qvtgMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 730
Cdd:cd14903 521 ----TSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIR 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 731 ICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 792
Cdd:cd14903 597 ISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-790 |
6.52e-166 |
|
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: 523.20 E-value: 6.52e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 249 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 485 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 561 SKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdeiqtiqrasfydsvsglhe 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 641 ppvdrivgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQL 720
Cdd:cd14901 531 --------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQL 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 721 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 790
Cdd:cd14901 579 RCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-754 |
1.02e-163 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 517.71 E-value: 1.02e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVT---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 254 -----GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP------------ 316
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 317 ------------IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL--- 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 382 CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 542 PKATDKTFVEKLVQEQGSHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVaelwkd 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI------ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 622 eiqtiqrasfydsvSGLHEPPVDRIVGLdqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCII 701
Cdd:cd14888 544 --------------SNLFSAYLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIK 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 702 PNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 754
Cdd:cd14888 595 PNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-792 |
8.78e-163 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 514.34 E-value: 8.78e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 337 GFSHEEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR-DYVQKAQTKE 415
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDkaD 574
Cdd:cd14873 394 EQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--N 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiqrasfYDSVSGLHEPPvdrivgldqvtg 654
Cdd:cd14873 468 FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE-----------HVSSRNNQDTL------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 655 mtetafGSAYKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd14873 525 ------KCGSKHRRP---TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 735 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14873 596 GYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-792 |
3.48e-161 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 509.51 E-value: 3.48e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVAsshkgrKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD--KDNFQETM 330
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNSgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA-LTSHSVVTRg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 484 QQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEKLvqEQGSHSK 562
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 563 FQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdeiqtiqrasfydsvsglhepp 642
Cdd:cd01379 463 YYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 643 vdrivgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 722
Cdd:cd01379 517 ------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRY 566
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 723 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 792
Cdd:cd01379 567 TGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-792 |
3.66e-157 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 498.45 E-value: 3.66e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASShkgrkdhnIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD-------KDNFQETM 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 487 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 567 rqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiqrasfydsvsglheppvdri 646
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 647 vgldqvtgmtetafgsayktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 726
Cdd:cd14897 522 -----------------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLM 572
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 727 EGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 792
Cdd:cd14897 573 EIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-792 |
2.82e-156 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 496.97 E-value: 2.82e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 172 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 403 VGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFELNSFE 472
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KATDKTFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 552 KLVQEQ-GSHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdeiqtiqras 630
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 631 fydsvsglheppvdrivgldqvtgmtetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGK 710
Cdd:cd14892 536 ----------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGG 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 711 LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRI 784
Cdd:cd14892 569 FSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQL 648
|
....*...
gi 1039738673 785 GQSKIFFR 792
Cdd:cd14892 649 GRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-792 |
1.41e-145 |
|
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: 467.46 E-value: 1.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-----KDNFQET 329
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRevqywKKKYDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 330 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd14889 227 CNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT-LTCTVTFTRg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 484 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 563
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 564 QKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiQTIQRASFYDSVSGLhePPV 643
Cdd:cd14889 461 GKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT---ATRSRTGTLMPRAKL--PQA 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 644 drivgldqvtgmTETAFGSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 723
Cdd:cd14889 534 ------------GSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYN 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 724 GVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 792
Cdd:cd14889 596 GLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-752 |
3.23e-145 |
|
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: 465.16 E-value: 3.23e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHV------ASSHKGRKDHNIPGelerQLLQANPILESFGNAKTVKND 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 238 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlksdlllegfnnyrflsngyipi 317
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 318 pGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLGMNVM 390
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 391 EFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEIF 466
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 467 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATD 546
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 547 KTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNmdplndnvatllhqssdrfvaelwKDEiqti 626
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKN------------------------KDV---- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 627 qrasfydsvsgLHEPPVDrivgldqvtgmtetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEK 706
Cdd:cd14900 502 -----------LHQEAVD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLC 544
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039738673 707 RAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 752
Cdd:cd14900 545 KAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-755 |
4.33e-143 |
|
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: 460.65 E-value: 4.33e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE-----------LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 239 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE----GFNNYRFLSNG 313
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 314 YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 391
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 392 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 464
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 465 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 543 KATDKTFVEKLVQEQGSHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDE 622
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 623 IQTIQRASFYDSVSglheppvdrivgldqvtgmtetafgsaYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIP 702
Cdd:cd14907 557 DGSQQQNQSKQKKS---------------------------QKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKP 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 703 NHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 755
Cdd:cd14907 606 NEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-792 |
1.54e-139 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 449.88 E-value: 1.54e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 172 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKDHNI--------PGELERQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 242 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 319
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 320 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 394
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 395 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 472
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 552
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 553 LVQEQGSHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSsdrfvaelwkdeiqtiqrASF 631
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS------------------AKF 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 632 YDSVSGLheppVDrivgldqvtgmtetafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKL 711
Cdd:cd14891 531 SDQMQEL----VD-------------------------------------------TLEATRCNFIRCIKPNAAMKVGVF 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 712 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIF 790
Cdd:cd14891 564 DNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVF 643
|
..
gi 1039738673 791 FR 792
Cdd:cd14891 644 FR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-792 |
1.33e-135 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 438.83 E-value: 1.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL-----RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-GRDYVQKAQTK 414
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 494 LEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlkDKA 573
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiQRAsfyDSVSGLHEPPVdrivgldqvt 653
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF-------QEA---EPQYGLGQGKP---------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 654 gmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14896 526 -------------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 734 QGFPNRIVFQEFRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14896 587 EGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-792 |
7.96e-135 |
|
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: 437.07 E-value: 7.96e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 496 QEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQlkDK 572
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvsglheppvdrivglDQV 652
Cdd:cd14904 466 TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF------------------------------GSS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 653 TGMTETAFGSAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14904 516 EAPSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRIT 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 733 RQGFPNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 792
Cdd:cd14904 595 RSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-792 |
4.71e-133 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 433.18 E-value: 4.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE---LERQLLQANPILESFGNAKTVKNDNSSRFGKF 245
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 246 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--------HLKSDLLLEGFNNYRFLSNGYIPI 317
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 318 PGQ-QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLGMNVMEFT 393
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 394 RAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIFELNSF 471
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 472 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFV 550
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 551 EKLV--------QEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNmdplndnvatllhqssdrfvaelwKD 621
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKN------------------------KD 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 622 EIQtiqrasfydsvsglheppvdrivgldqvtgmtetafgsayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCII 701
Cdd:cd14908 533 EIP----------------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIK 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 702 PNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDG 764
Cdd:cd14908 572 PNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCK 650
|
730 740 750
....*....|....*....|....*....|..
gi 1039738673 765 KQACERMIRALELDPNL----YRIGQSKIFFR 792
Cdd:cd14908 651 DLVKGVLSPAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-754 |
5.84e-131 |
|
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: 428.54 E-value: 5.84e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 169 REDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsNGYIP----IPGQQDK 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 324 DN--FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAILT 398
Cdd:cd14902 240 YAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 399 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEIFELNS 470
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 471 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFV 550
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 551 EKLVQEQGSHSKFqkprqlkdkadfCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdeiqtiqras 630
Cdd:cd14902 477 TKFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN------------------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 631 fydsvsglhepPVDRIVGLDQVTGMTETAFGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRA 708
Cdd:cd14902 527 -----------EVVVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKP 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039738673 709 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 754
Cdd:cd14902 596 GIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-753 |
3.56e-130 |
|
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: 425.91 E-value: 3.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGElerQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 242 FGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNG- 313
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 314 -YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD---------------QASMPENTV 377
Cdd:cd14895 232 cYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 378 AQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK------ 448
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 449 ----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 524
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 525 pANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDN 602
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 603 VATLLHQSSDRFVAELWKdeiqtiqrasfydsvsglhepPVDRIVGLDQVTGMTETAFGSAYKTKKGmfrtVGQLYKESL 682
Cdd:cd14895 547 LFSVLGKTSDAHLRELFE---------------------FFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQL 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 683 TKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 753
Cdd:cd14895 602 ASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-845 |
1.36e-129 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 428.29 E-value: 1.36e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 336 MGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 570
Cdd:PTZ00014 500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDS 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 571 DKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiQTIQRAsfydsvsglheppvdrivgld 650
Cdd:PTZ00014 577 NK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEG--VEVEKG--------------------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 651 qvtgmtetafgsayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 730
Cdd:PTZ00014 633 --------------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQ 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 731 ICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKI 807
Cdd:PTZ00014 697 LRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAW 776
|
730 740 750
....*....|....*....|....*....|....*...
gi 1039738673 808 TDIIIFFQAVCRGYLARKAFAKKqqqlsaLKVLQRNCA 845
Cdd:PTZ00014 777 EPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-790 |
1.30e-125 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 410.92 E-value: 1.30e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 338 FSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 412
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 413 TKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFqKPRQLKD 571
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKVDS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 572 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppvdrivgldq 651
Cdd:cd14876 468 NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVE-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 652 vtgmtetafgsAYKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 731
Cdd:cd14876 522 -----------KGKIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQL 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 732 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 790
Cdd:cd14876 589 RQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-792 |
7.65e-122 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 401.69 E-value: 7.65e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQA-NPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV--------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI------------LTPRIKV 403
Cdd:cd01386 233 LGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 404 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN------SFEQLCIN 477
Cdd:cd01386 313 SPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrgaTFEDLCHN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALLDEECWFPKAT 545
Cdd:cd01386 392 YAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEALYPGSS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 546 DKTFVEKLVQEQG--SHSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQSSDRFVAelw 619
Cdd:cd01386 472 DDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKETAA--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 620 kdeiqtiqrasfydsvsglheppvdrivgldqvtgmtetafgsayKTKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRC 699
Cdd:cd01386 549 ---------------------------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHC 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 700 IIPNH--EKRAGK----------LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----M 762
Cdd:cd01386 580 LLPQHnaGKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevA 659
|
730 740 750
....*....|....*....|....*....|
gi 1039738673 763 DGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd01386 660 DERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-754 |
7.05e-119 |
|
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: 391.91 E-value: 7.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKDNFQETMEAMH 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRIKVGRDYV--Q 409
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 490 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 569
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiQRASFYDSVSGLHEPPVdrivgl 649
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN----PEEKTQEEPSGQSRAPV------ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 650 dqvtgmtetafgsayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 729
Cdd:cd14880 544 ----------------------LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETI 601
|
650 660
....*....|....*....|....*
gi 1039738673 730 RICRQGFPNRIVFQEFRQRYEILTP 754
Cdd:cd14880 602 HISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-755 |
4.94e-116 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 385.87 E-value: 4.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 177 TGESGAGKTENTKKVIQYLAHVASS--HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 255 YIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLSGAGehlKSDLLLEGFNN----YRFL--------------SNGY 314
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissfksqsSNKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 315 IPIPGQQDKD-NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVM 390
Cdd:cd14906 238 SNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 391 EFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQGASFIGIL 458
Cdd:cd14906 318 VFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 459 DIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEE 538
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 539 CWFPKATDKTFVEKLVQEQgsHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL 618
Cdd:cd14906 475 CIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 619 WKdeiqtiqrasfydsvsglheppvdrivglDQVTGMTETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVR 698
Cdd:cd14906 553 FQ-----------------------------QQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 699 CIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 755
Cdd:cd14906 598 CIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-792 |
2.69e-111 |
|
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: 370.68 E-value: 2.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 176 CTGESGAGKTENTKKVIQYLAHVASSHKGR-KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD-VT 253
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 254 GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPGQ--QDKDNF 326
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILtprIKVGRD 406
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 407 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQ 564
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPyFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 565 KPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRAsfydsvsglheppvd 644
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK--------------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 645 rivgldqvtgmtetafgsayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 724
Cdd:cd14875 538 ---------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAG 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 725 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 792
Cdd:cd14875 591 VLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-792 |
9.82e-111 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 368.45 E-value: 9.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 173 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETME 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 332 AMHIMgFSHEEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILTPRIKVGRDYV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 409 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINYANERLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECwfpkatdktfvekLVQeQGSHSKFQK 565
Cdd:cd14886 388 YFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQC-------------LIQ-TGSSEKFTS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 566 PRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfyds 634
Cdd:cd14886 451 SCKSKIKNNsfipgkgsqcnFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 635 vsglheppvdrivgLDQVTGMTetafgsayktkKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPH 714
Cdd:cd14886 518 --------------IPNEDGNM-----------KGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETK 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 715 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14886 571 SVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-749 |
1.48e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 355.56 E-value: 1.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 168 DREDQSILCTGESGAGKTENTKKVIQYLA-------HVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 239 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-----AGEHLKSDLLLEGFNNYRFLSN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 313 GYIPI--PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ--------- 379
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 380 -KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT----------- 447
Cdd:cd14899 321 tKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 448 ---KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIER 524
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 525 paNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 601
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 602 NVATLLHQSSDRFvaelwkdeIQTIQRASFYDSVSGLHEppVDRIVGLDQVTGMTETAFGSayktkkgmfrtVGQLYKES 681
Cdd:cd14899 558 SAAQLLAGSSNPL--------IQALAAGSNDEDANGDSE--LDGFGGRTRRRAKSAIAAVS-----------VGTQFKIQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 682 LTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 749
Cdd:cd14899 617 LNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-792 |
4.11e-96 |
|
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: 328.53 E-value: 4.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 251 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFlsngyipipgqqDKDNFQETM 330
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------DLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 331 EAMHIMGFSHEEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL-------GMNVMEFTRA 395
Cdd:cd14887 225 KTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclssGLKVTEASRK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 396 ILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR------ 449
Cdd:cd14887 302 HLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesds 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 450 -------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQP 517
Cdd:cd14887 382 dedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 518 CIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGSHSKFQK--PRQ 568
Cdd:cd14887 462 ASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPAL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 569 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVaelwkdeiqtiqrasfydsvsglheppvdRIVG 648
Cdd:cd14887 542 SRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT-----------------------------RLVG 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 649 LDQVTGMtetafgSAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 728
Cdd:cd14887 592 SKKNSGV------RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDL 662
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 729 IRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14887 663 LRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-791 |
3.81e-95 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 322.96 E-value: 3.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 245 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGY--IPIPGQ 320
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 321 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMNVMEFtRAIL 397
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 398 TPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIF---ELN 469
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 470 SFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALLDEEC-WFPK 543
Cdd:cd14879 386 SLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDDQTrRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 544 ATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSSDrFVAelwk 620
Cdd:cd14879 458 KTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN---- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 621 deiqtiqrasfydsvsglheppvdrivgldqvtgmtetafgsayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCI 700
Cdd:cd14879 523 -------------------------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCI 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 701 IPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPN 780
Cdd:cd14879 553 RPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGR 626
|
730
....*....|.
gi 1039738673 781 LYRIGQSKIFF 791
Cdd:cd14879 627 DYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-756 |
2.34e-94 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 318.38 E-value: 2.34e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQETMEAMHIMGFS 339
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 340 HeeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 419
Cdd:cd14898 220 N--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 420 AVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 499
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 500 QREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgshSKFQKPRqLKDKADFCII- 578
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-INTKARDKIKv 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 579 -HYAGKVDYKADEWLMKNMDplndnvatllhqssdrfvaelwkdeiqtiqrasfydsvsglheppvdrivgldqvtGMTE 657
Cdd:cd14898 440 sHYAGDVEYDLRDFLDKNRE--------------------------------------------------------KGQL 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 658 TAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 737
Cdd:cd14898 464 LIFKNLLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFP 543
|
650
....*....|....*....
gi 1039738673 738 NRIVFQEFRQRYEILTPNA 756
Cdd:cd14898 544 QEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-792 |
1.21e-91 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 313.29 E-value: 1.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQQDKDNFQETM 330
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 488 NHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATDKTFVEKL--V 554
Cdd:cd14878 393 NEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLqsL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 555 QEQGSHSKFQKPRQ-------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTI 626
Cdd:cd14878 460 LESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVTI 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 627 qrASfydsvsglheppvdrivgldqvtgmtetafgsayktkkgmfrtvgQLYKeSLTKLMATLRNTNPNFVRCIIPNHEK 706
Cdd:cd14878 540 --AS---------------------------------------------QLRK-SLADIIGKLQKCTPHFIHCIKPNNSK 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 707 RAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRI 784
Cdd:cd14878 572 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQM 648
|
....*...
gi 1039738673 785 GQSKIFFR 792
Cdd:cd14878 649 GVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-792 |
1.97e-87 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 300.39 E-value: 1.97e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAhvasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 339 sHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 494 LEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKa 573
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrASFYDSVsglheppvdrivgldqvt 653
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-------VEVSESL------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 654 gmtetafgsayktkkGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIcR 733
Cdd:cd14937 516 ---------------GRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-S 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 734 QGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 792
Cdd:cd14937 580 FFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-744 |
1.07e-79 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 279.10 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT---ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 251 D---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-AGEHLKSDLLLEGFNNYRFL---------- 310
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 311 ----------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKkerntdqasmpentvaqK 380
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------A 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 381 LCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 453 ---SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpanpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 530 gVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGSHSK-FQKPR--------QLKDKADFCIIHYAGKVDYKADE 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 591 WLMKNMDPLNDNVATLLHQSSDRFVAElwkdeiqtiqrasfydsvsglheppvdrivgldqvtgmtetafgSAYKTKKGM 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE--------------------------------------------ANNGGNKGN 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 671 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 744
Cdd:cd14884 566 FLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-779 |
1.59e-75 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 265.05 E-value: 1.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 173 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhnipGELE----RQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG-----------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 249 NFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 326
Cdd:cd14881 139 QV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 327 QETMEAMHIMGFsheEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiLTPRIK- 402
Cdd:cd14881 218 QAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-LTTRTHn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 403 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFELNSFEQL 474
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 475 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKTFVEKL 553
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 554 VQEQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdeiqtiqrasfyd 633
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 634 svsglheppvdrivgldqvtgmteTAFGsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDP 713
Cdd:cd14881 499 ------------------------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDR 545
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 714 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 779
Cdd:cd14881 546 GTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-792 |
3.44e-72 |
|
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: 256.56 E-value: 3.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnipgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY---------ILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAqtkeq 416
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 417 adfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14905 304 -----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 497 EEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF-QKPRQlkdkad 574
Cdd:cd14905 377 REYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVaeLWKDEIQTIQRA-----SFYDSVSGLHEPPVDRIVGL 649
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL--FSRDGVFNINATvaelnQMFDAKNTAKKSPLSIVKVL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 650 --------DQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKLDPHLVLDQ 719
Cdd:cd14905 522 lscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQ 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 720 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIFFR 792
Cdd:cd14905 602 IKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-757 |
6.07e-70 |
|
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: 248.63 E-value: 6.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgelerqllQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSS----------AIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 258 GANIE-TYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKVGrdyvqKAQT 413
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSEDG-----TTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 494 LEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlKDK 572
Cdd:cd14874 373 DQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KER 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQrasfydsvsglheppvDRIVgldqv 652
Cdd:cd14874 450 LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTS----------------DMIV----- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 653 tgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14874 509 --------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFR 568
|
650 660
....*....|....*....|....*
gi 1039738673 733 RQGFPNRIVFQEFRQRYEILTPNAI 757
Cdd:cd14874 569 IKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-791 |
2.93e-67 |
|
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: 243.72 E-value: 2.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 172 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgEH---LKSDLLL-EGFNNYRFLSNGyIPIPGQ--Q 321
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPLATNfaL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 322 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------LGMNVME 391
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilLAAKLLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 392 FTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG----ASF 454
Cdd:cd14893 322 VEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 455 IGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIDLIERP 525
Cdd:cd14893 402 VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEDK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 526 anPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD------------FCIIHYAGKVDYKADEWLM 593
Cdd:cd14893 482 --PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 594 KNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRASFYDSVSGlheppvdrivgldqvTGMTETAFG----SAYKTKKG 669
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEE---------------RGSTSSKFRksasSARESKNI 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 670 MFRTVGQLYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 749
Cdd:cd14893 625 TDSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1039738673 750 eiltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 791
Cdd:cd14893 704 ---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-752 |
2.87e-63 |
|
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: 229.24 E-value: 2.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 180 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERqllqANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG----------QQDKDN 325
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyrrddpEGNVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14882 229 YKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNSFEQLCINYTN 480
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 481 EKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDKTFVEKLVQEQ 557
Cdd:cd14882 384 EQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 558 gsHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiqrasfydsvsg 637
Cdd:cd14882 456 --HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNS--------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 638 lheppvdrivgldQVTGMtetafgsayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLDPH 714
Cdd:cd14882 516 -------------QVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSE 567
|
650 660 670
....*....|....*....|....*....|....*...
gi 1039738673 715 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 752
Cdd:cd14882 568 VVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
1.03e-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: 1.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 200 SSHKGRKDHN-------IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01363 81 FNGINKGETEgwvylteITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-790 |
4.81e-58 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 215.47 E-value: 4.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 179 ESGAGKTENTKKVIQYLAHVA----------SSHKGRKDHNIP-----GELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrrlptnlNDQEEDNIHNEEntdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 244 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 324 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 378 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 455 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 535 LDEECWFPKATDKTFVEKLVQEQGSHSKF--QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 612
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 613 RFVAELwkdeiqtiqrASFYDSVSGLHEPPVDRIVGLDQVTGMtetaFGSAYKTKKGMFRTvgqLYKESLTKLMATLRNT 692
Cdd:cd14938 558 EYMRQF----------CMFYNYDNSGNIVEEKRRYSIQSALKL----FKRRYDTKNQMAVS---LLRNNLTELEKLQETT 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 693 NPNFVRCIIPNHEKRA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERM 771
Cdd:cd14938 621 FCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEAL 692
|
730
....*....|....*....
gi 1039738673 772 IRALELDPNLYRIGQSKIF 790
Cdd:cd14938 693 IKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1026-1882 |
1.64e-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: 148.28 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1026 EDRIAECSSQL------AEEEEKAKNL-AKIRNKQ-EVMISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQA 1097
Cdd:TIGR02168 192 EDILNELERQLkslerqAEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1098 QVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1177
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1178 DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATaLEELSEQLEQAKRFKANLEKNKQGLETDNkel 1257
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI--- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1258 acevkvlqqvkaeSEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDaaglESQ 1337
Cdd:TIGR02168 424 -------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1338 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVdddlgTIESLEEAKKk 1417
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-----VVENLNAAKK- 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1418 llkDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAeekGISARYAEERDRAEA 1497
Cdd:TIGR02168 561 ---AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1498 EAREKETKAL---------------SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1562
Cdd:TIGR02168 635 LELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1563 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQnEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1642
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL-EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1643 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1722
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1723 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSA-- 1800
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtl 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1801 ------AQKSDNARQQLERQNKELKAKLQELeGAVKSKFKATISALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEK 1870
Cdd:TIGR02168 954 eeaealENKIEDDEEEARRRLKRLENKIKEL-GPVNLAAIEEYEELKERYDFLTAQKEdlTEAKEtlEEAIEEIDREARE 1032
|
890
....*....|..
gi 1039738673 1871 KLKEIFMQVEDE 1882
Cdd:TIGR02168 1033 RFKDTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1152-1907 |
6.65e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 146.35 E-value: 6.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1152 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ----QELRTKREQE--------VAELKKALE--DETKNHEAQ 1214
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEdilNELERQLKSLERQaekaERYKELKAELrelelallVLRLEELREelEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1215 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDR 1294
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1295 LRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ-------EETRQKLNLSSRIRQLEEEKN 1367
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1368 SLQE-----QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKkkllkdvEALSQRLEEKVLAYDKLEKT 1442
Cdd:TIGR02168 411 RLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL-------EELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1443 KNRLQQELDDLTVDLDHQRQI---VSNLEKKQKKF--------DQLLAEEKGISARYAEERDRAEAEAREKETKAL---- 1507
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaia 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1508 SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL--- 1584
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrp 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1585 ---------------------RLEVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1642
Cdd:TIGR02168 644 gyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1643 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1722
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1723 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNdrfrkttLQVDTLNTELAAERSAAQ 1802
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1803 KSDNARQQLERQNKELKAKLQELEGAVKSKFKAtISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1882
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESK-RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
810 820
....*....|....*....|....*.
gi 1039738673 1883 -RRHADQYKEQMEKANARMKQLKRQL 1907
Cdd:TIGR02168 956 aEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1026-1879 |
1.32e-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: 132.50 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1026 EDRIAECSSQLAEEEEKAKNLAKIRNKQEvMISDLEERLKKEE-----KTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1100
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1101 ELKVQLTKKEEELQGALARGDDETLHKNNALKVA-RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDT 1179
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1180 LDTTAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELS---EQLEQAKRFKANLEKNKQGLETDNKE 1256
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1257 LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1336
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1337 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearknlEKQVLALQSQLADTKKK--VDDDLGTIESLEEA 1414
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG----------ERYATAIEVAAGNRLNNvvVEDDAVAKEAIELL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1415 KKKLL-----------KDVEALSQRLEEKV---LAYDKLE---KTKNRLQQELDDLTV--DLDHQRQIVSN--------- 1466
Cdd:TIGR02169 568 KRRKAgratflplnkmRDERRDLSILSEDGvigFAVDLVEfdpKYEPAFKYVFGDTLVveDIEAARRLMGKyrmvtlege 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1467 -LEKKQKKFDQLLAEEKGISaRYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG 1545
Cdd:TIGR02169 648 lFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1546 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQTRDEQNEEKKRLLLKQVRELEAE 1625
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1626 LEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKS 1705
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1706 LEAEILQLQEELAsserarrHAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttl 1785
Cdd:TIGR02169 873 LEAALRDLESRLG-------DLKKERDELEAQL-------RELERKIEELEAQIEKKRKRLSELKAKLEALEEE------ 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1786 qvdtlNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE--GAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1863
Cdd:TIGR02169 933 -----LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
890
....*....|....*.
gi 1039738673 1864 LVRRTEKKLKEIFMQV 1879
Cdd:TIGR02169 1008 RIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1206-1955 |
4.36e-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: 130.56 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1206 DETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA--NLEKNKQG--LETDNKELACEVKVLQQVKAESEHKRKKLDAQ 1281
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1282 VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQ 1361
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1362 LEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK 1441
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1442 TKNRLQQELDDLTVDLDHQR--QIVSNLEKKQKKFDQLLAEEKGISARYAE---ERDRAEAEAREKETKALSLARALEEA 1516
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1517 LEAKEEFERQNKQ----------------------------LRADMEDL-MSSKDDVGKNVHELEKS---KRALEQQVEE 1564
Cdd:TIGR02168 502 EGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvVENLNAAKKAIAFLKQNelgRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1565 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTR----------DEQNEEKKRLLLkqvRELEAELEDER---- 1630
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRP---GYRIVTLDGDLvrpg 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1631 ----KQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1706
Cdd:TIGR02168 659 gvitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1707 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeleeEQSNMELLNDRFRKTTLQ 1786
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1787 VDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSkFKATISALEAKIGQLEEQLEQEAKERAAANKLVR 1866
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1867 RTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA-------TEANEGL 1938
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAealenkiEDDEEEA 970
|
810
....*....|....*..
gi 1039738673 1939 SREVSTLKNRLRRGGPI 1955
Cdd:TIGR02168 971 RRRLKRLENKIKELGPV 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1719 |
1.42e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.90 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1075 EKAKRKLDGETTDL---QDQIAELQAQVDELKVQ---------LTKKEEELQGALargddetlhknnALKVARELQAQIA 1142
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPLERQaekaeryreLKEELKELEAEL------------LLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1143 ELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknheaqiQDMRQRH 1222
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------EERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1223 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1302
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1303 ANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKN 1382
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1383 LEKQVLALQSQLADtkkkvdddlgtieslEEAKKKLLKDVEALSQRLEEKVLAYDKLEKtKNRLQQELDDLTVDldhqrq 1462
Cdd:COG1196 475 LEAALAELLEELAE---------------AAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGV------ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1463 ivsnlekkQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD 1542
Cdd:COG1196 533 --------EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1543 DVgKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRLLLKQVREL 1622
Cdd:COG1196 605 AS-DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT-LEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1623 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEiFAQSKESEKK 1702
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEPPD 761
|
650
....*....|....*..
gi 1039738673 1703 LKSLEAEILQLQEELAS 1719
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1692 |
8.28e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 126.71 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 870 RQEEELQakdeeLLKVKEKQTKVEGELEEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARLAAK-KQELEEILHDL 948
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALLVLrLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 949 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1028
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1029 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1108
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1109 KEEELQGALARgdDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQE 1188
Cdd:TIGR02168 405 LEARLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1189 LRTKREQEvaelkkaleDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNK-ELACE------- 1260
Cdd:TIGR02168 477 LDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrl 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1261 ----VKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLqnelDNVSTLLEEAEKKGIKFAKDAAGLES 1336
Cdd:TIGR02168 548 qavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI----EGFLGVAKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1337 Q------LQDTQELLQEETRQ---------------------------KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL 1383
Cdd:TIGR02168 624 GvlvvddLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1384 EKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQi 1463
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1464 vsNLEKKQKKFDQLLAEEKGISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1540
Cdd:TIGR02168 783 --EIEELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1541 KDDVGKNVHELE-------KSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKR 1613
Cdd:TIGR02168 861 IEELEELIEELEseleallNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1614 LLLKQVREL-EAELEDERKQRALAVASKKKMEIDLKDLEAQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASR 1689
Cdd:TIGR02168 940 NLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
...
gi 1039738673 1690 DEI 1692
Cdd:TIGR02168 1020 EEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1188-1879 |
1.32e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1188 ELRTKREQevAELKkaLEdETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA------NLEKNKQGLETDNKELacEV 1261
Cdd:COG1196 169 KYKERKEE--AERK--LE-ATEENLERLEDILGELERQLEPLERQAEKAERYRElkeelkELEAELLLLKLRELEA--EL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1262 KVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDT 1341
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1342 QELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKD 1421
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1422 VEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEARE 1501
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1502 KETKALSLARaleealeakeefERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRaLEQQVEEMRTQLEELEDELQATED 1581
Cdd:COG1196 479 LAELLEELAE------------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1582 AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR 1661
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1662 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANS 1741
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1742 ASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKsdnARQQLERQNKEL--- 1818
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELERLEREIEALgpv 782
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1819 --KAkLQELEgavkskfkatisALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEKKLKEIFMQV 1879
Cdd:COG1196 783 nlLA-IEEYE------------ELEERYDFLSEQREdlEEAREtlEEAIEEIDRETRERFLETFDAV 836
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1713 |
2.54e-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: 124.78 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 870 RQEEELQAKDEELLKVKEKQtkVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 949
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 950 SRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRI 1029
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1030 AECssqlaeeeekaknlakirnkqevmisdleerlkkeektRQELEKAKRKLDgettDLQDQIAELQAQVDELKVQLtkk 1109
Cdd:TIGR02168 375 EEL--------------------------------------EEQLETLRSKVA----QLELQIASLNNEIERLEARL--- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1110 eEELQGALARGDDETLHKNNALKvarelQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQEL 1189
Cdd:TIGR02168 410 -ERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1190 RTKREQevaelkkalEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNK-ELACE-------- 1260
Cdd:TIGR02168 478 DAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrlq 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1261 ---VKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAnklqNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1337
Cdd:TIGR02168 549 avvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL----KNIEGFLGVAKDLVKFDPKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1338 LQDTQELLQE-ETRQKLNLSSRIRQLEEEK-----------NSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDL 1405
Cdd:TIGR02168 625 VLVVDDLDNAlELAKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1406 GTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL-DHQRQIVSNLEKKQKKFDQLLAEEKGI 1484
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1485 sARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEE 1564
Cdd:TIGR02168 785 -EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1565 MRTQLEELEDELQATEDAKLRLEVNMQAmkAQFERDLQTRDEQNEEKKRlllkqvRELEAELEDERKQralavaskkkme 1644
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALAL--LRSELEELSEELRELESKR------SELRRELEELREK------------ 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1645 idLKDLEAQIEAANKARDEVIKQLRklqaqmKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1713
Cdd:TIGR02168 924 --LAQLELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1057-1938 |
3.26e-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: 118.25 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1057 ISDLEERLKKEEKTRQELEKAKRKLDgettdlqdqiaELQAQVDELKVQLTKKEEElqgalargddetlhKNNALKvare 1136
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEELEEVEENIE-----------RLDLIIDEKRQQLERLRRE--------------REKAER---- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1137 LQAQIAELQEDFESEKASR-NKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQI 1215
Cdd:TIGR02169 213 YQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKL-------TEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1216 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETdnkelacevkvlQQVKAESEhkRKKLDAQVQELHAKVSEGDRL 1295
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE------------RLAKLEAE--IDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1296 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1375
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKE-------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1376 EEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDdltv 1455
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA---- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1456 DLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEarEKETKALSLAraleealeakeeferqnkqLRADME 1535
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA-------------------AGNRLN 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1536 DLMSSKDDVGKNVHELEKSK---RALEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMKAQFE-------RDlqTRD 1605
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafkyvfGD--TLV 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1606 EQNEEKKRLLLKQVR--ELEAELEDE--------RKQRALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1675
Cdd:TIGR02169 626 VEDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1676 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1755
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1756 EARIAQLEEELEEEQsnMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV------ 1829
Cdd:TIGR02169 785 EARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngk 862
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1830 KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRqLEE 1909
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKG 941
|
890 900
....*....|....*....|....*....
gi 1039738673 1910 AEEEATRANASRRKLQRELDDATEANEGL 1938
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1342-1907 |
1.64e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.42 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1342 QELLQEETRQKLNLSS-RIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1420
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1421 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1500
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1501 EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATE 1580
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------RLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1581 DAKLRLEvnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKA 1660
Cdd:COG1196 449 EEEAELE--------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1661 RdeVIKQLRKLQAQMKDYQRELEEARASR--------DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERD 1732
Cdd:COG1196 521 G--LAGAVAVLIGVEAAYEAALEAALAAAlqnivvedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1733 ELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLE 1812
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1813 RQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQ 1892
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 1039738673 1893 M---EKANARMKQLKRQL 1907
Cdd:COG1196 759 PpdlEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
865-1727 |
1.14e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.85 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 865 LLQVTRQEEELQAKDEEllkVKEKQTKVEGELEEMERkHQQLLEEKNILA--EQLQAETELFAEAEEMRARLAAKKQELE 942
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 943 EILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGarqKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEK 1022
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG---ELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1023 KLMEDRIAECSSQLAEEE-EKAKNLAKIRNKQEVM---ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQ 1098
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERkRRDKLTEEYAELKEELedlRAELEEVDKEFAETRDELKDYREKLE----KLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1099 VD---ELKVQLTKKEEELQGALARGDDetlhKNNALKVARE-LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1174
Cdd:TIGR02169 408 LDrlqEELQRLSEELADLNAAIAGIEA----KINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1175 ELE------DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALE----------------ELSEQ 1232
Cdd:TIGR02169 484 ELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1233 LEQAKRFKAN----LEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQN 1308
Cdd:TIGR02169 564 IELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF------GDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1309 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklNLSSRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVL 1388
Cdd:TIGR02169 638 KYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQSE-------LRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1389 ALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1468
Cdd:TIGR02169 706 ELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1469 KKQKKFDQLLAEEKGISARyaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNV 1548
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1549 HELEKSKRALEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqferDLQTRDEQNEEKKRLLLKQVRELEAELED 1628
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1629 ERKQRALAVASKKKMEIDLKDLEAQIeAANKARDEVIKQLRKLQAQMKDYQRELEE-------ARASRDEIFAQSKESEK 1701
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKE 993
|
890 900
....*....|....*....|....*.
gi 1039738673 1702 KLKSLEAEILQLQEELASSERARRHA 1727
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
828-1470 |
1.72e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 828 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRvftkvkplLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQL 906
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELE--------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 907 LEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdlesrveeeeeRNQILQNEKKKMQAHIQDLEEQLDEEEGA 986
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------------RLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 987 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK 1066
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1067 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQE 1146
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1147 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAL 1226
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1227 EELSEQLEQAKRFKANLeknkqGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKL 1306
Cdd:COG1196 586 AALAAALARGAIGAAVD-----LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1307 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQ 1386
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1387 VLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALsqrleEKV--LA---YDKLEKTKNRLQQELDDLTVDLDHQR 1461
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-----GPVnlLAieeYEELEERYDFLSEQREDLEEARETLE 815
|
....*....
gi 1039738673 1462 QIVSNLEKK 1470
Cdd:COG1196 816 EAIEEIDRE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
880-1761 |
1.75e-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: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 880 EELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlAAKKQELEEILHDLEsrVEEEEERN 959
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 960 QILQNEKKKMQAHIqdleeqldeeegARQKLQLEKVTAE--AKIKKMEEEVLLLEDQNSKFikeKKLMEDRIAECSSQLA 1037
Cdd:TIGR02169 233 EALERQKEAIERQL------------ASLEEELEKLTEEisELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1038 EEEEKAKNLAKIrnkqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1117
Cdd:TIGR02169 298 ELEAEIASLERS-------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1118 ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEV 1197
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE---AKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1198 AELKKAlEDETKNHEAQIQDMRQRH---ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLqqvkaesEHK 1274
Cdd:TIGR02169 448 LEIKKQ-EWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1275 RKKLDAQVQELhAKVSEGDRLRVELAekankLQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLN 1354
Cdd:TIGR02169 520 IQGVHGTVAQL-GSVGERYATAIEVA-----AGNRLNNVVVEDDAVAKEAIELLK-----RRKAGRATFLPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1355 LSSRIRqleeeknslqeqqeeeeearknlEKQVLALQSQLADTKKK-------VDDDLGTIESLEEAKKKL--------- 1418
Cdd:TIGR02169 589 DLSILS-----------------------EDGVIGFAVDLVEFDPKyepafkyVFGDTLVVEDIEAARRLMgkyrmvtle 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1419 ----------------LKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK----QKKF 1474
Cdd:TIGR02169 646 gelfeksgamtggsraPRGGILFSRSEPAELQRLrerlEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1475 DQLLAEEKGISARYAEERDRAEAEAREKETKALSLARaleeALEAKEEFERQNKQLRADMEDLMSSKDDVGknVHELEKS 1554
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE----LEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1555 KRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRA 1634
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1635 LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE------SEKKLKSLEA 1708
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQA 958
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1709 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1761
Cdd:TIGR02169 959 ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1127-1902 |
3.69e-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: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1127 KNNALKVARELQAQIAELQEDFESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALED 1206
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1207 ETKNHEAQiqdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD--NKELACEVKVLQQVKAESEHKR--------- 1275
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvDFEEASGKKIYEHDSMSTMHFRslgsaiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1276 -KKLDAQVQELHAKV-SEGDRLRVELAEKANK----LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ---LQDTQELLQ 1346
Cdd:pfam15921 226 lRELDTEISYLKGRIfPVEDQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1347 EETRQKLnlSSRIRQLEEeknslqeqqeeeeearknLEKQVLALQSQLADTKKKVDDdlgTIESLEeaKKKLLKDVEALS 1426
Cdd:pfam15921 306 EQARNQN--SMYMRQLSD------------------LESTVSQLRSELREAKRMYED---KIEELE--KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1427 QRLEEkvlayDKLEKTKNRLQQELDDLTVDLdHQRQIVSNLEKKQKKfdQLLAEEKGISARYAEERdraeaeaREKETKA 1506
Cdd:pfam15921 361 ARTER-----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNK--RLWDRDTGNSITIDHLR-------RELDDRN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1507 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1586
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1587 EVNMQAMKAqferdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKD-----LEAQIE-----A 1656
Cdd:pfam15921 506 QEKERAIEA-------TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDkvieiLRQQIEnmtqlV 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1657 ANKARDEVIKQLRK--LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1734
Cdd:pfam15921 579 GQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1735 ADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELLNDRFRKTTLQVDT----LNTELAAERSAAQKSDNARQQ 1810
Cdd:pfam15921 659 LNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKS 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1811 LERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERaaanKLVRRTEKKLKEIFMQVEDERRHADQYK 1890
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
810
....*....|..
gi 1039738673 1891 EQMEKANARMKQ 1902
Cdd:pfam15921 793 EVLRSQERRLKE 804
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-733 |
1.19e-23 |
|
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: 109.45 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 218 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHIFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 287 LLSGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHEEILSMLKVVS 351
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 352 SVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVEALA 425
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 426 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQqlfnh 489
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 490 tmfileQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKAT----------DKTFVEKLVQEQGS 559
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 560 HSKfQKPRQLKDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQtiqra 629
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ----- 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 630 sfydsvsglheppvdrivgLDQVTGMTETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAG 709
Cdd:cd14894 712 -------------------LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPS 771
|
570 580
....*....|....*....|....
gi 1039738673 710 KLDPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14894 772 LVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
867-1565 |
3.33e-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: 108.22 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 946
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 947 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ-----LEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1021
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieeLLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1022 KKLMEDRIAECSSQLAEEEEK----AKNLAKIRNKQEvMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI---AE 1094
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQAldaaERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1095 LQAQVDelkvqlTKKEEELQGALARGDD------ETLHKNNALKVA---------RELQAQIAELQEDFESEKASRNKAE 1159
Cdd:TIGR02168 535 YEAAIE------AALGGRLQAVVVENLNaakkaiAFLKQNELGRVTflpldsikgTEIQGNDREILKNIEGFLGVAKDLV 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1160 KQKRDLSEELEAL--KTELEDTLDTTAAQQEL-------------------------------RTKREQEVAELKKALEd 1206
Cdd:TIGR02168 609 KFDPKLRKALSYLlgGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIE- 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1207 ETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELH 1286
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1287 AKVSEGDRLRVELAEKANKLQNELDNVSTLLEEaekkgikfakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1366
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKA--------------LREALDELRAELTLLNEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1367 NSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL 1446
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1447 QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFER 1525
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1039738673 1526 QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1565
Cdd:TIGR02168 987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1152-1761 |
1.42e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1152 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ-------QELRTKREQEVAELKKALEDETKNHEAQIQDMRQR 1221
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEdilGELERQLEPLERQaekaeryRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1222 HATALEELSEQLEQAkrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1301
Cdd:COG1196 251 LEAELEELEAELAEL---EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1302 KANKLQNELDNVSTL----------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQE 1371
Cdd:COG1196 328 LEEELEELEEELEELeeeleeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1372 QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1451
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1452 DLTVDLDHQRQIVSNLEKKQK--KFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA----RALEEALEAKEEFER 1525
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnivVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1526 QNKQLRA------DMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER 1599
Cdd:COG1196 568 AAKAGRAtflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1600 DLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1679
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1680 RELEEARASRDEIFAQSK----ESEKKLKSLEAEILQLQEELASSERARRH-------AEQERDELADEIANSASGKSAL 1748
Cdd:COG1196 728 EQLEAEREELLEELLEEEelleEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDL 807
|
650
....*....|...
gi 1039738673 1749 LDEKRRLEARIAQ 1761
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 ... |
1335-1951 |
3.29e-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: 101.79 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1335 ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEeeeeARKNLEKQVLALQSQLADTKKKVDDDLGTIES---- 1410
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETELCAEAEEMRARLAARKQELEEILHELESrlee 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1411 -------LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEekg 1483
Cdd:pfam01576 87 eeersqqLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1484 isaryaeerdrAEAEAREKETKALSLARALEealeakeeferQNKQLRADMEDLMSSKDdvgKNVHELEKSKRALEQQVE 1563
Cdd:pfam01576 164 -----------FTSNLAEEEEKAKSLSKLKN-----------KHEAMISDLEERLKKEE---KGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1564 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKM 1643
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1644 EIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELE-EARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1722
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1723 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQ 1802
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1803 KSDNARQQLERQNKELKAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1882
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1883 RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1951
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
870-1741 |
5.98e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.37 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 870 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEleEILHDLE 949
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE--EVRKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 950 SRVEeeeernqilQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRI 1029
Cdd:PTZ00121 1193 LRKA---------EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1030 AECSSQLAEEEEKAKNLAKIRNKQEVMISDleERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKK 1109
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK----KK 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1110 EEELQGALARGDDETLHKNNALKVARElQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQEL 1189
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1190 RTKREqevaELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelACEVKVLQQVKA 1269
Cdd:PTZ00121 1417 KKKAD----EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADEAKK 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1270 ESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNEldnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET 1349
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1350 RQKlnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK----KKVDDDLGTIESLEEAKKKlLKDVEAL 1425
Cdd:PTZ00121 1563 KKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKAEEE-KKKVEQL 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1426 SQRLEEKVLAYDKLEKTknrlqqelddltvdlDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETK 1505
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---------------EEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAE 1699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1506 AlslARALEEALEAKEEFERQNKQLRADMEDLMSskddvgkNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLR 1585
Cdd:PTZ00121 1700 E---AKKAEELKKKEAEEKKKAEELKKAEEENKI-------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1586 LEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEidlkdleaqieaankarDEVI 1665
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-----------------DSAI 1832
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1666 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSleaEILQLQEELASSERARRHAEQERDELADEIANS 1741
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNK---EKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1617-1907 |
1.75e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1617 KQVRELEAELEdeRKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQS 1696
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1697 KESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1776
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1777 NDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAK 1856
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1857 ERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1907
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 ... |
868-1737 |
1.29e-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: 96.58 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 868 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlAAKKQELEEILHD 947
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 948 LESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1027
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1028 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKrkldgettDLQDQIAELQAQVDELKVQLT 1107
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE--------EELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1108 KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDF-ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaq 1186
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLlKEEKKEELEILEEEEESIELKQGKLTEEKEELEK---- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1187 QELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ 1266
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1267 VKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ 1346
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1347 EETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALS 1426
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1427 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerdrAEAEAREKETKA 1506
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE------------EEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1507 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1586
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1587 EVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVI 1665
Cdd:pfam02463 844 EEQKLEKLAEEElERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1666 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKsleaEILQLQEELASSERARRHAEQERDELADE 1737
Cdd:pfam02463 924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN----KRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
857-1477 |
1.97e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.91 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 857 RVFTKVKPLLQVTRQEEELqaKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQL-QAETELFAEAEEM----- 930
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLaKLEAEIDKLLAEIeeler 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 931 --------RARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIK 1002
Cdd:TIGR02169 344 eieeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1003 KMEEEVLLLEDQNSKFIKEKKLMEDRIaecssqlAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLD 1082
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEI-------KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1083 GETTDLQDQIAELQAQVDELK----------VQLTKKEEELQGALargddETLHKNNALKVARELQAQIAELQEDFESEK 1152
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKasiqgvhgtvAQLGSVGERYATAI-----EVAAGNRLNNVVVEDDAVAKEAIELLKRRK 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1153 ASR------NKAEKQKRDLSEELE-------------------ALKTELEDTL---DTTAAQQELRTKR----EQEVAE- 1199
Cdd:TIGR02169 572 AGRatflplNKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYVFGDTLvveDIEAARRLMGKYRmvtlEGELFEk 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1200 ----------------LKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKV 1263
Cdd:TIGR02169 652 sgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1264 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEkkgikfakdAAGLESQLQDTQE 1343
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLE---------ARLSHSRIPEIQA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1344 LLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVE 1423
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1424 ALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL-EKKQKKFDQL 1477
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1315-1951 |
1.86e-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: 92.81 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1315 TLLEEAekKGI-KFAKDAAGLESQLQDTQELLQeetRQKLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEKQVLALQ 1391
Cdd:TIGR02168 159 AIFEEA--AGIsKYKERRKETERKLERTRENLD---RLEDILNELERQLKslERQAEKAERYKELKAELRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1392 sqLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTvdldhqrQIVSNLEKKQ 1471
Cdd:TIGR02168 234 --LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-------NEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1472 KKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL 1551
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1552 EKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDERK 1631
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERL-----------------QQEIEELLKKLEEAELKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1632 QRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK--LKSLEAE 1709
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1710 ILQLQE--ELASSERARRHAEQ---ERDELADEI----ANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRF 1780
Cdd:TIGR02168 528 LISVDEgyEAAIEAALGGRLQAvvvENLNAAKKAiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1781 RKTTLQ--------------VDTLNTELAAERS-----------------------AAQKSDNARQQLERQNKELKAKLQ 1823
Cdd:TIGR02168 608 VKFDPKlrkalsyllggvlvVDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1824 ELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQL 1903
Cdd:TIGR02168 688 ELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738673 1904 KRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1951
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
871-1441 |
2.31e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.05 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 871 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEqLQAETElfaEAEEMRARLAAKKQELEEILHDLES 950
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 951 RVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEVLLLEDQNSkfikEKKLMEDRIA 1030
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1031 ECSSQLAEEEEKAKNLAKIRNKQEVMisdleERLKKEEKTR---------QELEKAKRKLDGETTDLQDQIAELQAQVDE 1101
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEEL-----ERLKKRLTGLtpeklekelEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1102 LKvqltKKEEELQGAlargddetlhKNNALKVARELQAQiaELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1181
Cdd:PRK03918 424 LK----KAIEELKKA----------KGKCPVCGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1182 TTAAQQELRtkREQEVAELKKALEDETKNHEAQiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETD---NKELA 1258
Cdd:PRK03918 488 VLKKESELI--KLKELAEQLKELEEKLKKYNLE----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1259 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKfakdaagLESQL 1338
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-------LEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1339 QDTQELLQEETRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1413
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
570 580 590
....*....|....*....|....*....|
gi 1039738673 1414 AKKKLLKDVEALS--QRLEEKVLAYDKLEK 1441
Cdd:PRK03918 709 AKKELEKLEKALErvEELREKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
866-1505 |
5.41e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.36 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 866 LQVTRQEEELQaKDEELLKVKEKQTKVEGELEEMERKHQQLLE-EKNILAEQLQAETELFAEAEEmrARLAAKKQELEEI 944
Cdd:PTZ00121 1178 AEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 945 LHDLESRVEEEEERNQILQNEKKKM-----QAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----IKKMEEEVLLLEDQN 1015
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKadelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1016 SKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK--EEKTRQELEKAKRKLDGETTDLQDQIA 1093
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1094 ELQAQVDEL--KVQLTKKEEEL--QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS--RNKAEKQKRDlSE 1167
Cdd:PTZ00121 1415 AAKKKADEAkkKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1168 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataleelSEQLEQAKRFKANLEKNK 1247
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--------ADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1248 qgleTDNKELACEVKVLQQVKAESEHKRKKldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTllEEAEKKGIKF 1327
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQ 1637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1328 AKDAAglESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlalQSQLADTKKKVdddlgt 1407
Cdd:PTZ00121 1638 LKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-----LKKEAEEAKKA------ 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1408 iESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISAR 1487
Cdd:PTZ00121 1705 -EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 1039738673 1488 YAEERDRAEAEAREKETK 1505
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
998-1597 |
9.16e-18 |
|
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: 90.08 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 998 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKA 1077
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1078 KRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEEL---QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS 1154
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1155 RNKAEKQKRDLSEELEALKTELEDT----LDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRqrhaTALEELS 1230
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTqtqlNQLKDEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQLK----SEISDLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1231 EQLEQ--AKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKkldaqvqELHAKVSEGDRLRVELAEKANKLQN 1308
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1309 ELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1388
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQIND----LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1389 ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1468
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1469 KKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKALSLaraleeaLEAKEEFERQNKQLRADMEDLMSSKDDVGK 1546
Cdd:TIGR04523 531 SEKKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1547 NVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF 1597
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1417 |
1.29e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 849 KLRHWQWWRVFTKVKPLLQVTRQ---EEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQAETELFA 925
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 926 EAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----- 1000
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaee 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1001 IKKMEEEVLLLEDQNSKFIKEKKLMED-RIAECSSQLAEEEEKAKNLAKirnKQEVMISDLEERLKKEEKTRQELEKAKR 1079
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1080 KLDGETTDLQDQIAELQAQVDELK--VQLTKKEEELQGALARGDDETLHKNNALKVARELQaQIAELQEDFESEKASRNK 1157
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1158 AEKQKRdlseELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAlEELSEQLEQAK 1237
Cdd:PTZ00121 1559 KAEEKK----KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1238 RF----KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQElhakvsEGDRLRVELAEKANKLQNELDNV 1313
Cdd:PTZ00121 1634 KVeqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAEEL 1707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1314 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1393
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
570 580 590
....*....|....*....|....*....|...
gi 1039738673 1394 LADTK---------KKVDDDLGTIESLEEAKKK 1417
Cdd:PTZ00121 1784 ELDEEdekrrmevdKKIKDIFDNFANIIEGGKE 1816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1224-1943 |
1.44e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 89.59 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1224 TALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKAESEhKRKKLDAQVQELHAkvsEGDRLRVELAE-K 1302
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELAE-RYAAARERLAELEY---LRAALRLWFAQrR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1303 ANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLS-SRIRQLEEEKNSLQEQQEEEEEARK 1381
Cdd:COG4913 290 LELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1382 NLEKQVLALQSQLADTKkkvdddlgtiESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1461
Cdd:COG4913 363 RLEALLAALGLPLPASA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1462 QIVSNLEKKQKKFDQLLAEEKGISA---RYA------EERDRAEAEAREKE--TKALSLARALEEALEAKEEFERQNKQL 1530
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEaelPFVgelievRPEEERWRGAIERVlgGFALTLLVPPEHYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1531 RADMEdlmsskdDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedaklRLEVNMQAMKAQFERDLQTrdeqneE 1610
Cdd:COG4913 513 RLVYE-------RVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDYVCVDSPEELRR------H 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1611 KKRL----LLKQVRELeAELEDERKQRALAV----ASKKkmeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1682
Cdd:COG4913 574 PRAItragQVKGNGTR-HEKDDRRRIRSRYVlgfdNRAK-----LAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1683 EEARAsrdeiFAQSKESEKKLKSLEAEILQLQEELASSERAR---RHAEQERDELADEIANSASGKSALLDEKRRLEARI 1759
Cdd:COG4913 648 EALQR-----LAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1760 AQLEEELEEEQSNMELLNDRFRK-TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV---KSKFKA 1835
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMrafNREWPA 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1836 TISALEAKIGQLEE------QLEQE---AKERAAANKLVRRTEKKLKEIFMQVEDERRHAdqyKEQMEKANARMKQLK-- 1904
Cdd:COG4913 803 ETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPfg 879
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1039738673 1905 --RQLeeAEEEATRANASRRKLQRELDDATEANEGLSREVS 1943
Cdd:COG4913 880 pgRYL--RLEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
876-1576 |
2.50e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.58 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 876 QAKDEELLKVKEKQTKVEGE---LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH---DLE 949
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQilgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 950 SRVEEEEERNQILQNEKKKMQAHIQDLEeqldeeegarqKLQLEKVTAEAKIKKMEEEVllledqnskfikekKLMEDRI 1029
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIE-----------ELEKELESLEGSKRKLEEKI--------------RELEERI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1030 AECSSQLAEEEEKAKNLAKIRNKQEVMISdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvQLTKK 1109
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1110 EEELQGALARgdDETLHKnnALKVARELQAQIAELqedfeSEKASRNKAEKQKRDLsEELEALKTELEDTLDTTAAQqel 1189
Cdd:PRK03918 347 LKELEKRLEE--LEERHE--LYEEAKAKKEELERL-----KKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITAR--- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1190 RTKREQEVAELKKALEdetknheaQIQDMRQRHATALEELSEqlEQAKRFKAnleknkqgletdnkELACEVKVLQQVKA 1269
Cdd:PRK03918 414 IGELKKEIKELKKAIE--------ELKKAKGKCPVCGRELTE--EHRKELLE--------------EYTAELKRIEKELK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1270 ESEHKRKKLDAQVQELHAKVSEGDRLRV--ELAEKANKLQNELDNVStlLEEAEKKGIKFakdaaglesqlqdtqellqE 1347
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYN--LEELEKKAEEY-------------------E 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1348 ETRQKLN-LSSRIRQLEEEKNSLQEQQEEeeeaRKNLEKQVLALQSQLADTKKKvdddlgtiesLEEAKKKLLKDVEALS 1426
Cdd:PRK03918 529 KLKEKLIkLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKE----------LEELGFESVEELEERL 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1427 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEErdraeaEAREKETKA 1506
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEY 668
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1507 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEqQVEEMRTQLEELEDEL 1576
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
963-1894 |
4.94e-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: 88.10 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 963 QNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKME-------EEVLLLEDQNSKFIKEKKLmedriaecSSQ 1035
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLkekleleEEYLLYLDYLKLNEERIDL--------LQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1036 LAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLdgettdLQDQIAELQAQVDELKVQLTKKEEELQG 1115
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1116 ALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ 1195
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1196 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEqakrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR 1275
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-----SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1276 KKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNL 1355
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1356 SSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLA 1435
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1436 YDKLEKTKNRLQQELDDlTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEE 1515
Cdd:pfam02463 634 LTKLKESAKAKESGLRK-GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1516 ALEAKEEFERQNKQLRADMEDLmsskddvgknvhelekSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1595
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKI----------------NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1596 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQaqm 1675
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE--- 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1676 kdyqrelEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIansasgkSALLDEKRRL 1755
Cdd:pfam02463 854 -------EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL-------NLLEEKENEI 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1756 EARIAQLEEELeeeqsnmellndrfrkttLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1835
Cdd:pfam02463 920 EERIKEEAEIL------------------LKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1836 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQME 1894
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1408-1951 |
5.65e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1408 IESLEEAKKKLLKDVEALSQRLEEKVLaYDKLektkNRLQQELDDLTVDLDHqrqivsnLEKKQKKFDQLLAEEKGISAR 1487
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDL-HERL----NGLESELAELDEEIER-------YEEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1488 YAEERDRAE------AEAREK----ETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA 1557
Cdd:PRK02224 246 HEERREELEtleaeiEDLRETiaetEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1558 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK---AQFERDLQTRDEQNEEKKrlllKQVRELEAELEDERKQRA 1634
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRR----EEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1635 LAvaskkkmEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDE--------------IFAQSKESE 1700
Cdd:PRK02224 402 DA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1701 KKLKSLEAEILQLQEELASSErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRf 1780
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1781 rkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfkATISALEAKIGQLEEQLEqeakeraa 1860
Cdd:PRK02224 546 ------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-------- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1861 anklvRRTEKKlkEIFMQVEDERRhadqykEQMEKANARMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEAN 1935
Cdd:PRK02224 610 -----RLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570
....*....|....*.
gi 1039738673 1936 EGLSREVSTLKNRLRR 1951
Cdd:PRK02224 677 DDLQAEIGAVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1001-1816 |
7.42e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.89 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1001 IKKMEEevLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1080
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1081 LDGETTDLQDQIAELQAQV---DELKVQLTKKEEELQGAL-ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1156
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKkaeDARKAEEARKAEDARKAEeARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1157 KAEKQKRDlseelEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1236
Cdd:PTZ00121 1184 AEEVRKAE-----ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1237 KRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLQNELDNVSTL 1316
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1317 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssrirqlEEEKNSLQEQQEEEEEARKNLEkqvlaLQSQLAD 1396
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----------EEAKKKADAAKKKAEEKKKADE-----AKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1397 TKKKVDDdlgtIESLEEAKKKllkdVEALSQRLEEKVLAyDKLEKtKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQ 1476
Cdd:PTZ00121 1403 DKKKADE----LKKAAAAKKK----ADEAKKKAEEKKKA-DEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1477 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKE-EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1555
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1556 RALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLK--QVRELEAELEDERKQR 1633
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEK 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1634 ALAVASKKKMEIDLKDLEA--QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK---LKSLEA 1708
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeeLKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1709 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRrleaRIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1788
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
810 820
....*....|....*....|....*...
gi 1039738673 1789 TLNTELAAERSAAQKSDNARQQLERQNK 1816
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1135-1742 |
4.03e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.97 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1135 RELQAQIAELQEDFESEKASRNKAEK--QKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknHE 1212
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA---EL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1213 AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE-LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSE 1291
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1292 GDRlrvELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQE 1371
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEE-------ALAEAEAALRDLRR--------------ELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1372 QqeeeeeaRKNLEKQVLALQSQLADTKKKVDDDL-----------------GTIESL-----------EEAKKKLLKDVE 1423
Cdd:COG4913 434 R-------KSNIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1424 ALSQRLE---EKVLAYDKLEKT-----------------------KNRLQQELDDLTVD----LDHQR-------QIVSN 1466
Cdd:COG4913 507 RLHLRGRlvyERVRTGLPDPERprldpdslagkldfkphpfrawlEAELGRRFDYVCVDspeeLRRHPraitragQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1467 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKEtKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG- 1545
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1546 --KNVHELEKSKRALEQ---QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVR 1620
Cdd:COG4913 666 aeREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1621 ELEAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEVIKQLRKLqaqMKDYQRELEEARASRDEIFAQSKESE 1700
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYL 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738673 1701 KKLKSLEAEIL-QLQEELAssERARRHAEQERDELADEIANSA 1742
Cdd:COG4913 819 ALLDRLEEDGLpEYEERFK--ELLNENSIEFVADLLSKLRRAI 859
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1225-1950 |
6.89e-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: 84.35 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1225 ALEELSEQLEQAKRFKANLEKNKQGLET--DNKELACEVKVLQQVKAESE-----HKRKKLDAQVQELHAKVSEGDRLRV 1297
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1298 ELAEKANKLQNELDNVSTLLEEAEKK--------GIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1369
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1370 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1449
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1450 LDDLTVDLDHQRQIVSNLEKKQKKFDqllaeekgisaryaEERDRAEAEAREKETKALSLAraleealEAKEEFERQNKQ 1529
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWKLEQLA-------ADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1530 LRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAT-----------EDAKLRLEV----NMQAMK 1594
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgERYATAIEVaagnRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1595 AQFERDLQTRDEQNEEKKR-----LLLKQVRELEAELEDERKQRALAVAskkkmeIDLKDLEAQIEAANKA--RDEVIKQ 1667
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRKAgratfLPLNKMRDERRDLSILSEDGVIGFA------VDLVEFDPKYEPAFKYvfGDTLVVE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1668 ----LRKL--QAQMKDYQRELEE--------ARASRDEIFAQSKESEKkLKSLEAEILQLQEELASSERARRHAEQERDE 1733
Cdd:TIGR02169 628 dieaARRLmgKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1734 LadeiansasgKSALLDEKRRLEARiaqleeeleeeQSNMELLNDRFRKttlqvdtLNTELAAERSAAQKSDNARQQLER 1813
Cdd:TIGR02169 707 L----------SQELSDASRKIGEI-----------EKEIEQLEQEEEK-------LKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1814 QNKELKAKLQELEgAVKSKFKATISALEAKIG-----QLEEQLEQEAKERAAANKLVRRTEKKLKEIFM---QVEDERRH 1885
Cdd:TIGR02169 759 ELKELEARIEELE-EDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQE 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1886 ADQY----KEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELddateanEGLSREVSTLKNRLR 1950
Cdd:TIGR02169 838 LQEQridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL-------GDLKKERDELEAQLR 899
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
987-1614 |
7.81e-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: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 987 RQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKF-----IKEKKLMEDRIAECSSQLAEEEEKaknlakirnkqevmISDL 1060
Cdd:COG4913 249 EQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAE--------------LERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1061 EERLKKEEKTRQELEKAKRKLDGettdlqDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQ 1140
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1141 IAELQEDFESEKAS----RNKAEKQKRDLSEELEALKTELEdtldttaaqqELRTKR---EQEVAELKKALEDETKNHEA 1213
Cdd:COG4913 389 AAALLEALEEELEAleeaLAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1214 QIQ------DMRQRHA---TALEEL-----------SEQLEQAKRFkanLEKNKQGLETdnkelacevkVLQQVKAESEH 1273
Cdd:COG4913 459 ELPfvgeliEVRPEEErwrGAIERVlggfaltllvpPEHYAAALRW---VNRLHLRGRL----------VYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1274 -KRKKLDAQ--VQELHAKVSE-GDRLRVELAEKANKLQneLDNVSTLleEAEKKGI-----------KFAKDAagleSQL 1338
Cdd:COG4913 526 pERPRLDPDslAGKLDFKPHPfRAWLEAELGRRFDYVC--VDSPEEL--RRHPRAItragqvkgngtRHEKDD----RRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1339 QDTQELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ--SQLADTKKKVDDDLGTIESLEEAK 1415
Cdd:COG4913 598 IRSRYVLGFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1416 KKLLK---DVEALSQRLEEKVLAYDKLEKTKN-------RLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgis 1485
Cdd:COG4913 678 ERLDAssdDLAALEEQLEELEAELEELEEELDelkgeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER--- 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1486 aRYAEERDRAEAEAREKETKALSLARaleealeakeefeRQNKQLRADMEDLMSS-KDDVGKNVHELEKSKRALEqQVEE 1564
Cdd:COG4913 755 -FAAALGDAVERELRENLEERIDALR-------------ARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLA 819
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1565 MRTQLEelEDEL-QATEDAKLRLEVNMQAMKAQFERDLqtRDEQNEEKKRL 1614
Cdd:COG4913 820 LLDRLE--EDGLpEYEERFKELLNENSIEFVADLLSKL--RRAIREIKERI 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
865-1450 |
2.47e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 865 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELE----EMERKHQQLLEEK-NILAEQLQAETELFAEAEEMRARLAAKKQ 939
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERVLSDQRGSLDqlkaQIEEKEEKDLHERlNGLESELAELDEEIERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 940 ELEEILHDLESRveeeEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLL-------LE 1012
Cdd:PRK02224 238 EADEVLEEHEER----REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1013 DQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI 1092
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1093 AELQAQVDELKVQLTKKEEELQGALARGDDetLHKNNA-----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSE 1167
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDE--LREREAeleatLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1168 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRQRHATALEELSEQLEQAkrfkANLEKNK 1247
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERA----EELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1248 QGLEtdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNeLDNVSTLLEEAEKKGikf 1327
Cdd:PRK02224 547 AELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE--- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1328 aKDAAGLESQLQDTQElLQEETRQKL-NLSSRIRQLEEE--KNSLQEQQEEEEEARKNLEKQVLALQsQLADTKKKVDDD 1404
Cdd:PRK02224 606 -DEIERLREKREALAE-LNDERRERLaEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLD-ELREERDDLQAE 682
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1405 LG----TIESLEEAKKKlLKDVEALSQRLEEKVLAYDKLEKTKNRLQQEL 1450
Cdd:PRK02224 683 IGavenELEELEELRER-REALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1301-1907 |
2.60e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1301 EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEAR 1380
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1381 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDVEALSQRLEEKVLAYDKLEK-------TKNRLQQELD 1451
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKLSEfyeeyldELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1452 DLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAlslaraleealeakeeferQNKQLR 1531
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-------------------ELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1532 ADMEDLmsSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQTRDEQNEEK 1611
Cdd:PRK03918 379 KRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1612 KRLLlkqvRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR--DEVIKQLRKLQAQMKDYQRE-LEEARAS 1688
Cdd:PRK03918 451 KELL----EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1689 RDEIFAQSKESEKKLKSLEAEILQLQE---ELASSERARRHAEQERDELADEIANSASGKSALLDEKrrleariaqleee 1765
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEER------------- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1766 leeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1845
Cdd:PRK03918 594 ----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1846 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEdERRHADQYKEQMEKANARMKQLKRQL 1907
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKV 730
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
867-1714 |
4.41e-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: 81.63 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleeKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 946
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI---KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 947 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfikekklme 1026
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR------------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1027 driaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQL 1106
Cdd:TIGR00606 377 -------LELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1107 TKKEEELQGALARGDDETLHKNNALKVARELQAQIAELqedfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1186
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1187 QELRTKREQEVAELKKALEDETKNHEaQIQDMRQRHATALEELSEQLEQAKRFKA---NLEKNKQGLETDNKELACEVKV 1263
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQTRDRLAKLNKELAS 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1264 LQQVKAESEHKRKKLDAQVQELHAKVSEgdrlrvelAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQE 1343
Cdd:TIGR00606 603 LEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1344 -------LLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1416
Cdd:TIGR00606 675 enqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1417 KLLKDVEALSQRLEEKvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1496
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1497 AEarEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEleksKRALEQQVEEMRTQLEELEDEL 1576
Cdd:TIGR00606 831 KQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1577 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQN---EEKKRLLLKQVRELEAELED-ERKQRALAVASKKKMEIDLKDLEA 1652
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1653 QIEAANKARDEVIKQLRKLQAQM--KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1714
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1278-1849 |
4.96e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1278 LDAQVQELHAKvsegdrlrvELAEKANKLQNELDNVSTLLEEAEKKgikfaKDAAglESQLQDTQELLQ--EETRQklnl 1355
Cdd:PRK02224 192 LKAQIEEKEEK---------DLHERLNGLESELAELDEEIERYEEQ-----REQA--RETRDEADEVLEehEERRE---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1356 ssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIEsLEEAkkkllkDVEALSQRLEEkvla 1435
Cdd:PRK02224 252 --ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-LDDA------DAEAVEARREE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1436 ydkLEKTKNRLQQELDDLTVDL-DHQRQIvsnlekkqkkfdqllaeekgisARYAEERDRAEAEAREKETKALSLARALE 1514
Cdd:PRK02224 319 ---LEDRDEELRDRLEECRVAAqAHNEEA----------------------ESLREDADDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1515 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK 1594
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1595 A-------QFERDLQTRDEQNEekkrlllkQVRELEAELEDERKQRAlAVASKKKMEIDLKDLEAQIEAANKARDEVIKQ 1667
Cdd:PRK02224 454 CpecgqpvEGSPHVETIEEDRE--------RVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1668 LRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADeIANSASGKSA 1747
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIAD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1748 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQELEg 1827
Cdd:PRK02224 604 AEDEIERLREKREALAELNDERRERLAEKRER-------KRELEAEFDEARIEEARED--KERAEEYLEQVEEKLDELR- 673
|
570 580
....*....|....*....|..
gi 1039738673 1828 AVKSKFKATISALEAKIGQLEE 1849
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEE 695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1146-1887 |
6.86e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1146 EDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQrhata 1225
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1226 lEELSEQLEQAKRfkanLEKNKQGLETDNkelACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1305
Cdd:PTZ00121 1166 -AEEARKAEDAKK----AEAARKAEEVRK---AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1306 LQNELDNVstlleEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNSlqeqqeeeEEARKNLEK 1385
Cdd:PTZ00121 1238 DAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKA--------DEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1386 QVLALQSQLADTKKKVDDdlgTIESLEEAKKKllkdVEALSQRLEEKvlaYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1465
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADE---AKKKAEEAKKK----ADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1466 NLEKKQKKFDQllAEEKGISARYAEERDRAEAEAREK--ETKALSLARALEEALEAKEEFERQNKQLRADMEDlmSSKDD 1543
Cdd:PTZ00121 1372 KKEEAKKKADA--AKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--AKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1544 VGKNVHELEKSKRALEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFERDLQTRDEQNEEKKRLLLKQVRE 1621
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1622 LEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1701
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1702 KLKSLEA----EILQLQEELASSERARRHAEQERDELADEIANS---------ASGKSALLDEKRRLEARIAQLEEELEE 1768
Cdd:PTZ00121 1606 KMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1769 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQqlERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLE 1848
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
730 740 750
....*....|....*....|....*....|....*....
gi 1039738673 1849 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHAD 1887
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
861-1453 |
2.43e-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: 79.24 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 861 KVKPLLQVTRQEEELQAKDEELL-KVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFA-EAEEMRARLAA 936
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHtELQSKMRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRdAHEVATSIREI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 937 KKQELEEI--LHDLESRVEEEEERNQILQNEKKKMQAhiqdLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQ 1014
Cdd:TIGR00618 371 SCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQR----EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1015 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIrnkqevmisdleerLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1094
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI--------------HLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1095 LQAqvdelKVQLTKKEEELQGALARGDDETLHKNNALKVAR----ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1170
Cdd:TIGR00618 513 PNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1171 ALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN-----HEAQIQDMRQRHATALEELSEQL------EQAKRF 1239
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLqdvrlHLQQCSQELALKLTALHALQLTLtqervrEHALSI 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1240 KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLdaqvQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEE 1319
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1320 AEKKGIKFAKDA--AGLESQLQDTQELL------QEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1391
Cdd:TIGR00618 744 SLKELMHQARTVlkARTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1392 SQLADTKKKVDDDLgtiesleEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDL 1453
Cdd:TIGR00618 824 ETLVQEEEQFLSRL-------EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1269-1949 |
2.89e-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: 78.96 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1269 AESEHKRKKLDAQVQELHAKVsegDRLRVEL--AEKANKLQNELDNVSTLLEEAEKKgiKFAKDAAGLESQLQDTQELLQ 1346
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQL---ERLRRERekAERYQALLKEKREYEGYELLKEKE--ALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1347 EETRQKLNLSSRIRQLEEEKNSLQEQQeeeeeaRKNLEKQVLALQSQLADTKkkvdddlGTIESLEEAKKKLLKDVEALS 1426
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI------KDLGEEEQLRVKEKIGELE-------AEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1427 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKE--- 1503
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRD---KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklk 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1504 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1583
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1584 LRLEVNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELEAELE------------DERKQRALAVASKKKME------- 1644
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1645 ---------------------------------------------IDLKDLEAQIEAANK--ARDEVIKQ----LRKL-- 1671
Cdd:TIGR02169 558 avakeaiellkrrkagratflplnkmrderrdlsilsedgvigfaVDLVEFDPKYEPAFKyvFGDTLVVEdieaARRLmg 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1672 QAQMKDYQRELEE--------ARASRDEIFAQSKESEkKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSAS 1743
Cdd:TIGR02169 638 KYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1744 GKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLER-----QNKEL 1818
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1819 KAKLQELEgAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANA 1898
Cdd:TIGR02169 797 QAELSKLE-EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1899 RMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1949
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1157-1873 |
2.93e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1157 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELK---KALEDETKNHEAQIQDMRQRHATaLEELSEQL 1233
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLreiNEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1234 EQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLqneldnv 1313
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIREL--------------EERIEELKKEIEELEEKVKELKELK-EKAEEYIKL------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1314 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETrqklNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqVLALQSQ 1393
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1394 LADTKKKVdddlgTIESLEEAKKKLlkdvEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldhqRQIVSNLEKKQKK 1473
Cdd:PRK03918 374 LERLKKRL-----TGLTPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIKEL-------KKAIEELKKAKGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1474 F---DQLLAEE--KGISARYAEERDRAEAEAREKETKaLSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK-N 1547
Cdd:PRK03918 438 CpvcGRELTEEhrKELLEEYTAELKRIEKELKEIEEK-ERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKyN 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1548 VHELEKSKRALEQQVEEMRT---QLEELEDELQatedaklrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEA 1624
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKlkgEIKSLKKELE--------------------------KLEELKKKLAELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1625 ELED-ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDeVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1703
Cdd:PRK03918 571 ELAElLKELEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1704 KSLEAEIlqlqeelasSERARRHAEQERDELADEIAnsasgksalldekrRLEARIAQLEEELEEEQSNMELLNDRFrkt 1783
Cdd:PRK03918 650 EELEKKY---------SEEEYEELREEYLELSRELA--------------GLRAELEELEKRREEIKKTLEKLKEEL--- 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1784 tlqvdtlntelaaersaaQKSDNARQQLERQNKELkAKLQELEGAVKS-KFKATISALeAKIGQLEEQLEQEAKERAAAN 1862
Cdd:PRK03918 704 ------------------EEREKAKKELEKLEKAL-ERVEELREKVKKyKALLKERAL-SKVGEIASEIFEELTEGKYSG 763
|
730
....*....|.
gi 1039738673 1863 KLVRRTEKKLK 1873
Cdd:PRK03918 764 VRVKAEENKVK 774
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1000-1826 |
3.15e-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: 78.94 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1000 KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE----EEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELE 1075
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRT---VREKERELVDCQRELEKLN 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1076 KAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQG--------ALARGDDETLHKNNALKVARELQAQIAELQED 1147
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1148 FESEKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELKKALEDETKNHEAQIQDMRQRH 1222
Cdd:TIGR00606 413 LCADLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAEK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1223 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESehkRKKLDAQVQELHAKVSEGDRLRVELAEK 1302
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1303 ANK--LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL---EEEKNSLQEQQEEEE 1377
Cdd:TIGR00606 570 PNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1378 EARKNLekQVLALQSQLADTK-KKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDD 1452
Cdd:TIGR00606 650 KSSKQR--AMLAGATAVYSQFiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLApdklKSTESELKKKEKRRDE 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1453 LTVDLDHQRQIvsnLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKET--KALSLARALEEALEAKEEFERQNKQL 1530
Cdd:TIGR00606 728 MLGLAPGRQSI---IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDV 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1531 RADMEDLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA---QFERDLQTRd 1605
Cdd:TIGR00606 805 ERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRR- 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1606 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKardevikqlrKLQAQMKDYQRELEEA 1685
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1686 RASRDEIFAQSKES-EKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEE 1764
Cdd:TIGR00606 954 HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1765 ELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE 1826
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
991-1588 |
3.95e-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: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 991 QLEKVTAEAKiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKI-----RNKQEVMISDLEERLK 1065
Cdd:pfam15921 246 QLEALKSESQ-NKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiqeqaRNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1066 KEEKTRQELEKAKRKLDGettdlqdqiaelqaQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1145
Cdd:pfam15921 325 TVSQLRSELREAKRMYED--------------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1146 EDFESEKASRNKAEKQKRDLSEELEALKTELEDtldttaaqqelrtkREQEVAELKKALedetKNHEAQIQDMRQRHATA 1225
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDD--------------RNMEVQRLEALL----KAMKSECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1226 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ---------------------VKAESEHKRKKLDAQVQE 1284
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdltaslqekeraieaTNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1285 LHAKVSEGDRLR----------VELAEKANK---LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ 1351
Cdd:pfam15921 533 LQHLKNEGDHLRnvqtecealkLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1352 KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVlalqsqlADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE 1431
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV-------KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1432 KVlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL-LAEEKGISARyaeerdRAEAEAREKETKALSLA 1510
Cdd:pfam15921 686 KS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDALQSKIQFLEEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1511 raLEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAK 1583
Cdd:pfam15921 757 --MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQES 834
|
....*
gi 1039738673 1584 LRLEV 1588
Cdd:pfam15921 835 VRLKL 839
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1036-1737 |
6.33e-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: 77.70 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1036 LAEEEEKAKNLAKIRNKQEV-MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI--AELQAQVDELKvQLTKKEEE 1112
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYtQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTyhERKQVLEKELK-HLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1113 LQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEK-----QKRDLSEELEALKTELEDTLDTTAAQQ 1187
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1188 ELRTKREQEVAELKKALEDETkNHEAQIQDMRQRHAtALEELSEQLEQAKRFKANLEKNKQgLETDNKELACEVKVLQQV 1267
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1268 KAESEHKRKKLDAQVQELHAKVSEGDRLRVELA----------EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1337
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAhakkqqelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1338 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL-------------EKQVLALQSQLADTKKKVDDD 1404
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1405 LGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdLDHQRQIV-SNLEKKQKKFDQLLAEEKG 1483
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---SEAEDMLAcEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1484 ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK---RALEQ 1560
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQtllRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1561 QVEEMRTQLEELEDELQATEdaklrlevnmqamkaqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASK 1640
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLG------------------SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1641 KKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK----KLKSLEAEILQLQEE 1716
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLK 853
|
730 740
....*....|....*....|.
gi 1039738673 1717 LASSERARRHAEQERDELADE 1737
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL 874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1193-1906 |
7.86e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1193 REQEVAELKKALEDETK-NHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKnkqgletdnKELACEVKVLQQVKAES 1271
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEA---------FGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1272 EHKRKKldaqvqelhAKVSEGDRLRVELAEKANKLQNeldnvstlLEEAEKkgikfAKDAAGLESQLQDTQELLQEETRQ 1351
Cdd:PTZ00121 1114 ARKAEE---------AKKKAEDARKAEEARKAEDARK--------AEEARK-----AEDAKRVEIARKAEDARKAEEARK 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1352 klnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlALQSQLADTKKKVDDdlgtIESLEEAKK-KLLKDVEALSQRLE 1430
Cdd:PTZ00121 1172 ----AEDAKKAEAARKAEEVRKAEELRKAEDARK---AEAARKAEEERKAEE----ARKAEDAKKaEAVKKAEEAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1431 EkvlAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE--KGISARYAEERDRAEAEAR--EKETKA 1506
Cdd:PTZ00121 1241 E---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkkKADEAKKAEEKKKADEAKKkaEEAKKA 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1507 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELE---DELQATEDAK 1583
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAK 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1584 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKqralAVASKKKMEIDLKDLEAQIEAANKARDE 1663
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1664 VIKQLRKLQAQMKDYQRELEEARASRDEifAQSKESEKKlkslEAEILQLQEELASSERARRHAEQERdelADEIANSAS 1743
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKK----KADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1744 GKSAllDEKRRLE-ARIAQLEEELEEEQSNMELLNDRFRKTTL--QVDTLNTELAAERSAAQKSDNARQQLERQNKELKA 1820
Cdd:PTZ00121 1545 KKKA--DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1821 KLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTE---KKLKEIFMQVEDERRHADQYKEQMEKAN 1897
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
....*....
gi 1039738673 1898 aRMKQLKRQ 1906
Cdd:PTZ00121 1703 -KAEELKKK 1710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
875-1536 |
1.12e-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: 76.68 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 875 LQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEE 954
Cdd:pfam05483 115 IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 955 eeernQILQNEKKKMQAhiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEvllledqnskFIKEKKLMEDRIAECSS 1034
Cdd:pfam05483 195 -----MILAFEELRVQA------------ENARLEMHFKLKEDHEKIQHLEEE----------YKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1035 QLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD----LQDQIAELQAQVDELKVQLTKKE 1110
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1111 EELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ---- 1186
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKevel 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1187 QELRT-----------------------KREQEVAELKKALEDETKNHEAQ---IQDMRQRHATALEELSEQLEQAKRFK 1240
Cdd:pfam05483 408 EELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQltaIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1241 ANLEKNKQGLETDNKEL-------ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNV 1313
Cdd:pfam05483 488 IELTAHCDKLLLENKELtqeasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN---LRDELESVREEFIQKGDEV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1314 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1393
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1394 LADTKKKVDDDLGTIESLEEAKK----KLLKDVEALSQRLEEKVlaydklektknRLQQELDdltVDLDHQ-RQIVSNLE 1468
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAV-----------KLQKEID---KRCQHKiAEMVALME 710
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1469 KKQKKFDQLLAE---EKGISARYAEERDRA----EAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1536
Cdd:pfam05483 711 KHKHQYDKIIEErdsELGLYKNKEQEQSSAkaalEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
938-1714 |
1.63e-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: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 938 KQELEEILHDLESRVEEEEER----NQILQNEKKKMQAHIQDLEEQLdeeegarQKLQLEKvTAEAKIKKME---EEVLL 1010
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRlnesNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRREsqsQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1011 LEDQNS--KFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQEL------------EK 1076
Cdd:pfam15921 145 NQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1077 AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAlargddetlHKNNALKVARELQAQIAELqedfeSEKASrn 1156
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ---------HQDRIEQLISEHEVEITGL-----TEKAS-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1157 KAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1236
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1237 KRF---KANLEKNKQGLETD----NKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1309
Cdd:pfam15921 366 DQFsqeSGNLDDQLQKLLADlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1310 LDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQqeeeeearknlEKQVLA 1389
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1390 LQSQLADTKKKVDDDLGTIESL---EEAKKKLLKDVEALSQRLEEKvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1466
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLkneGDHLRNVQTECEALKLQMAEK-------DKVIEILRQQIENMTQLVGQHGRTAGA 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1467 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM----SSKD 1542
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRN 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1543 DVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAKLRLE-VNMQAMKAQFerDLQTRDEQNEEKKRL 1614
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMETttnklkmQLKSAQSELEQTRNTLKSMEgSDGHAMKVAM--GMQKQITAKRGQIDA 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1615 LLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQieaankaRDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1694
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-------KNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818
|
810 820
....*....|....*....|
gi 1039738673 1695 QSKESEKKLKSLEAEILQLQ 1714
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 ... |
865-1613 |
1.75e-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: 76.55 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 865 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQE 940
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 941 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEG-ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFI 1019
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1020 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGettdlqdqiaeLQAQV 1099
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-----------LLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1100 DELKVQLTKKEEELQGALARGDDETLHKN-NALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED 1178
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAIsTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1179 TLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1258
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1259 CEVKVLQQVKAES--EHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1336
Cdd:pfam02463 677 EIQELQEKAESELakEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1337 QLQDTQEllQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1416
Cdd:pfam02463 757 LKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1417 KLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1496
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1497 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsskddvgknvhELEKSKRALEQQVEEMRTQLEELEDEL 1576
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-----------EEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750
....*....|....*....|....*....|....*..
gi 1039738673 1577 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKR 1613
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1156-1824 |
2.52e-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: 75.44 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1156 NKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREqevaELKKALEDETKNHEAQIQDMRQrhataleelseqleq 1235
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDE----EKINNSNNKIKILEQQIKDLND--------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1236 akrfKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVS 1314
Cdd:TIGR04523 90 ----KLKKNKDKiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1315 TLLEEAEKKGIKFAKDAAGLESQLQDTQellQEETRQKLNLSSrIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQL 1394
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIK---NKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1395 ADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLT--VDLDHQRQIVSNLEKKQK 1472
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqKEQDWNKELKSELKNQEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1473 KFDQL---LAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVH 1549
Cdd:TIGR04523 322 KLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL-------RLEVNMQAMKAQFERDLQTRDEQNEEKKrLLLKQVREL 1622
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1623 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARasrDEIfaQSKESEKK 1702
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE---DEL--NKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1703 LKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1782
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1039738673 1783 TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQE 1824
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
988-1753 |
3.66e-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: 75.14 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 988 QKLQLEKVTAEAKIK----KMEEEVLLLEDQNsKFIKEKKLMEDRIaecSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1063
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1064 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHknnalkVARELQAQIAE 1143
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH------LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1144 LQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDetknheaqIQDMRQRHA 1223
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1224 TALEELSEQLEQAKRFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1302
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1303 anklqneldnvSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklnlssriRQLEEEKNSLQEQQEEEEEARKN 1382
Cdd:pfam05483 390 -----------SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1383 LEKQVLALQSQLADTKKKVDDDLGTIESLE-EAKKKLLKDVEALSQRleekvlayDKLEKTKNRLQQELDDLTVDLDHQR 1461
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1462 QIVSNLEKKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKAL--SLARALEEALEAKEEFERQNKQLRADMEDL 1537
Cdd:pfam05483 520 EDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEFIQKGDEVKCKldKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1538 MSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQatedaklRLEVNMQAMKAQFERDLQTRDEQNEEKKrlllk 1617
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-------KLELELASAKQKFEEIIDNYQKEIEDKK----- 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1618 qVRELEAELEDERKQRALAVASKKKMEIDLkdleaqieaanKARDEVIKQLRKLQAQMKDYQRELEEaRASRDEIFAQSK 1697
Cdd:pfam05483 668 -ISEEKLLEEVEKAKAIADEAVKLQKEIDK-----------RCQHKIAEMVALMEKHKHQYDKIIEE-RDSELGLYKNKE 734
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1698 ESEKKLK-SLEAEILQLQEELASSERARRHAEQERDELADEiansASGKSALLDEKR 1753
Cdd:pfam05483 735 QEQSSAKaALEIELSNIKAELLSLKKQLEIEKEEKEKLKME----AKENTAILKDKK 787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
824-1470 |
4.92e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 824 RKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEgeleemERKH 903
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 904 QQLLEEKnilAEQLQAETELFAEAEEMRARLAAKKQELEeilhdlesrveeeeernqilqnekkkmqahiqdleeqldee 983
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKKAEE----------------------------------------- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 984 egARQKLQLEKVTAEAkiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1063
Cdd:PTZ00121 1482 --AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1064 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQVDELKVQ----LTKKEEELQGALARGDDETLHKNNALKVARELQA 1139
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1140 QIAELQEDFESEKasrNKAEKQKRdlSEELEALKTELEdtldttaAQQELRTKREQEvaELKKALEDETKNHEAQIQDmr 1219
Cdd:PTZ00121 1634 KVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE-- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1220 qrhatalEELSEQLEQAKRFKAnlEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE------LHAKVSEGD 1293
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEK 1768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1294 RLRVELAEKANKLQNELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET----RQKLNLSSRIRQLEEEKNSL 1369
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELD------EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEDSAIKEVADSKNMQ 1842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1370 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1449
Cdd:PTZ00121 1843 LEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
650 660
....*....|....*....|.
gi 1039738673 1450 lDDLTVDLDHQRQIVSNLEKK 1470
Cdd:PTZ00121 1923 -EYIKRDAEETREEIIKISKK 1942
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1298-1947 |
5.01e-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: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1298 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEE 1377
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1378 EARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL 1457
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1458 DHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLradmedl 1537
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1538 msskDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLK 1617
Cdd:TIGR04523 270 ----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1618 QVRELEAELEDERKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSK 1697
Cdd:TIGR04523 343 QISQLKKELTNSESE-------NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-------LNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1698 ESEKKLKSLEAEILQLqeelasserarrhaEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1777
Cdd:TIGR04523 409 QKDEQIKKLQQEKELL--------------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1778 DRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQ--EA 1855
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKddFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1856 KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATranasrrKLQRELDDATEAN 1935
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-------SLEKELEKAKKEN 626
|
650
....*....|..
gi 1039738673 1936 EGLSREVSTLKN 1947
Cdd:TIGR04523 627 EKLSSIIKNIKS 638
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
863-1278 |
5.61e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 863 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEknilAEQLQAETELFAEAEEMRARLAAK-KQEL 941
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER----HELYEEAKAKKEELERLKKRLTGLtPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 942 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ--------------LEKVTAEakIKKMEEE 1007
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPvcgrelteehrkelLEEYTAE--LKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1008 VLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNK-QEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1086
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1087 DLQdQIAELQAQVDELKVQLTKKEEELqgalarGDDETLHKNNALKVARELQAQIAELqEDFESEKASRNKAEKQKRDLS 1166
Cdd:PRK03918 547 ELE-KLEELKKKLAELEKKLDELEEEL------AELLKELEELGFESVEELEERLKEL-EPFYNEYLELKDAEKELEREE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1167 EELEALKTELEDTLDTTA-AQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEK 1245
Cdd:PRK03918 619 KELKKLEEELDKAFEELAeTEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
410 420 430
....*....|....*....|....*....|...
gi 1039738673 1246 NKQGLETdNKELACEVKVLQQVKAESEHKRKKL 1278
Cdd:PRK03918 699 LKEELEE-REKAKKELEKLEKALERVEELREKV 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
861-1322 |
2.23e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 861 KVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQE 940
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 941 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIK 1020
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1021 EKKLMEDRIAECSSQLAEEEEKaknlaKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT---------DLQDQ 1091
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1092 IAELQAQVDELKVQ-LTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASRNKA---EKQKRDLSE 1167
Cdd:PRK03918 505 LKELEEKLKKYNLEeLEKKAEEYEKLKEK--------------LIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1168 ELEALKTELEdtldttaaqqELRTKREQEVAELKKALEdETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNK 1247
Cdd:PRK03918 571 ELAELLKELE----------ELGFESVEELEERLKELE-PFYNEYLELKDAEKE----LEREEKELKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1248 QGLETDNKELACEVKVLQQVKAESEHKRK-----KLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1322
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1274-1731 |
2.57e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1274 KRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEKKGIKFAKDAAGLEsQLQDTQELLQEETRQKL 1353
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1354 NLSSRIRQLEEEKNSLQeqqeeeeeARKNLEKQVLALQSQLADTKKKVDDDL-GTIESLEEAKKKLLKDVEALSQRLEEK 1432
Cdd:COG4717 140 ELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1433 VLAYDKLEKTKNRLQQELDDLTVDLDHQrqivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA-- 1510
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1511 --------RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATE 1580
Cdd:COG4717 287 allflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1581 DAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERK--QRALAVASKKKMEIDLKDLEAQIEAAN 1658
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1659 KARDEVIKQLRKLQAQMKDY--QRELEEARASRDEIFAQskesekkLKSLEAEILQLQEELASSERARRHAEQER 1731
Cdd:COG4717 446 EELEELREELAELEAELEQLeeDGELAELLQELEELKAE-------LRELAEEWAALKLALELLEEAREEYREER 513
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
868-1470 |
3.36e-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: 72.13 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 868 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNilaEQLQAETELFAEAEEMRARLaakKQELEEILHD 947
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNRL---QQELDDLLVD 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 948 LESrveeeeeRNQILQNEKKKMQ-----------AHIQDLEEQLDEEEGARQK----LQLEKVTAEAKIKKME------- 1005
Cdd:pfam01576 589 LDH-------QRQLVSNLEKKQKkfdqmlaeekaISARYAEERDRAEAEAREKetraLSLARALEEALEAKEElertnkq 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1006 -----EEVLLLEDQNSKFIKE----KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEK 1076
Cdd:pfam01576 662 lraemEDLVSSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1077 AKRKLdgettdLQDQIAELQAQVDELKVQLT-------KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFE 1149
Cdd:pfam01576 742 EKRRQ------LVKQVRELEAELEDERKQRAqavaakkKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1150 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAEL----------KKALEDETKNHEAQIQDMR 1219
Cdd:pfam01576 816 EARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELadeiasgasgKSALQDEKRRLEARIAQLE 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1220 qrhatalEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkaeSEHKRKKLDAQVQELHAKVSEgdrlrvel 1299
Cdd:pfam01576 896 -------EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKLQE-------- 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1300 aekanklqneldnvstlLEEAEKKgiKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknslqeqqeeeeea 1379
Cdd:pfam01576 957 -----------------MEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK--------------- 1002
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1380 rknlekqvlalqsQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDH 1459
Cdd:pfam01576 1003 -------------KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNES 1069
|
650
....*....|.
gi 1039738673 1460 QRQIVSNLEKK 1470
Cdd:pfam01576 1070 MNREVSTLKSK 1080
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1634-1874 |
3.90e-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: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1634 ALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1713
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1714 QEELasserarrhaEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1793
Cdd:COG4942 96 RAEL----------EAQKEELAELLR-------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1794 LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLK 1873
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
.
gi 1039738673 1874 E 1874
Cdd:COG4942 238 A 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
920-1648 |
4.23e-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: 71.79 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 920 ETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEA 999
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1000 KIKKMEEEVLLLEDQNSKFIKEK----KLMEDRIAECSSQLAEEEEKAK----NLAKIRNKQEVMISDLEERLKK----- 1066
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKaltgKHQDVTAKYNRRRSKIKEQNNRdiagi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1067 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddETLHKNNALKVARELQAQIAELQE 1146
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG----ELKLRLNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1147 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDttAAQQElrtkrEQEVAELKKALEdetknhEAQIQDMRQRHaTAL 1226
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASE--ALRQA-----SRRLEERQSALD------ELELQLFPQAG-TLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1227 EELSEQLEQAKRFKANLEKNKQGLETDnkeLACEVkVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvelaEKANKL 1306
Cdd:pfam12128 538 HFLRKEAPDWEQSIGKVISPELLHRTD---LDPEV-WDGSVGGELNLYGVKLDLKRIDVPEWAASEEELR----ERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1307 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNSLQeqqeeeeearknlekq 1386
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK-------NARLDLRRLFDEKQSEK---------------- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1387 vLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1466
Cdd:pfam12128 667 -DKKNKALAERKDSANER---LNSLEAQLKQLDKKHQAWLEEQKE--------QKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1467 LEKKQKKFDQLLAEEKGISARYAEE-------RDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1539
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDlaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1540 SKDDVGKNVHELEKSkraLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQV 1619
Cdd:pfam12128 815 QLSNIERAISELQQQ---LARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQG---SI 888
|
730 740
....*....|....*....|....*....
gi 1039738673 1620 RELEAELEDERKQRALAVASKKKMEIDLK 1648
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1020-1242 |
6.77e-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: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1020 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQV 1099
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1100 DEL--KVQLTKKEEELQGALARGDDETLHKNNAL--KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTE 1175
Cdd:COG4942 107 AELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1176 LedtldttAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRhATALEELSEQLEQAKRFKAN 1242
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 |
1.10e-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: 61.29 E-value: 1.10e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1039738673 31 TAKKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
895-1496 |
2.46e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 895 ELEEMERKHQQLLEEKnilaEQLQAETELFAEAEEmRARLAAKKQELEEILHDLesRVEEEEERNQILQNEKKKMQAhiq 974
Cdd:COG4913 233 HFDDLERAHEALEDAR----EQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRA--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 975 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfIKEKKLmeDRIAECSSQLAEEEEKAKNLAKIRNKQE 1054
Cdd:COG4913 303 -----------ELARLEAELERLEARLDALREELDELEAQ----IRGNGG--DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1055 VMISDLEERLKKEEK----TRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD--DETLHK- 1127
Cdd:COG4913 366 ALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLAl 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1128 ----NNALKVARELQAQIAELQEDFESEKASRNKAEK----QKRDL--SEELEALKTELEDTLDTTAAQQELRTKREQEV 1197
Cdd:COG4913 446 rdalAEALGLDEAELPFVGELIEVRPEEERWRGAIERvlggFALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1198 AELKKALED------ETKNHEAQ--IQD-MRQRHATALEELSEQLEQAKR-------FKANL---EKNKQGLET------ 1252
Cdd:COG4913 526 PERPRLDPDslagklDFKPHPFRawLEAeLGRRFDYVCVDSPEELRRHPRaitragqVKGNGtrhEKDDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1253 -DNKE----LACEVKVLQQVKAESEHKRKKLDAQVQEL------HAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAE 1321
Cdd:COG4913 606 fDNRAklaaLEAELAELEEELAEAEERLEALEAELDALqerreaLQRLAEYSWDEIDVAS----AEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1322 KkgikFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKkv 1401
Cdd:COG4913 682 A----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF-- 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1402 dDDLGTIESLEEAKKKLLKDVEALSQRLEEkvlAYDKLEKTKNRLQQELDDLTVDLD------------HQRQIVSNLEK 1469
Cdd:COG4913 756 -AAALGDAVERELRENLEERIDALRARLNR---AEEELERAMRAFNREWPAETADLDadleslpeylalLDRLEEDGLPE 831
|
650 660 670
....*....|....*....|....*....|..
gi 1039738673 1470 KQKKFDQLLAEEKG-----ISARYAEERDRAE 1496
Cdd:COG4913 832 YEERFKELLNENSIefvadLLSKLRRAIREIK 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1556-1951 |
3.07e-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: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1556 RALEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQ 1632
Cdd:COG4913 238 ERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1633 RALAVASKKKME--------IDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQrelEEARASRDEIFAQSKESEKKLK 1704
Cdd:COG4913 318 LDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1705 SLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA----------------------------LLD------ 1750
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparllalrdalaealgldeaelpfvgeLIEvrpeee 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1751 -------------------------------EKRRLEARI-AQLEEELEEEQSNMELLNDR------FRKTTLQvDTLNT 1792
Cdd:COG4913 475 rwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLvYERVRTGLPDPERPRLDPDSlagkldFKPHPFR-AWLEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1793 ELAaERSAAQKSDNArQQLER------------QNKEL-------------------KAKLQELEGAVKsKFKATISALE 1841
Cdd:COG4913 554 ELG-RRFDYVCVDSP-EELRRhpraitragqvkGNGTRhekddrrrirsryvlgfdnRAKLAALEAELA-ELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1842 AKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeiFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASR 1921
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510
....*....|....*....|....*....|
gi 1039738673 1922 RKLQRELDDATEANEGLSREVSTLKNRLRR 1951
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1084-1853 |
5.64e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1084 ETTDLQDQIAELQAQVDELkvqltkkeEELQGALargdDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-----A 1158
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1159 EKQKRDLSEELEALKTELEDTldttaaqqelrtkrEQEVAELKKALEDetknHEAQIQDMRQRHATALEELSEQLEQakr 1238
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARLDA----LREELDELEAQIRGNGGDRLEQLER--- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1239 fkanleknkqgletdnkelacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRlrvELAEKANKLQNELDNVSTLLE 1318
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1319 EAEkkgikfaKDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVLALQSQLADTK 1398
Cdd:COG4913 402 ALE-------EALAEAEAALRDLRR--------------ELRELEAEIASLERR-------KSNIPARLLALRDALAEAL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1399 KKVDDDL-----------------GTIESL-----------EEAKKKLLKDVEALSQRLEekvLAYDKLEKT-KNRLQQE 1449
Cdd:COG4913 454 GLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVNRLHLRGR---LVYERVRTGlPDPERPR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1450 LDDltvdldhqRQIVSNLEKKQKKFDQLLAEEkgisarYAEERDRA---EAEAREKETKALSLARaleealeakeeferq 1526
Cdd:COG4913 531 LDP--------DSLAGKLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRHPRAITRAG--------------- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1527 nkqlradmedLMSSkddvGKNVHELEKSKRALEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlqtr 1604
Cdd:COG4913 582 ----------QVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---- 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1605 deqneEKKRLLLKQVRELEAElederkqralavaskkkmEIDLKDLEAQIEAANKARDEVIK---QLRKLQAQMKDYQRE 1681
Cdd:COG4913 644 -----QERREALQRLAEYSWD------------------EIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAE 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1682 LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELassERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1761
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1762 LEEELEEEQSNMELLNDRFRKT-TLQVDTLNTELAAERSAAQKsdnaRQQLERQN-KELKAKLQELEGAVKSKFKATI-S 1838
Cdd:COG4913 778 LRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEEDGlPEYEERFKELLNENSIEFVADLlS 853
|
810
....*....|....*
gi 1039738673 1839 ALEAKIGQLEEQLEQ 1853
Cdd:COG4913 854 KLRRAIREIKERIDP 868
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1061-1891 |
1.75e-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: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1061 EERLKKEEKT---RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlHKN---NAL--- 1131
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAASD-------HLNlvqTALrqq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1132 -KVAR------ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED---TLDT--TAA---QQELRTKRE-Q 1195
Cdd:COG3096 347 eKIERyqedleELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqALDVqqTRAiqyQQAVQALEKaR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1196 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLEtdnkelacevKVLQQVKAESEHKR 1275
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVC----------KIAGEVERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1276 -KKLDAQVQELHAKVSEGDRLRVELAEkANKLQNELDNVSTLLEEaekkgikFAKDAAGLESQLQDTQELLQEETRQKLN 1354
Cdd:COG3096 497 aRELLRRYRSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEE-------FCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1355 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLkdvealsQRLEE 1431
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLL-------ERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1432 KVLAYDKLEKTKNRLQQElddltvdldhqrqiVSNLEKKQKKFD---QLLAEEKG------------------ISARYAE 1490
Cdd:COG3096 642 ATVERDELAARKQALESQ--------------IERLSQPGGAEDprlLALAERLGgvllseiyddvtledapyFSALYGP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1491 ER------DraeaeareketkaLSLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK----- 1553
Cdd:COG3096 708 ARhaivvpD-------------LSAVK-------------EQLAGLEDCPEDLYliegdpDSFDDSVFDAEELEDavvvk 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1554 -SKRAL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEE 1610
Cdd:COG3096 762 lSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEA 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1611 KKRLLLKQVRELEAELEDERKQralavaskkkmeidLKDLEAQIEAANkardEVIKQLRKLQAQM------------KDY 1678
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQ--------------EQQLRQQLDQLK----EQLQLLNKLLPQAnlladetladrlEEL 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1679 QRELEEARASRDEIFAQSK---ESEKKLKSLEAEILQ---LQEELASSERARRHAEQERDELADEIANSA----SGKSAL 1748
Cdd:COG3096 899 REELDAAQEAQAFIQQHGKalaQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1749 LDEKRRLEARIAQLEEELEEEQSNmelLNDRFRKTTLQVDTLNTELAAERSAAqksDNARQQLerqnKELKAKLQELEGA 1828
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARRE---AREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTL----QELEQELEELGVQ 1048
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1829 V-----------KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqveDERRHADQYKE 1891
Cdd:COG3096 1049 AdaeaeerarirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKA 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1651-1874 |
1.96e-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: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1651 EAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELasserarrhaEQE 1730
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1731 RDELADEIA------NSASGKSALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKs 1804
Cdd:COG3883 85 REELGERARalyrsgGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1805 dnARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1874
Cdd:COG3883 155 --KLAELEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1628-1950 |
2.45e-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: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1628 DERKQRALAvaskkkmeiDLKDLEAQIEAANKARDEVIKQLRKLQAQ------MKDYQRELEEARASrdEIFAQSKESEK 1701
Cdd:TIGR02169 169 DRKKEKALE---------ELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGY--ELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1702 KLKSLEAEILQLQEELASSERarrhaeqERDELADEIAnsasgksALLDEKRRLEARIaqleeeleeeqsnMELLNDRFR 1781
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTE-------EISELEKRLE-------EIEQLLEELNKKI-------------KDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1782 KTTLQVDTLNTELAaersaaqksdnarqQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQEAKERAAA 1861
Cdd:TIGR02169 291 RVKEKIGELEAEIA--------------SLERSIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1862 NKLVRRTEKKLKEIFMQVEDE-------RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA 1934
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330
....*....|....*.
gi 1039738673 1935 NEGLSREVSTLKNRLR 1950
Cdd:TIGR02169 436 INELEEEKEDKALEIK 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1125-1842 |
3.94e-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: 65.24 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1125 LHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAA-QQELRTKREQeVAELKKA 1203
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQ-WKEKRDE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1204 LEDETKNHEAQIQDMRqrhatalEELSEQLEQAKRF-KANLEKNKQGLETdnkelacevkvLQQVKAESEHKRKKLDAQV 1282
Cdd:pfam12128 306 LNGELSAADAAVAKDR-------SELEALEDQHGAFlDADIETAAADQEQ-----------LPSWQSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1283 QELHAKVSEGDRLRV----ELAEKANKLQNELDNVStllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETR-QKLNLSS 1357
Cdd:pfam12128 368 GKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESELREQLEAGKLEFNeEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1358 RIRQL----------EEEKNSLQEQQEEEEEARKNLE---KQVLALQSQLADTKKKVDddlgtiesleEAKKKLlkdvEA 1424
Cdd:pfam12128 445 RLGELklrlnqatatPELLLQLENFDERIERAREEQEaanAEVERLQSELRQARKRRD----------QASEAL----RQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1425 LSQRLEEkvlaydklektknrLQQELDDLTVDLDHQR-QIVSNLEKKQKKFDQLLAeeKGISARYAEERDRAEAEAREKE 1503
Cdd:pfam12128 511 ASRRLEE--------------RQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1504 TKALSLARALEEALEAKEEFERQ-NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDA 1582
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAAsEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1583 KLRLEVNMQAMKAQFERDLQTRDEQNEE--------KKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQI 1654
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANErlnsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1655 EAANKARDEVIKqlRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaEILQLQEELASSERARRHA-EQERDE 1733
Cdd:pfam12128 735 KAAIAARRSGAK--AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE-RIAVRRQEVLRYFDWYQETwLQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1734 LADEIANSASGKSALLDEKRRLEA----RIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTeLAAERSAAQKSDNARQ 1809
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT-LKEDANSEQAQGSIGE 890
|
730 740 750
....*....|....*....|....*....|....*.
gi 1039738673 1810 QLeRQNKELKAKLQELEGAVKSK---FKATISALEA 1842
Cdd:pfam12128 891 RL-AQLEDLKLKRDYLSESVKKYvehFKNVIADHSG 925
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
869-1478 |
3.99e-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: 65.04 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 869 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 948
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 949 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIKEKKLMEdr 1028
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLE-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1029 iaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEK----TRQELEKAKRKLDGETTDLQD---QIAELQAQVDE 1101
Cdd:TIGR04523 218 -----SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1102 LKVQLtkkeeelqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1181
Cdd:TIGR04523 293 LKSEI----------------SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1182 TTAAQQELRTKREQEVAELKKALE---DETKNHEAQIQDMRQrhataleelseQLEQAKRFKANLEKNKQGLETDNKELA 1258
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1259 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQL 1338
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1339 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQL--ADTKKKVDDDLGTIESLEEAKK 1416
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQK 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1417 KLLKDVEALSQRLeekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL 1478
Cdd:TIGR04523 579 SLKKKQEEKQELI-------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1134-1927 |
4.70e-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: 65.07 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1134 ARELQAQIAELQEDFESEKASRNKAEKQKRDLSE---ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN 1210
Cdd:TIGR00606 219 ACEIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1211 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ-QVKAESEHKRKKlDAQVQELHAkv 1289
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLAT-- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1290 segdRLRVELAEKANKLQNELDNVSTLLEEAEKKGikfAKDAAGLESQLQDTQELLQE---ETRQKLNLSSRIRQLEEEK 1366
Cdd:TIGR00606 376 ----RLELDGFERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTIELKKEI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1367 nslqeqqeeeeearknLEKQvlalQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSqRLEEKVLAYDKLEKTKNRL 1446
Cdd:TIGR00606 449 ----------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1447 QQELDdltvdldhqrqivsnLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKalslaraleealeakeefERQ 1526
Cdd:TIGR00606 508 NEKAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------------------DEQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1527 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFERDLQTRDE 1606
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEE 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1607 QneekkrlllkqvrelEAELEDerkqRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1686
Cdd:TIGR00606 620 Q---------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1687 ASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1766
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1767 EEEQSNMElLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVK----SKFKATISALEA 1842
Cdd:TIGR00606 761 QRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELD 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1843 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRR 1922
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE 919
|
....*
gi 1039738673 1923 KLQRE 1927
Cdd:TIGR00606 920 KDQQE 924
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
873-1319 |
4.73e-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: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 873 EELQAKDEELLKVKEKQTKVEGE-------LEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQEL 941
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 942 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK- 1020
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1021 ----EKKLMEDR--IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1094
Cdd:pfam05483 491 tahcDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1095 LQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1174
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1175 ELEDTLDTTAAQQELRTKREQEV---AELKKALEDETKNHEAQIqDMRQRHATAleelseqleqakRFKANLEKNKQGLE 1251
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEKLleeVEKAKAIADEAVKLQKEI-DKRCQHKIA------------EMVALMEKHKHQYD 717
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1252 TDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAK-VSEGDRLRVELAEKANKLQNELDNVSTLLEE 1319
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAElLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1654-1951 |
4.82e-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: 65.09 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1654 IEAANKARDEVIKQLrklqAQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELassERARRHAEqERDE 1733
Cdd:TIGR02169 148 ISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKRQQLERL---RREREKAE-RYQA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1734 LADEIANSASgkSALLDEKRRLEARIAQLEEELEEEQSNMEllndrfrKTTLQVDTLNTELAAersaaqksdnARQQLER 1813
Cdd:TIGR02169 216 LLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELE-------KLTEEISELEKRLEE----------IEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1814 QNKELKAKLQELEGAVKSK---FKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1890
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1891 EQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1951
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1088-1874 |
4.98e-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: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1088 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVAREL-QAQIAELQE-DFESEKASRNKAE--KQKR 1163
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEeiQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1164 DLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIqdmrqrhaTALEELSEQLEQAK-RFKAN 1242
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlEMHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1243 LEKNKQGLETDNKELACEVKvlqqvkaESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1322
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEIN-------DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1323 KGIKFAKDAAGLESQLQ---DTQELLQEETRQKlnlSSRIRQLEEEKNSlqeQQEEEEEARKNLEKQVLALQSQLADTKK 1399
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQrsmSTQKALEEDLQIA---TKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1400 KVDDDLGTIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTVDLDHQRQIVSnlekKQKKFDQLLA 1479
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEE-------MTKFKNNKEVELEELKKILAEDEKLLD----EKKQFEKIAE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1480 EEKGisaryAEERDRAEAEAREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1559
Cdd:pfam05483 433 ELKG-----KEQELIFLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1560 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfERDLQTRDEqneekkrllLKQVRELEAELEDERKQRAlavas 1639
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDE---------LESVREEFIQKGDEVKCKL----- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1640 kKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAS 1719
Cdd:pfam05483 569 -DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1720 serARRHAEQERDELADEIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnDRFRKTTLQVDTLNTELAAERS 1799
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA------------------DEAVKLQKEIDKRCQHKIAEMV 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1800 AAQKSDNAR--QQLERQNKEL---KAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1874
Cdd:pfam05483 707 ALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1550-1761 |
7.41e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDE 1629
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1630 RKQRA--LAVASKKKMEIDLKDLEAQIEAANKARD-EVIKQL-RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS 1705
Cdd:COG4942 103 KEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1706 LEAEILQLQEELASSERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQ 1761
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIAR 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1650-1902 |
7.56e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.27 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1650 LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIF--AQSKESEKKLKSLEAEILQLQEELASSErARRHA 1727
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAE-ARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1728 EQERDELADEIANSASGKSALldekRRLEARIAQleeeleeeqsnmellndrfrkttlqvdtLNTELAAERSAAQKSDNA 1807
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVI----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1808 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLvrrtEKKLKEIFMQVEDERRHAD 1887
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYE 368
|
250
....*....|....*
gi 1039738673 1888 QYKEQMEKANARMKQ 1902
Cdd:COG3206 369 SLLQRLEEARLAEAL 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
867-1323 |
9.18e-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: 63.89 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEmerkHQQLLEEKNILAEQLQAE-TELFAEAEEMrarlaaKKQELEEIL 945
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSE----KQKELEQNNKKIKELEKQlNQLKSEISDL------NNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 946 HDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLM 1025
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1026 EDRIAECSSQLAEEEEKAKNlakirnkqevmisdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ 1105
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQ--------------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1106 LTKKEeelqgalargddetlhknnalKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL---KTELEDTLDT 1182
Cdd:TIGR04523 456 IKNLD---------------------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneeKKELEEKVKD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1183 TAAQQELRTKREQEVAELKKALEDETKNHEAQIQDM-----RQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKEL 1257
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1258 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKK 1323
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1088-1841 |
1.10e-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: 63.69 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1088 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD---ETLHKNNALKvaRELQAQIAELQEdfesekasrnkaekQKRD 1164
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTfwsPELKKERALR--KEEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1165 LSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDE------TKNHEAQIQDMRQRHATALEELSEQLEQakr 1238
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKfstpelTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1239 FKANLEKNKQGLETDNKELACEVKVLQ-----QVKAESEHKRKK----LDAQVQE----LHAKVSEGDRLRVELAEKaNK 1305
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHlevlLDQKEKENIHLREELHRR-NQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1306 LQNELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKNSLQEQQEEEEEARK 1381
Cdd:pfam10174 221 LQPDPAKTKALQTVIEMKDTKISS----LERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKIDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1382 NLEK---QVLALQSQLADTKKKVDDDLGTIESLEE---AKKK----LLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1451
Cdd:pfam10174 297 ELSKkesELLALQTKLETLTNQNSDCKQHIEVLKEsltAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1452 DLTVDLDHQRQIVSNLEKK----QKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLaraleealeakeeferqn 1527
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL------------------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1528 kqlrADMEDLMSSKDDVGKNV-HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQTRDE 1606
Cdd:pfam10174 439 ----TTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----ASSLA 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1607 QNEEKKRLLLKQvreLEAELEDERKQRALAVASKKKMEidlkdleaQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1686
Cdd:pfam10174 510 SSGLKKDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQ 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1687 ASRDEIFAQSKESE-------KKLKSLEAEILQLQEELASSERARRHAEQERDEladeiansasgKSALLDEkrrlEARI 1759
Cdd:pfam10174 579 AEVERLLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE----EARR 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1760 AQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSD----NARQQLERQNKE-LKAKLQELEGAVKSKfK 1834
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghltNLRAERRKQLEEiLEMKQEALLAAISEK-D 722
|
....*..
gi 1039738673 1835 ATISALE 1841
Cdd:pfam10174 723 ANIALLE 729
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1352-1948 |
1.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1352 KLNLSSRIRQLEEEKNSLQEQQEEEEeaRKNLEKQVLALQSQLADTKKKVDDdlGTIEslEEAKKKLLKDVEALSQRLEE 1431
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAK--EDNRADEATEEAFGKAEEAKKTET--GKAE--EARKAEEAKKKAEDARKAEE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1432 KVLAYDKLEKTKNRLQQelDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETKALSLAR 1511
Cdd:PTZ00121 1133 ARKAEDARKAEEARKAE--DAKRVEIARKAEDARKAEEARKAEDAKKAEA----ARKAEEVRKAEELRKAEDARKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1512 ALEEALEAKEEFERQNKQLRADMEDLMSSKDDVgknvhelEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmQ 1591
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA-------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---E 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1592 AMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL----------AVASKKKMEIDLKDLEAQIEAANKAR 1661
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeakkkADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1662 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEA-----EILQLQEELASSERARRHAEQERDelAD 1736
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkadELKKAAAAKKKADEAKKKAEEKKK--AD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1737 EIANSASGKSALLDEKRRLE-ARIAQLEEELEEEQSNMELLndrfRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQN 1815
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEA----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1816 KELKAKLQELEGAVKSKFKATISALEAKIGQLEEQleQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEK 1895
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1896 ANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1948
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1057-1233 |
1.21e-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: 60.71 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1057 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNAlKVARE 1136
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1137 LQAqiaeLQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQIQ 1216
Cdd:COG1579 91 YEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 1039738673 1217 DMRQRHATALEELSEQL 1233
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1169-1640 |
1.26e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1169 LEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQ 1248
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE--------LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1249 GLET--DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiK 1326
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---D 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1327 FAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK-NLEKQVLALQSQLADTKKKVDDDL 1405
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1406 G----TIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE 1481
Cdd:COG4717 277 GvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1482 KGISARYAEER---------DRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS--SKDDVGKNVHE 1550
Cdd:COG4717 357 EELEEELQLEEleqeiaallAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1551 LEKSKRALEQQVEEMRTQLEELEDELQATEDaklrlEVNMQAMKAQFERDLQTRDEQNEE--KKRLLLKQVRELEAELED 1628
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEwaALKLALELLEEAREEYRE 511
|
490
....*....|..
gi 1039738673 1629 ERKQRALAVASK 1640
Cdd:COG4717 512 ERLPPVLERASE 523
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
887-1761 |
1.50e-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: 63.43 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 887 EKQTKVEGELEemerKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeILHDLESRVeeeeeRNQILQNEK 966
Cdd:COG3096 279 ERRELSERALE----LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQ-AASDHLNLV-----QTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 967 -KKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV-----------LLLEDQNSKFIKEKKLMEdRIAECSS 1034
Cdd:COG3096 349 iERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladyqQALDVQQTRAIQYQQAVQ-ALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1035 QLAEEEEKAKN----LAKIRNKQEVMIS---DLEERLKKEEKTRQELEKAK---RKLDGETTdlqdqiaelQAQVDELKV 1104
Cdd:COG3096 428 LCGLPDLTPENaedyLAAFRAKEQQATEevlELEQKLSVADAARRQFEKAYelvCKIAGEVE---------RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1105 QLTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASR------NKAEKQKRDLSEELEALKTELED 1178
Cdd:COG3096 499 ELLRRYRSQQALAQR--------------LQQLRAQLAELEQRLRQQQNAErlleefCQRIGQQLDAAEELEELLAELEA 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1179 TLDTTAAQQElrtkreqEVAELKKALEDETKNHEAQIQDMRQRH------ATALEELSEQLEQAkrfkanLEkNKQGLET 1252
Cdd:COG3096 565 QLEELEEQAA-------EAVEQRSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEA------LA-DSQEVTA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1253 DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAN-KLQNEL-DNVStlLEeaekkgikfakD 1330
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGgVLLSEIyDDVT--LE-----------D 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1331 AAGLESqlqdtqelLQEETRQKL---NLSSRIRQLEEEKNSLQEqqeeeeearknlekqvLALQSQLADTkkkVDDDLGT 1407
Cdd:COG3096 698 APYFSA--------LYGPARHAIvvpDLSAVKEQLAGLEDCPED----------------LYLIEGDPDS---FDDSVFD 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1408 IESLEEAkkkllkDVEALSQRL-------EEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAE 1480
Cdd:COG3096 751 AEELEDA------VVVKLSDRQwrysrfpEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1481 EKGIsaryAEERDrAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA-LE 1559
Cdd:COG3096 825 HLAV----AFAPD-PEAELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADEtLA 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1560 QQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMK---AQFERdLQTRDEQNEEKKRLL------LKQVRELEAELE 1627
Cdd:COG3096 893 DRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLkqqifaLSEVVQRRPHFS 971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1628 DERKQRALAVASkkkmeiDLKD-LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1706
Cdd:COG3096 972 YEDAVGLLGENS------DLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1707 EaeilqLQEELASSERARrhaeQERDELADEIANSASGKSALLDEKRRLEARIAQ 1761
Cdd:COG3096 1046 G-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1549-1951 |
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 1039738673 1549 HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE-RDLQTRDEQNEEKkrllLKQVRELEAELE 1627
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEER----LEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1628 DERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1706
Cdd:COG4717 167 ELEAELAeLQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1707 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQ 1786
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1787 VDTLNTELAAE--RSAAQKSDNARQQLERQNK-ELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1863
Cdd:COG4717 327 ALGLPPDLSPEelLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1864 LVRRTEKKLKEIFMQVEDErrhadqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE--GLSRE 1941
Cdd:COG4717 407 LEEQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQE 477
|
410
....*....|
gi 1039738673 1942 VSTLKNRLRR 1951
Cdd:COG4717 478 LEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1495-1723 |
1.96e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1495 AEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1574
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1575 ELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlkqvrELEAELEDERKQRALAVASKKKMEIDLK-DLEAQ 1653
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRaELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1654 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA 1723
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
915-1283 |
2.19e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.83 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 915 EQLQAETELFAEAEEMRA-------RLAAKKQELEEILHDLESRVEEEEERNQILQNEK--KKMQAHIQDLEEQLDEEEG 985
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 986 ARQKLQLEKVTAEAKIKKmeEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE--EEEKAKNLAKIRNKQEVMIsdleER 1063
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERirQEEIAMEISRMRELERLQM----ER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1064 LKKEEKTRQELEKAkRKLDGETTDLQDQIAELQAQVDELK--------VQLTKKEEELQGALARGDDETLHKNNALKVAR 1135
Cdd:pfam17380 388 QQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1136 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEElealktELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQI 1215
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1216 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKaESEHKRKKLDAQVQ 1283
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 ... |
871-1598 |
2.51e-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: 62.68 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 871 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIlhdles 950
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 951 rveeeeernqILQNEKKKMQAHIQDLEEQLDEEEGARQKLQlekvTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIA 1030
Cdd:TIGR00618 287 ----------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ----SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1031 ECsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDeLKVQLTKKE 1110
Cdd:TIGR00618 353 QE-IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1111 EELQGALARGDDETLHknnALKVARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR 1190
Cdd:TIGR00618 431 KQQELQQRYAELCAAA---ITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1191 TKREQEV-AELKKALEDE-TKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELAcevKVLQQVK 1268
Cdd:TIGR00618 507 CGSCIHPnPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT---QCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1269 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEkkgikFAKDAAGLESQLQDTQ-ELLQE 1347
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-----CSQELALKLTALHALQlTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1348 ETRQKlnlSSRIRQLEEEKnslqeqqeeeEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1427
Cdd:TIGR00618 659 RVREH---ALSIRVLPKEL----------LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1428 RLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQRQIVSNLEKKQKKFDQLLAEEKgISARYAEERDRAEAEAREKETKAL 1507
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQSLKELMHQ-----ARTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTH 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1508 SLARALEealeakeeferQNKQLRADMEDLMSSKDdvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE 1587
Cdd:TIGR00618 800 LLKTLEA-----------EIGQEIPSDEDILNLQC------ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730
....*....|.
gi 1039738673 1588 vnmQAMKAQFE 1598
Cdd:TIGR00618 863 ---QLTQEQAK 870
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
928-1507 |
2.56e-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: 62.53 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 928 EEMRARLAAKKQELEeilhdlesrveeeeERNQILQNEKKKMQAHIQDLEEQLDEEEGARQklqleKVTAEAKIKKMEee 1007
Cdd:pfam10174 140 EEMELRIETQKQTLG--------------ARDESIKKLLEMLQSKGLPKKSGEEDWERTRR-----IAEAEMQLGHLE-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1008 vLLLEDQNSKFIKEKKLMEDRiaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEktrQELEKAKRKLDGETTD 1087
Cdd:pfam10174 199 -VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1088 LQDQIAELQA----------QVDELKVQLTKKEEELQGALARgdDETLHKNNA-----LKVARE-----------LQAQI 1141
Cdd:pfam10174 270 REEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTK--LETLTNQNSdckqhIEVLKEsltakeqraaiLQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1142 AELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELKKALE---DETKNHEAQIQDM 1218
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1219 RQRHA----------TALEELSEQLEQAKRFKANLEKNKqglETDNKELACEVKVLQQvkaesehKRKKLDAQVQELHAK 1288
Cdd:pfam10174 421 KERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK-------ENKDLKEKVSALQPE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1289 VSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQElLQEETRQKLNLSSRIRQLEEEkns 1368
Cdd:pfam10174 491 LTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE--- 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1369 LQEQQEEEEEARKNLEKqVLALQSQLADTKKKVDDDLGTIESL------EEAKKKL-LKDVEALSQRLEEKVLA---YDK 1438
Cdd:pfam10174 567 VARYKEESGKAQAEVER-LLGILREVENEKNDKDKKIAELESLtlrqmkEQNKKVAnIKHGQQEMKKKGAQLLEearRRE 645
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1439 LEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAL 1507
Cdd:pfam10174 646 DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
882-1475 |
3.26e-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: 61.96 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 882 LLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQI 961
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 962 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLE-----KVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQL 1036
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1037 AEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELqga 1116
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI--- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1117 largddetlhknnalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaQQELRTKrEQE 1196
Cdd:TIGR04523 443 ------------------KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK------QKELKSK-EKE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1197 VAELKKaledETKNHEAQIQDMRQRHATALEELSEqleqakrfkanLEKNKQGLETDNKELACEVKvlqqvKAESEHKRK 1276
Cdd:TIGR04523 498 LKKLNE----EKKELEEKVKDLTKKISSLKEKIEK-----------LESEKKEKESKISDLEDELN-----KDDFELKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1277 KLDAQVQELHAKVSE----GDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFakdaagleSQLQDTQELLQEETRQk 1352
Cdd:TIGR04523 558 NLEKEIDEKNKEIEElkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI--------SSLEKELEKAKKENEK- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1353 lnLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1432
Cdd:TIGR04523 629 --LSSIIKNIKSKKNKLKQEV-------KQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITR 699
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1039738673 1433 VLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFD 1475
Cdd:TIGR04523 700 MIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFD 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1704-1948 |
4.02e-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: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1704 KSLEAEILQLQEELASSERARRHAEQERDELAdeiansasgksaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1783
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1784 tlQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1863
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1864 LVRRTEkklkeifMQVEDErrhADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateanegLSREVS 1943
Cdd:COG4913 367 LLAALG-------LPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 1039738673 1944 TLKNR 1948
Cdd:COG4913 430 SLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
873-1291 |
4.10e-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: 61.96 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 873 EELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEK-----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 947
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 948 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1027
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1028 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLT 1107
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1108 KKEEELQgALARGDDETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKA--EKQKRDLSEELEALKTELEDTLDTTA 1184
Cdd:TIGR04523 507 ELEEKVK-DLTKKISSLKEKIEKLESEKkEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1185 AQQELRTKREQEVAELKKALEDETKnheaqiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVL 1264
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEK---------------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
410 420
....*....|....*....|....*..
gi 1039738673 1265 QQVKAESEHKRKKLDAQVQELHAKVSE 1291
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1425-1874 |
5.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1425 LSQRLEEKVLAYDKLE-KTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEerDRAEAEAREKE 1503
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1504 TKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskddvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1583
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1584 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL-----------AVASKKKMEIDLKDLEA 1652
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1653 QIEAA------------------NKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1714
Cdd:COG4717 274 TIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1715 EELASSERARR--HAEQERDELADEIA----NSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDrfrktTLQVD 1788
Cdd:COG4717 354 REAEELEEELQleELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1789 TLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGavkskfKATISALEAKIGQLEEQLEQEAKERAAAN---KLV 1865
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE------DGELAELLQELEELKAELRELAEEWAALKlalELL 502
|
....*....
gi 1039738673 1866 RRTEKKLKE 1874
Cdd:COG4717 503 EEAREEYRE 511
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1529-1861 |
5.36e-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: 60.47 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1529 QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQTRDEQN 1608
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1609 EEKKRLL---LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEA 1685
Cdd:pfam19220 107 EELRIELrdkTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1686 RASRDEIFAQSKESEKKLKSLEAEILQLQ----EELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1761
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1762 LEEELEEEQSNMELLNDRFRKTTLQVDT-------LNTELAAERSAAQKSDNARQQLERQ----NKELKAKLQELEGAVK 1830
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTlerrlagLEADLERRTQQFQEMQRARAELEERaemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039738673 1831 S-------------KFKATISALEAKIGQLEEQLEQEAKERAAA 1861
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1952 |
5.68e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1714 QEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1793
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1794 LAAERSAAQKSDNARQQLERQNK-ELKAKLQELEGAVKSkfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1872
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1873 KEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRG 1952
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1412-1950 |
5.93e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1412 EEAKKKLLKDVealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARyaEE 1491
Cdd:PRK03918 144 DESREKVVRQI----LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE--LP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1492 RDRAEAEAREKETKalslaraleealeakeeferqnkqlraDMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEE 1571
Cdd:PRK03918 218 ELREELEKLEKEVK---------------------------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1572 LEDELQATEDAKLRLEvNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELEAELED-ERKQRALAVASKKKME 1644
Cdd:PRK03918 271 LKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKElEEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1645 I--DLKDLEAQIEAANKARdEVIKQLRKLQAQMKDY-----QRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEEL 1717
Cdd:PRK03918 350 LekRLEELEERHELYEEAK-AKKEELERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1718 ASSERARRH--------AEQERDEL-----------ADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN- 1777
Cdd:PRK03918 429 EELKKAKGKcpvcgrelTEEHRKELleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEl 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1778 ----------------DRFRKTTLQVDTLNTE---LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATIS 1838
Cdd:PRK03918 509 eeklkkynleelekkaEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1839 ALEAKIGQLEEqLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEatRAN 1918
Cdd:PRK03918 589 ELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELR 665
|
570 580 590
....*....|....*....|....*....|..
gi 1039738673 1919 ASRRKLQRELDDATEANEGLSREVSTLKNRLR 1950
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
829-1612 |
7.23e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.22 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 829 KKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLE 908
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIR 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 909 EKNILAEQLQAETEL-------FAEAE------EMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQD 975
Cdd:TIGR00606 365 ARDSLIQSLATRLELdgfergpFSERQiknfhtLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 976 LEEQLDEEEGARQ--KLQLEKVTAEAK-IKKMEEEV------LLLEDQNS----KFIKEKKLMEDRIAECSSQLAEEEEK 1042
Cdd:TIGR00606 445 KKEILEKKQEELKfvIKELQQLEGSSDrILELDQELrkaereLSKAEKNSltetLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1043 A-KNLAKIRNKQEVMISD--------------------------------LEERLKKEEKTRQELEKAKRKLDGETTDLQ 1089
Cdd:TIGR00606 525 EqLNHHTTTRTQMEMLTKdkmdkdeqirkiksrhsdeltsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1090 DQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKN--NALKVARELQAQIA---ELQEDFESEKASRN-------- 1156
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERlkEEIEKSSKQRAMLAgatAVYSQFITQLTDENqsccpvcq 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1157 ---KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL 1233
Cdd:TIGR00606 685 rvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK----LQKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1234 EqakRFKANLEKNKQGLETDN------KELACEVKVLQQVKAESEHKRKKLDAQVQELHAkvSEGDRLRVELAEKANKLQ 1307
Cdd:TIGR00606 761 Q---RLKNDIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQ 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1308 NELDNVSTLLEEAEKkgikfakdaaglesqlqdtqeLLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV 1387
Cdd:TIGR00606 836 HELDTVVSKIELNRK---------------------LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1388 LALQSQLADTKKKVDDDLgtieSLEEAKKKLLKDVEAL-SQRLEEKVLAYDKLEKTKNRLQQELDDLTvDLDHQRQIVSN 1466
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDS----PLETFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHGYMK-DIENKIQDGKD 969
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1467 LEKKQKKfdqllAEEKGISARYAEERDRaeaeaREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK 1546
Cdd:TIGR00606 970 DYLKQKE-----TELNTVNAQLEECEKH-----QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1547 NVHELEkskralEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQ---FERDLQTRDEQNEEKK 1612
Cdd:TIGR00606 1040 HLKEMG------QMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQFRDAEEK 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1203-1432 |
8.08e-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: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1203 ALEDETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQV 1282
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1283 QELHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1362
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1363 EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1432
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
867-1398 |
9.63e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.51 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELE 942
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 943 EILHDLESRVEEEEernQILQNEKKKMQAHIQDLEEQLDEEEGARQKL-QLEKVTAEAKIKKMEEEVLLLEDQnsKFIKE 1021
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELeEMTKFKNNKEVELEELKKILAEDE--KLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1022 KKLMEdRIAEcssQLAEEEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1101
Cdd:pfam05483 424 KKQFE-KIAE---ELKGKEQELIFLLQAREKE---IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1102 LKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQedfESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1181
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1182 TTAAQQELRTKREQEVAELKKA---LEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1258
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1259 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAnklQNELDNVSTLLEEAEKKGIKFAKDAaglESQL 1338
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1339 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK 1398
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
881-1411 |
9.82e-09 |
|
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: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 881 ELLKVKEKQTKVEGELEEMERKHQQLLEEKnilAEQLQAETELF----AEAEEMRARLAAKKQELEEILHDLESRVEEEE 956
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 957 ERNQILQNEKKKMQAHIqdleeqldeeegaRQKLQLEKVTAEAKIKKMEEEV-LLLEDQNSKFIKEKKLMEDRIAECSSQ 1035
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKI-------------REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1036 LAEEEEKAKNLAKIRNKQEV---MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKK 1109
Cdd:pfam12128 453 LNQATATPELLLQLENFDERierAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSALDELELQLFPQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1110 ---------------EEELQGALARG---------------------------DDETLHKNNALKVARELQAQIAELQED 1147
Cdd:pfam12128 533 agtllhflrkeapdwEQSIGKVISPEllhrtdldpevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEA 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1148 FESEKASRNKAEKQKRDLSEELEALKTELEDTLDT-----------TAAQQELRTKREQEVAELKKALEDETKNHEAQIQ 1216
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1217 DMRQRHATALEELSEQLEQAKRFK------------ANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR-------KK 1277
Cdd:pfam12128 693 QLDKKHQAWLEEQKEQKREARTEKqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpdviAK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1278 LDAQVQELHAKVSEGDRLRVELAE-----------KANKLQNELDNVSTLLEEAEKKGIKFAKDA----AGLESQL---Q 1339
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTklrrAKLEMERkasE 852
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1340 DTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKnLEKQVLALQSQLADTKKKVDDDLGTIESL 1411
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1569-1951 |
1.41e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1569 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERKQRALAVASKKKME--ID 1646
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ-EELEELEEELEELEAELEELREELEKLEklLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1647 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDY---QRELEEARASRDEIFAQ--------SKESEKKLKSLEAEILQLQE 1715
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1716 ELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1795
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1796 A--------ERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKL-VR 1866
Cdd:COG4717 287 AllflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1867 RTEKKLKEIFMQV----EDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEANEGLSR 1940
Cdd:COG4717 367 ELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEE 446
|
410
....*....|.
gi 1039738673 1941 EVSTLKNRLRR 1951
Cdd:COG4717 447 ELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1606-1810 |
1.60e-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: 59.01 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1606 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEE- 1684
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1685 --------------ARASRDEIFAQSKESEKKLKSLE----------AEILQLQEELASSERARRHAEQERDELADEIAN 1740
Cdd:COG4942 103 keelaellralyrlGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1741 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQ 1810
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1559-1771 |
2.41e-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: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1559 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVA 1638
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1639 SKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELA 1718
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1719 SSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1771
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1130-1333 |
2.60e-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: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1130 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETK 1209
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1210 NHEAQIQDMRQRHATA------------------------LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1265
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1266 QVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAG 1333
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1385-1951 |
3.17e-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: 59.08 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1385 KQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIV 1464
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1465 SNLEKKQKKFDQLLAEEKgisARYAEERD--RAEAEAREKETKALSlarALEEALEAKEEFERQNKQLRadmedlmsSKD 1542
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKALT---GKHQDVTAKYNRRRSKIKEQ--------NNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1543 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaqferdlqtrdEQNEEKKRLllkqvrel 1622
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL--------------------EFNEEEYRL-------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1623 EAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1702
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLL----QLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1703 LKSLEAEILQLQEELASS-----ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR----- 1753
Cdd:pfam12128 515 LEERQSALDELELQLFPQagtllHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1754 ------RLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1827
Cdd:pfam12128 595 waaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1828 AVKSKFKATISALEAKIGQLEEQLeQEAKERAAANKLVRRTEKklKEIFMQVEDERRhaDQYKEQMEKANARMKQLKRQL 1907
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALD--AQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738673 1908 EEAEEEATRANASRrklqrelDDATEANEGLSREVSTLKNRLRR 1951
Cdd:pfam12128 750 KALETWYKRDLASL-------GVDPDVIAKLKREIRTLERKIER 786
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1217-1829 |
3.35e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1217 DMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLR 1296
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1297 VELAEKANKLQNELDNVstlleeaekkgikfakdaaglesqlqdtqellqeetrqklnlsSRIRQLEEEKNSLqeqQEEE 1376
Cdd:PRK01156 256 SEIKTAESDLSMELEKN-------------------------------------------NYYKELEERHMKI---INDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1377 EEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLlkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVD 1456
Cdd:PRK01156 290 VYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1457 LDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalslaraleealeakeeferqnkqLRADMED 1536
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA----------------------------IKKELNE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1537 LMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDE---------LQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ 1607
Cdd:PRK01156 414 INVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1608 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEI-DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQR-ELEEA 1685
Cdd:PRK01156 494 DIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLeDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRtSWLNA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1686 RASRD--EIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEiANSASGKSALLDEKRRLEARIAQLE 1763
Cdd:PRK01156 574 LAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE-ANNLNNKYNEIQENKILIEKLRGKI 652
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1764 EELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV 1829
Cdd:PRK01156 653 DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
926-1759 |
3.88e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 926 EAEEMRARLAAKKQELEEILHDLESRVeeeeernqilqnekKKMQAHIQDLEEQLDEEEGARQKLQL--EKVTAEAKIKK 1003
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMA--------------RELAELNEAESDLEQDYQAASDHLNLvqTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1004 MEEEVLLLEDQnskfiKEKKLMEdrIAECSSQLAEEEEKAKnlakiRNKQEV-----MISDLEERLKkEEKTR------- 1071
Cdd:PRK04863 353 YQADLEELEER-----LEEQNEV--VEEADEQQEENEARAE-----AAEEEVdelksQLADYQQALD-VQQTRaiqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1072 -QELEKAKRKL---DGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETlhknNALKVARELQAQIaELQED 1147
Cdd:PRK04863 420 vQALERAKQLCglpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEV-SRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1148 FESEKASRNKAEKQkRDLSEELEALKTELEDtldttaAQQELRTKREQE--VAELKKALEdETKNHEAQIQDMRQRHATA 1225
Cdd:PRK04863 495 WDVARELLRRLREQ-RHLAEQLQQLRMRLSE------LEQRLRQQQRAErlLAEFCKRLG-KNLDDEDELEQLQEELEAR 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1226 LEELSEQLEQAkrfkanleknkqgletdnkelacevkvlQQVKAESEHKRKKLDAQVQELHAKVSEGdrlrVELAEKANK 1305
Cdd:PRK04863 567 LESLSESVSEA----------------------------RERRMALRQQLEQLQARIQRLAARAPAW----LAAQDALAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1306 LQneldnvstlleeaEKKGIKFAkDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEK 1385
Cdd:PRK04863 615 LR-------------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1386 QVLA-LQSQLADtkkkvD---DDLGTIES-------------LEEAKKKLLKD---------VEALSQRLEEKVLAYDKL 1439
Cdd:PRK04863 681 RFGGvLLSEIYD-----DvslEDAPYFSAlygparhaivvpdLSDAAEQLAGLedcpedlylIEGDPDSFDDSVFSVEEL 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1440 EKT--------------------------KNR---LQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAE 1490
Cdd:PRK04863 756 EKAvvvkiadrqwrysrfpevplfgraarEKRieqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADP 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1491 ERDRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelekskRALEQQVEEMRTQL 1569
Cdd:PRK04863 836 EAELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ETLADRVEEIREQL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1570 EELEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELeaeleDERKQRALAVASKKKM 1643
Cdd:PRK04863 904 DEAEEAkrfVQQHGNALAQLEpivSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TEVVQRRAHFSYEDAA 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1644 EIDLKD------LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaeiLQLQEEL 1717
Cdd:PRK04863 978 EMLAKNsdlnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG---VPADSGA 1054
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1039738673 1718 AssERARRHaeqeRDELADEIANSASGKSALLDEKRRLEARI 1759
Cdd:PRK04863 1055 E--ERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1463-1933 |
4.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1463 IVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskd 1542
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1543 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE-VNMQAMKAQFERDLQTRDEQNEEKKRL--LLKQV 1619
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEELEELLEQLSLATEEELqdLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1620 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQM-------------KDYQRELEEAR 1686
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAaallallglggslLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1687 ASRDEIFAQSKESEKKLKsleAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1766
Cdd:COG4717 280 FLVLGLLALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1767 EEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSdNARQQLERQNKELKAKLQELEGAVKSKFKA-TISALEAKIG 1845
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1846 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQ 1925
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
....*...
gi 1039738673 1926 RELDDATE 1933
Cdd:COG4717 516 PVLERASE 523
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1541-1761 |
4.74e-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: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1541 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVR 1620
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1621 ELEAELEDERKQRALAVASKKKMEID--LKDLEAQIEAANKARDEVIK-------QLRKLQAQMKDYQREL-EEARASRD 1690
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1691 EIFAQSKESEKKLKSLEAEILQLQEELAS-SERARRHAEQERD-ELADEIANSasgksaLLdeKRRLEARIAQ 1761
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1486-1858 |
5.52e-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: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1486 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1565
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1566 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQVRELEAELEDERKQRALAVASKKkmei 1645
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1646 dlkdLEAQIEAANKARDEVIKQLRKL-QAQMKDYQRE--LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1722
Cdd:pfam07888 201 ----LAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1723 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERsaaq 1802
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK---- 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1803 ksDNARQQL---ERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKER 1858
Cdd:pfam07888 353 --DCNRVQLsesRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1093-1393 |
6.05e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.00 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1093 AELQAQVDELKVQltKKEEELQGALARGDDETLhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL 1172
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTL----------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1173 KTELEDTLDTTAAQQELR------TKREQEVAELKKALeDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKN 1246
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRqlesrlAQTLDQLQNAQNDL-AEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1247 KQGLETDNK-ELACEvkvLQQVKAESEHKRKKLDA--QVQELhakvseGDRLRVELAEKANKLQNELdnvsTLLEEA--E 1321
Cdd:PRK11281 186 GKALRPSQRvLLQAE---QALLNAQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL----QLLQEAinS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1322 KKGIKFAKDAAGLESQlQDTQE-----LLQEETRQKLNLSSRIRQLEEEKNSLQeqqeeeeeaRKNLE-KQVL--ALQSQ 1393
Cdd:PRK11281 253 KRLTLSEKTVQEAQSQ-DEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLT---------QQNLRvKNWLdrLTQSE 322
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
866-1238 |
6.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 866 LQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEL---- 941
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 942 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1021
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1022 KK---------------LMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1086
Cdd:COG4717 271 LIltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1087 DLQDQIAELQAQVdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQkrdls 1166
Cdd:COG4717 351 ELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA----- 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1167 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEaqIQDMRQRHATALEELSEQLEQAKR 1238
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1379-1642 |
7.20e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1379 ARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTvdld 1458
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1459 hqrqivSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1538
Cdd:COG4942 83 ------AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1539 SSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRlLLKQ 1618
Cdd:COG4942 157 ADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEAL 228
|
250 260
....*....|....*....|....
gi 1039738673 1619 VRELEAELEDERKQRALAVASKKK 1642
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
873-1863 |
7.38e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.14 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 873 EELQAK-DEELLKVKEKQTK-VEGELEEMERKHQQLLEekNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 950
Cdd:TIGR01612 699 DDLKSKiDKEYDKIQNMETAtVELHLSNIENKKNELLD--IIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 951 RveeeeernqilQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIA 1030
Cdd:TIGR01612 777 E-----------KDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1031 ECSSQLAEEEEKAK--------NLAKIRNKQEVMISD----------------LEERLKKEEKTRQELEKAKrKLDG--- 1083
Cdd:TIGR01612 846 NKVDKFINFENNCKekidseheQFAELTNKIKAEISDdklndyekkfndskslINEINKSIEEEYQNINTLK-KVDEyik 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1084 --ETTdlQDQIAELQAQVDELKVQLTKKEEELQgalargDDETLHKNNALKVARELQAQIAELQEDFEseKASRNKAEKQ 1161
Cdd:TIGR01612 925 icENT--KESIEKFHNKQNILKEILNKNIDTIK------ESNLIEKSYKDKFDNTLIDKINELDKAFK--DASLNDYEAK 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1162 KRDLSEELEALKTELEDTLDTTAAQQelRTKREQEVAELKKALEDETKNheaqIQDMRQRHATALEELSEQLEqaKRFKA 1241
Cdd:TIGR01612 995 NNELIKYFNDLKANLGKNKENMLYHQ--FDEKEKATNDIEQKIEDANKN----IPNIEIAIHTSIYNIIDEIE--KEIGK 1066
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1242 NLEK-NKQGLETDNKELACEVKVLQQVK------------AESEHKRKKLDAQVQELHAKVsegDRLRVELAEKANKLQN 1308
Cdd:TIGR01612 1067 NIELlNKEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINKIKDDIKNLDQKI---DHHIKALEEIKKKSEN 1143
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1309 ELDNVSTLLEEAEKKGIK--FAKDAAGLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNSLQEQQEEEEEAR 1380
Cdd:TIGR01612 1144 YIDEIKAQINDLEDVADKaiSNDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYG 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1381 KNLEKQVLalqSQLADTKKKVDDdlgTIESLEeAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDD----LTVD 1456
Cdd:TIGR01612 1221 KNLGKLFL---EKIDEEKKKSEH---MIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDdkdhHIIS 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1457 LDHQRQIvSNLEKKQKKFDQLLAEEKGIS------ARYAEERDRAEAEAREKETKALSLARALEEALEakeeferqnKQL 1530
Cdd:TIGR01612 1294 KKHDENI-SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDINLYLNEIANIYNILKLNKI---------KKI 1363
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1531 RADMEDLMSSKDDVGKNVH-ELEKSKRALEQQVEEmrTQLEELEDELQATEDAKLRLEV--NMQAMKAQF---ERDLQT- 1603
Cdd:TIGR01612 1364 IDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDD--INLEECKSKIESTLDDKDIDECikKIKELKNHIlseESNIDTy 1441
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1604 --RDEQNEEKKRLLLKQVreleaELEDERKQRALAVA---SKKKMEIDLKDLEAQIEAANKARDEV---IKQLRKLQAQM 1675
Cdd:TIGR01612 1442 fkNADENNENVLLLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELF 1516
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1676 KDYQRE---------------------------LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAE 1728
Cdd:TIGR01612 1517 EQYKKDvtellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAI 1596
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1729 QERDELAD------EIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellndrfrkTTLQVDTLNTELAAERSAAQ 1802
Cdd:TIGR01612 1597 DIQLSLENfenkflKISDIKKKINDCLKETESIEKKI-----------------------SSFSIDSQDTELKENGDNLN 1653
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1803 KSDNARQQLERQNKELKAKLQELEGaVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1863
Cdd:TIGR01612 1654 SLQEFLESLKDQKKNIEDKKKELDE-LDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
891-1354 |
8.36e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 891 KVEGELEEMERKHQQLLEeknILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdLESRVEEEEERNQILQNEKKKMQ 970
Cdd:COG4717 50 RLEKEADELFKPQGRKPE---LNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 971 AHIqdleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR 1050
Cdd:COG4717 123 KLL------------QLLPLYQELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1051 NKQEvmisdlEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE------------------ 1112
Cdd:COG4717 187 SLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaalla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1113 LQGALARGDDETLHKNNAL---------------KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1177
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1178 DTLDTTAAQQELRTKREQEVAELKKAledetKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQ-----GLET 1252
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEEleeqlEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1253 DNKELACEVKVLQQVKAESEHKRKKLDA---QVQELHAKVSEgDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAK 1329
Cdd:COG4717 416 GELEELLEALDEEELEEELEELEEELEEleeELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|....*
gi 1039738673 1330 DAAGLESqLQDTQELLQEETRQKLN 1354
Cdd:COG4717 495 LKLALEL-LEEAREEYREERLPPVL 518
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1277-1831 |
9.10e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1277 KLDAQVQELHAKVSEGDRLRVELAEKanklQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQ---DTQELLQEETRQKL 1353
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSS----NLELENIKKQIADDEKSHSITLKEIERLSIEYNnamDDYNNLKSALNELS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1354 NLSSRIRQLEEE---KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLE 1430
Cdd:PRK01156 246 SLEDMKNRYESEiktAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1431 E--KVLA--------YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1500
Cdd:PRK01156 326 AiiKKLSvlqkdyndYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1501 EketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL---------------EKSKRALEQQVEE- 1564
Cdd:PRK01156 406 A-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeEKSNHIINHYNEKk 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1565 --MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKkRLLLKQVRELEAELEDERKQRALAVASKKK 1642
Cdd:PRK01156 479 srLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1643 MeiDLKDLEAQ---------------IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFaqsKESEKKLKSLE 1707
Cdd:PRK01156 558 L--KLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI---REIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1708 AEILQLQEELASSERARRHAEQERDELAdeiansasGKSALLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTLQV 1787
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND--------------IEDNLKKSRKAL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738673 1788 DTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKS 1831
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
895-1119 |
9.20e-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: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 895 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIq 974
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 975 dleeqldeeegARQKLQLEKVTAEA-KIKKMEEEVLLLEDQN-SKFIKEKKLME-------DRIAECSSQLAEEEEKAKN 1045
Cdd:COG4942 100 -----------EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKylaparrEQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1046 LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1119
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1298-1929 |
1.54e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.65 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1298 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNSLQEQQEE 1375
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1376 EEEA-----RKNLEKQVLALQSQLADTKK-------KVDDDLGTIESLEEAKKKLLKDVEAlsqrlEEKVLAYDKLEKtk 1443
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEINDKEK-----QVSLLLIQITEK-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1444 nrlQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerDRAEAEAREKETKALSLARALEEALEAKEEF 1523
Cdd:pfam05483 253 ---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI----------EKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1524 ERQNKQL-------RADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAM 1593
Cdd:pfam05483 320 QIATKTIcqlteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1594 KAQFERDLQTRDEQNEEKKRLLL--KQVRELEAELEDERKQRALAVASKKKmeiDLKDLEAQIEAANKARDEVIKQLRKL 1671
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1672 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERarrhaeqERDELADEIANSASGKSALLDE 1751
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK-------QEERMLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1752 krrLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELaaeRSAAQKSDNARQQLERQNKELKaKLQELEGAVKS 1831
Cdd:pfam05483 550 ---LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM---KILENKCNNLKKQIENKNKNIE-ELHQENKALKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1832 KFKA---TISALEAKIGQLEEQLEqeakerAAANKLVRRTEKKLKEIfmqvEDERRHADQYKEQMEKANARMKQLKrqle 1908
Cdd:pfam05483 623 KGSAenkQLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV---- 688
|
650 660
....*....|....*....|.
gi 1039738673 1909 eaeeeatranasrrKLQRELD 1929
Cdd:pfam05483 689 --------------KLQKEID 695
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1419-1951 |
1.56e-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: 56.98 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1419 LKDVEALSQRLEE------KVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEE------KGISA 1486
Cdd:TIGR00606 165 LSEGKALKQKFDEifsatrYIKALETLRQVRQTQGQKVQEHQMELKYLKQ---YKEKACEIRDQITSKEaqlessREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1487 RYAEERDRAEAEAREKE---TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK-RALEQQV 1562
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1563 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER-------------DLQTRDEQNEEKKRLLLKQVRELEAELEDE 1629
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehirardsliqSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1630 RKQRALAVASKKKMEIDLKDLEAQiEAANKARDEVI----------KQLRKLQAQMKDYQRELEEARASRDEIFAQSKES 1699
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKglgrtielkkEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1700 EKKLKSL------------EAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEK-RRLEARIAQ 1761
Cdd:TIGR00606 481 RKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmeMLTKDKMDKDEQiRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1762 LEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVkskFKATIS-AL 1840
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---FDVCGSqDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1841 EAKIGQLEEQLEQEAKERA---AANKL---------------------VRRTEKKLKEIFMQVEDERRHADQYKEQMEKA 1896
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAmlaGATAVysqfitqltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESE 717
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1897 NARMKqlKRQLEEAEEEATRANASRRKlQRELDDATEANEGLSREVSTLKNRLRR 1951
Cdd:TIGR00606 718 LKKKE--KRRDEMLGLAPGRQSIIDLK-EKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1298-1945 |
1.72e-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: 56.77 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1298 ELAEKANKLQNELDNVSTLleEAEKKGIKFA-KDAAGLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNSLQEQQEEE 1376
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESA--ELRLSHLHFGyKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1377 EEARKNLEKQVLALQSQLadtKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQElddltVD 1456
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH---GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSK-----IK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1457 LDHQRQIVSNLEKKQKKFD----QLLAEEKGISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQ 1529
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREardrQLAVAEDDLQALESELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1530 LRADMEDLMSSKDDVGKNVHELEKSKRAL-----------------EQQVEEMRTQLEELEDELQA----------TEDA 1582
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasealrqaSRRLEERQSALDELELQLFPqagtllhflrKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1583 KLRLEVNMQAMKAQFER--------DLQTRDEQNEEKKRLLLKQVRELE-AELEDERKQRAlavaskKKMEIDLKDLEAQ 1653
Cdd:pfam12128 546 DWEQSIGKVISPELLHRtdldpevwDGSVGGELNLYGVKLDLKRIDVPEwAASEEELRERL------DKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1654 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQsKESEKklksleaeiLQLQEELassERARRHAEQERDE 1733
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE-KQSEK---------DKKNKAL---AERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1734 LADEIANSASGKSALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTLQVDTLNTELAAERSAAqksDNARQQL 1811
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGA---KAELKAL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1812 ERQNK-ELKAKLQELEgavkskfkaTISALEAKIGQLEEQLEQEAKERAAanklVRRTEKKLKEIFMQvederrHADQYK 1890
Cdd:pfam12128 753 ETWYKrDLASLGVDPD---------VIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLA 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1891 EQMEKANARMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTL 1945
Cdd:pfam12128 814 TQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1150-1389 |
1.78e-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: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1150 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALedetKNHEAQIQDMRQRHATALEEL 1229
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1230 SEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1309
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1310 LDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLA 1389
Cdd:COG4942 173 RAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1549-1945 |
2.26e-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: 56.50 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1549 HELEKSKRAL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQfERDLQTRDEQNEEKKRLllkq 1618
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQ-EKIERYQEDLEELTERL---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1619 vRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEviKQLRKLQAQMKdyQRELEEARA-------SRDE 1691
Cdd:COG3096 364 -EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV--QQTRAIQYQQA--VQALEKARAlcglpdlTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1692 IFAQSKESEKKLKSLEAEILQLQEELASSERARR---HAEQERDELADEIANSASGKSA--LLDEKRRLEARIAQleeel 1766
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTAreLLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1767 eeeqsnmellndrfrkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQ 1846
Cdd:COG3096 514 --------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1847 LEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHA--------------DQYKEQMEKANARMKQLKRQLEEAee 1912
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqdalerlrEQSGEALADSQEVTAAMQQLLERE-- 639
|
410 420 430
....*....|....*....|....*....|...
gi 1039738673 1913 eatranasrRKLQRELDDATEANEGLSREVSTL 1945
Cdd:COG3096 640 ---------REATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1342-1585 |
2.70e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1342 QELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1420
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1421 DVEALSQRLEEKVLAYDKLEKTKNRL----QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1496
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1497 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlmsskddvgknvhELEKSKRALEQQVEEMRTQLEELEDEL 1576
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELA--------------ELQQEAEELEALIARLEAEAAAAAERT 243
|
....*....
gi 1039738673 1577 QATEDAKLR 1585
Cdd:COG4942 244 PAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1528-1744 |
3.22e-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: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1528 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFeRDLQTRDEQ 1607
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERA-RALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1608 NEEKKRLL--------LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1679
Cdd:COG3883 102 VSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1680 RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASG 1744
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1061-1332 |
5.54e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1061 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQ 1140
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---------------------KLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1141 IAELQEDFESEKA---SRNKAEKQKRDLSEELEALK--TELEDTLDTTAAqqelrtkreqevaelkkaledetknheaqI 1215
Cdd:COG3883 74 IAEAEAEIEERREelgERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-----------------------------L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1216 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRL 1295
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039738673 1296 RVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAA 1332
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1313-1886 |
6.19e-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: 54.75 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1313 VSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNslqeqqEEEEEARKNLEKQVLALQS 1392
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREA------EAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1393 QLADTKKKVDDDLgTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQK 1472
Cdd:pfam05557 85 LEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1473 kfdqllaeekgisaryaeerDRAEAEAREKETKalslARALEEALEAKEEFERQNKQLR-ADMEDLMSSKDDVGKNVHEL 1551
Cdd:pfam05557 164 --------------------SLAEAEQRIKELE----FEIQSQEQDSEIVKNSKSELARiPELEKELERLREHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1552 EKSKRALEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKAQFE---------RDLQTRDEQNEEKKRLLLKQV 1619
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSWVKLAQdtglnlrspEDLSRRIEQLQQREIVLKEEN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1620 RELEAELEDERKQRalavaskKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQS 1696
Cdd:pfam05557 300 SSLTSSARQLEKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1697 KESEKKLKSLE--AEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNME 1774
Cdd:pfam05557 373 NYSPQLLERIEeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1775 LL--NDRFR--KTTLQVDTLNTELAAERSAA-----QKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1845
Cdd:pfam05557 453 LEleRQRLReqKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738673 1846 QLEEQLEQEAKERAAANKLVRRTEKK---LKEIFMQVEDERRHA 1886
Cdd:pfam05557 533 LPETTSTMNFKEVLDLRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
871-1094 |
6.37e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 871 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELEEILH 946
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 947 DLESRVEEEEERNQILQnekKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEevllLEDQNSKFIKEKKLME 1026
Cdd:COG4942 98 ELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1027 DRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1094
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1071-1934 |
9.05e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1071 RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALARgddetLHK-NNAL----KVAR------ELQA 1139
Cdd:PRK04863 292 RRELYTSRRQLAAE----QYRLVEMARELAELNEAESDLEQDYQAASDH-----LNLvQTALrqqeKIERyqadleELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1140 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALE---------DETKN 1210
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1211 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEH-KRKKLDAQVQELHAKV 1289
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1290 SEGDRlRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1369
Cdd:PRK04863 523 SELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1370 qeqqeeeeeaRKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQrleekvlAYDKLEKTKNRL 1446
Cdd:PRK04863 595 ----------IQRLAARApawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV-------ERDELAARKQAL 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1447 QQELDDL----TVDLDHQRQI--------VSNLekkqkkFDQLLAEEKG-ISARYAEER------DraeaeareketkaL 1507
Cdd:PRK04863 658 DEEIERLsqpgGSEDPRLNALaerfggvlLSEI------YDDVSLEDAPyFSALYGPARhaivvpD-------------L 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1508 SLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEKS----------------------KRALE 1559
Cdd:PRK04863 719 SDAA-------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAARE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1560 QQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEEKKRLLLKQVRELEAELED----E 1629
Cdd:PRK04863 786 KRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1630 RKQRALAVASKKKMEiDLKDLEAQIEAAnkARDEVIKQLRKLQAQMKdyqrELEEARASRDE---IFAQSKESEKKLKSL 1706
Cdd:PRK04863 861 QQQRSQLEQAKEGLS-ALNRLLPRLNLL--ADETLADRVEEIREQLD----EAEEAKRFVQQhgnALAQLEPIVSVLQSD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1707 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAllDEKRRLEAriaqleeeleeEQSNMELLNDRFRKTTLQ 1786
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAK-----------NSDLNEKLRQRLEQAEQE 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1787 VDTLNTELaaeRSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKlvr 1866
Cdd:PRK04863 1001 RTRAREQL---RQAQAQLAQYNQVLASLKSSYDAKRQMLQ------------ELKQELQDLGVPADSGAEERARARR--- 1062
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1867 rtekklKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaeeeatranasrRKLQRELDDATEA 1934
Cdd:PRK04863 1063 ------DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL--------------RKLERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1053-1510 |
1.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1053 QEVMISDLEERLKKEektRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQlTKKEEELQGALARGDDETLHKNNALK 1132
Cdd:COG4717 40 LAFIRAMLLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1133 VARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1212
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1213 AQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1292
Cdd:COG4717 192 EELQDLAEE----LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1293 DRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLS-----SRIRQLEEEKN 1367
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1368 SLQEQQEEEEEARKNLEKQVL--ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK--TK 1443
Cdd:COG4717 348 ELQELLREAEELEEELQLEELeqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1444 NRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL--AEEKGISARYAEERDRAEAEAREKETKALSLA 1510
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1550-1828 |
1.32e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRdeQNEEKKRLL-----------L 1616
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELerirqeeiameI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1617 KQVRELE--------------AELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1682
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1683 EEARASRDEIFAQsKESEKKLKSLEAEILQLQEELASSERaRRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1762
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1763 EEELEEEQSNMELLNDRFRKTTLQVDTLNTElaaERSAAQKSDNARQQLeRQNKELKAKLQELEGA 1828
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1081-1323 |
1.55e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1081 LDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlhKNNALKVARELQ---AQIAELQEDFESEKASRNK 1157
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ--------KNGLVDLSEEAKlllQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1158 AEKQKRDLSEELEALKTELEDTLDTTAAQQeLRTKREQEVAELKKALEDETKNHEaQIQDMRQRhataLEELSEQLEQ-A 1236
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSARYTPNHP-DVIALRAQ----IAALRAQLQQeA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1237 KRFKANLEKNKQGLETdnkelacevkvlqqvkaesehKRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTL 1316
Cdd:COG3206 312 QRILASLEAELEALQA---------------------REASLQAQLAQLEARLAELPELEAELRR----LEREVEVAREL 366
|
....*..
gi 1039738673 1317 LEEAEKK 1323
Cdd:COG3206 367 YESLLQR 373
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
872-1284 |
1.58e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 872 EEELQAKDEELLKVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 949
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 950 SrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR- 1028
Cdd:COG4717 174 E---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1029 -------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQElEKAKRKLDGETTDLQDQiaELQAQVDE 1101
Cdd:COG4717 251 llliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK-EAEELQALPALEELEEE--ELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1102 LKVQLTKKEEELQGALARGDDetlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1181
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEE-----------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1182 TTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelacev 1261
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE------ 470
|
410 420
....*....|....*....|...
gi 1039738673 1262 kvLQQVKAESEHKRKKLDAQVQE 1284
Cdd:COG4717 471 --LAELLQELEELKAELRELAEE 491
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1068-1345 |
1.77e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.23 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1068 EKTRQeLEKAKRKLDGETTDLQDQ---------------IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALK 1132
Cdd:pfam00038 18 DKVRF-LEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1133 VARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTEledtldttaaqqelrtkREQEVAELKKALEDETKNHE 1212
Cdd:pfam00038 97 LRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1213 ---AQIQDMrqrhATALEELSEQLE-QAKRFKANLEKN-KQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1287
Cdd:pfam00038 160 mdaARKLDL----TSALAEIRAQYEeIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1288 KVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiKFAKDAAGLESQLQDTQELL 1345
Cdd:pfam00038 236 LKKQKASLERQLAETEERYELQLADYQELISELEA---ELQETRQEMARQLREYQELL 290
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1621-1867 |
2.01e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1621 ELEAELeDERKQRALAVASKKKMEIDLK---DLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1697
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1698 ES------EKKLKSLEAEILQLQEELAS-----------SERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1756
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1757 ARIAQleeeleeeqsnMELLNDrFRKTTLQVDTLNTELAAER----SAAQksdnarQQLERQnkelkakLQELEGAVKSK 1832
Cdd:PRK11281 199 AEQAL-----------LNAQND-LQRKSLEGNTQLQDLLQKQrdylTARI------QRLEHQ-------LQLLQEAINSK 253
|
250 260 270
....*....|....*....|....*....|....*
gi 1039738673 1833 fkatisALEAKIGQLEEQLEQEAKERAAANKLVRR 1867
Cdd:PRK11281 254 ------RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1560-1937 |
2.87e-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: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1560 QQVEEMRTQLEELEDELQATEDAKLRL---EVNMQAMKAQFERDLQTRDEQNEEKK---RLLLKQVRELEAELEDERKQR 1633
Cdd:pfam12128 234 AGIMKIRPEFTKLQQEFNTLESAELRLshlHFGYKSDETLIASRQEERQETSAELNqllRTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1634 ALAVAsKKKMEIDLkdLEAQIEAANKARDEVIK----QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS-LEA 1708
Cdd:pfam12128 314 DAAVA-KDRSELEA--LEDQHGAFLDADIETAAadqeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1709 EILQLQEELASS--ERARRHAEQE----------RDELADEIANSASG----KSALLDEKRRLEARIAQLEEELEEEQSN 1772
Cdd:pfam12128 391 DIAGIKDKLAKIreARDRQLAVAEddlqaleselREQLEAGKLEFNEEeyrlKSRLGELKLRLNQATATPELLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1773 MEL--LNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatiSALEAKIGQLEEQ 1850
Cdd:pfam12128 471 ERIerAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE-----------LQLFPQAGTLLHF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1851 LEQEAKE------RAAANKLVRRTEK--------------------KLKEI----FMQVEDE-RRHADQYKEQMEKANAR 1899
Cdd:pfam12128 540 LRKEAPDweqsigKVISPELLHRTDLdpevwdgsvggelnlygvklDLKRIdvpeWAASEEElRERLDKAEEALQSAREK 619
|
410 420 430
....*....|....*....|....*....|....*...
gi 1039738673 1900 MKQLKRQLEEaeeeatrANASRRKLQRELDDATEANEG 1937
Cdd:pfam12128 620 QAAAEEQLVQ-------ANGELEKASREETFARTALKN 650
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1694-1933 |
3.33e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1694 AQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDeladeIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNM 1773
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1774 ELLNDRFRKTTLQVDTLNtelaaersaaqkSDNARQQLERQNKELKAKLQELEgavkSKFKA---TISALEAKIGQLEEQ 1850
Cdd:COG3206 243 AALRAQLGSGPDALPELL------------QSPVIQQLRAQLAELEAELAELS----ARYTPnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1851 LEQEAKERAAanklvrrtekklkEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEaeeeatranasRRKLQRELDD 1930
Cdd:COG3206 307 LQQEAQRILA-------------SLEAELEALQAREASLQAQLAQLEARLAELPELEAE-----------LRRLEREVEV 362
|
...
gi 1039738673 1931 ATE 1933
Cdd:COG3206 363 ARE 365
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1610-1905 |
3.51e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1610 EKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR 1689
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1690 DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKsALLDEKRRLEARIAQLEEELEEE 1769
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1770 QSNMELLNdRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELegavkskfKATISALEAKIGQLEE 1849
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1850 QLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRHADQyKEQMEKANARMKQLKR 1905
Cdd:COG1340 231 EIIELQKE-------LRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1595-1933 |
4.06e-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: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1595 AQFERDLQ-TRDEQNEEKKRLL-----LKQVRELEAELEDE---------RKQRALAVASK-KKMEIDLKDLEAQIEAAN 1658
Cdd:COG3096 288 LELRRELFgARRQLAEEQYRLVemareLEELSARESDLEQDyqaasdhlnLVQTALRQQEKiERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1659 KARDEVIKQLRKLQAQmkdyqreLEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR-------HAEQER 1731
Cdd:COG3096 368 EVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcglpdlTPENAE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1732 DELADEIANSASGKSALLDEKRRLeariaqleeeleeeqSNMELLNDRFRKTtLQvdtLNTELAAERSAAQKSDNARQQL 1811
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKL---------------SVADAARRQFEKA-YE---LVCKIAGEVERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1812 eRQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqvederrHADQYKE 1891
Cdd:COG3096 502 -RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----------AAEELEE 557
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039738673 1892 QMEKANARMKQLKRQLEeaeeeatRANASRRKLQRELDDATE 1933
Cdd:COG3096 558 LLAELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRA 592
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
930-1391 |
4.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 930 MRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVL 1009
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1010 LLED--QNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNkqevmisDLEERLKKEEKTRQELEKAKRKLDGET-- 1085
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-------ELEELEAELAELQEELEELLEQLSLATee 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1086 --TDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDD-----ETLHKNNALKVARELQAQIAELQEdFESEKASRNKA 1158
Cdd:COG4717 193 elQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlenelEAAALEERLKEARLLLLIAAALLA-LLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1159 EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKR 1238
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1239 FKANLEKNKQGLETDNKELACEvKVLQQVKAESEHKRKKLDAQVQELHAkvsegdrLRVELAEKANKLQNELDNVSTLLE 1318
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQE-------LKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1319 EAEKKGIKfaKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKN--SLQEQQEEEEEARKNLEKQVLALQ 1391
Cdd:COG4717 424 ALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
872-1458 |
4.17e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 872 EEELQAKDEELLKVKE-------KQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 944
Cdd:PRK01156 189 EEKLKSSNLELENIKKqiaddekSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 945 LHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ---LEKVTAEAKIKKMEEevllLEDQNSKFIKE 1021
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1022 KKLMEDRIAECS----------SQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1091
Cdd:PRK01156 345 KSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1092 IAELQAQVDELKVQLTKKEEELQGALAR----------GDDETLH--------KNNALKVARELQAQIAELQEDFESEKA 1153
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlGEEKSNHiinhynekKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1154 SRNKAEKQKRDLSE----ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATALEE 1228
Cdd:PRK01156 505 RKEYLESEEINKSIneynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1229 LSEQLEQAKRFKANLEKNKQGLETDnkelacevkvLQQVKAESEHKRKKLDAQVQELHAKVsegdrlrvelaekanklqN 1308
Cdd:PRK01156 585 NRSRSNEIKKQLNDLESRLQEIEIG----------FPDDKSYIDKSIREIENEANNLNNKY------------------N 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1309 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEllqeetrqklnLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1388
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-----------ITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1389 ALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDV-EALSQ-------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLD 1458
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKKAIgdLKRLrEAFDKsgvpamiRKSASQAMTSLTRKYLFEFNLDFDDIDVDQD 785
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1092-1348 |
4.34e-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: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1092 IAELQAQVDELKVQLTKKEEElQGALArgdDETLHKNNALKVARELQAQIAEL---QEDFES--EKASRNKAEKQKRDLS 1166
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAA-QNALA---DKERAEADRQRLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1167 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKALE---DETKNH-EAQIQDMRQRHATALEELSEQLE 1234
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1235 QAKRFKANLEKNKQGLETDNKelacevkvlqqvKAESEHKRKKLDAQVQELHAKVSEGDrlrvelaekanklqneldnVS 1314
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAESD-------------------AN 1741
|
250 260 270
....*....|....*....|....*....|....*
gi 1039738673 1315 TLLEEAEKKGIKFAKDAAGLESQLQ-DTQELLQEE 1348
Cdd:NF012221 1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
823-1320 |
5.05e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 823 ARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWWRVFTKVKpLLQ--VTRQEEELQAKDEELLKVKEKQ 889
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 890 TKV-----------------------------EGELEEMERKHQQLLEekniLAEQLQAETELFAEA-EEMRARLAAKKQ 939
Cdd:COG4913 319 DALreeldeleaqirgnggdrleqlereierlERELEERERRRARLEA----LLAALGLPLPASAEEfAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 940 ELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLeeqldeeegARQKLQLEKvtAEAKIKKMEEEVLLLEDQNSKFI 1019
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASL---------ERRKSNIPA--RLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1020 KEkkLMEDRIAECSSQLAEE-------------EEKAKNLAKI--RNKQEVMISDLEERLKKEEKTRQELEKAK--RKLD 1082
Cdd:COG4913 464 GE--LIEVRPEEERWRGAIErvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPDSlaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1083 GETTDLQDQI-AELQAQVDELKVQltkKEEELQ---------------GALARGDDETLHK-------NNALKVAReLQA 1139
Cdd:COG4913 542 FKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitragqvkgnGTRHEKDDRRRIRsryvlgfDNRAKLAA-LEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1140 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE---DTLDTTAAQQELRTKrEQEVAELKKAlEDETKNHEAQIQ 1216
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAEL-EAELERLDAS-SDDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1217 DMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgDRLR 1296
Cdd:COG4913 696 ELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLEERFAAALGDAVE-RELR 768
|
570 580
....*....|....*....|....
gi 1039738673 1297 VELAEKANKLQNELDNVSTLLEEA 1320
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1413-1663 |
7.01e-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: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1413 EAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKkfdqllaeekgisaryAEER 1492
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----------------ALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1493 DRAEAEAREKETKAlSLARALEEALEAKEEFERQNKQLRADMedLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLE 1570
Cdd:COG4942 84 ELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDflDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1571 ELE---DELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRL--LLKQVRELEAELEDERKQRALAVASKKKMEI 1645
Cdd:COG4942 161 ELAalrAELEAERAELEAL-----------------LAELEEERAALeaLKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*...
gi 1039738673 1646 DLKDLEAQIEAANKARDE 1663
Cdd:COG4942 224 ELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1636-1803 |
7.29e-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: 49.54 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1636 AVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQE 1715
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1716 ELASSERARrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1795
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*...
gi 1039738673 1796 AERSAAQK 1803
Cdd:COG1579 156 AELEELEA 163
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1138-1357 |
7.70e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1138 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQD 1217
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1218 MRQ--RHATALEEL--SEQLEQakrFKANLEKNKQGLETDNKELacevKVLQQVKAESEHKRKKLDAQVQELHAKVSEGD 1293
Cdd:COG3883 95 LYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1294 RLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSS 1357
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1421-1677 |
8.49e-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: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1421 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLD--HQRQIVS--NLEKKQKKFDQllAEEKGISARYAEERDRAE 1496
Cdd:pfam05667 227 NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTeaTSGASRSaqDLAELLSSFSG--SSTTDTGLTKGSRFTHTE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1497 AEAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1574
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVETEEELQQQREEEleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1575 ELQATEDAKLRL---EVNMQAMKAQFE---RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQralavASKKKMEI-DL 1647
Cdd:pfam05667 385 QYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE-----SQRKLEEIkEL 459
|
250 260 270
....*....|....*....|....*....|
gi 1039738673 1648 KDLEAQIEAANKARDEVIKQlrkLQAQMKD 1677
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1528-1747 |
8.92e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1528 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDEL-------QATEDAKLRLEV------------ 1588
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralYRSGGSVSYLDVllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1589 NMQAMKAQFERDLQTRDEQNEEKKRLllkqvRELEAELEDERKQralAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1668
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAEL-----EAKKAELEAKLAE---LEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1669 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA 1747
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1026-1237 |
1.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1026 EDRIAECSSQLAEEEEKAKNLakirnKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ 1105
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1106 LT--KKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAlktELEDTLDTT 1183
Cdd:COG3206 256 LPelLQSPVIQQLRAQ--------------LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ---EAQRILASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1184 AAQQELRTKREQEVAELKKALEDETKN---HEAQIQDMRQRHATA---LEELSEQLEQAK 1237
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVArelYESLLQRLEEAR 378
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1414-1680 |
1.08e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1414 AKKKLLKDVealsqrLEEKVLA-YDKLEKTKNR-LQQELDDLTVDLDH-QRQIVS--------------NLEKKQKKFDQ 1476
Cdd:PHA02562 151 ARRKLVEDL------LDISVLSeMDKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1477 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadmedlMSSKDDV----GKNVHELE 1552
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIK------MYEKGGVcptcTQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1553 KSKRALEQQVEEMRTQLEELEDELQatEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEderkq 1632
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIE----- 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039738673 1633 ralavaskkKMEIDLKDLEAQIEAANKARDEVIKQLRKLqaQMKDYQR 1680
Cdd:PHA02562 369 ---------ELQAEFVDNAEELAKLQDELDKIVKTKSEL--VKEKYHR 405
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1227-1876 |
1.16e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1227 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSegdRLRVELAEKA--- 1303
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS---AQRVELAERQlqe 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1304 NKLQN-ELDNVSTLLEEAEKKGIKFAKDaaglesqlqdTQELLQEETRQKLNLSSRirqLEEEKNSLQEQQEEEEEARKN 1382
Cdd:COG5022 887 LKIDVkSISSLKLVNLELESEIIELKKS----------LSSDLIENLEFKTELIAR---LKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1383 LEKQVLALQ-SQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1461
Cdd:COG5022 954 PELNKLHEVeSKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1462 QIVSNLEKKQKKfdQLLAEEKGISAryaeerdrAEAEAREKETKALSLARALEEALEAKEEFER--QNKQLRADMEDLMS 1539
Cdd:COG5022 1034 IISSESTELSIL--KPLQKLKGLLL--------LENNQLQARYKALKLRRENSLLDDKQLYQLEstENLLKTINVKDLEV 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1540 SKDDVGKNVHELEK-----SKRALEQQVEEMRTQLeeledeLQATEDAKLRLEVNMQAMKAQFerDLQTRDEQNEEKKRL 1614
Cdd:COG5022 1104 TNRNLVKPANVLQFivaqmIKLNLLQEISKFLSQL------VNTLEPVFQKLSVLQLELDGLF--WEANLEALPSPPPFA 1175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1615 LLKQVRELEAELEDERKQRALAVASKKKMEIDLkdlEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1694
Cdd:COG5022 1176 ALSEKRLYQSALYDEKSKLSSSEVNDLKNELIA---LFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDT 1252
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1695 QSKESEKKLKSLEAEI---LQLQEELASSERARRHAEQER--DELADEIANSAS-GKSALLDEKRRLEARIAQLEEELEE 1768
Cdd:COG5022 1253 PASMSNEKLLSLLNSIdnlLSSYKLEEEVLPATINSLLQYinVGLFNALRTKASsLRWKSATEVNYNSEELDDWCREFEI 1332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1769 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNarqQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLE 1848
Cdd:COG5022 1333 SDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLN---PAEIQNLKSRYDPADKENNLPKEILKKIEALLIK---QE 1406
|
650 660
....*....|....*....|....*...
gi 1039738673 1849 EQLEQEAKeraaanklvRRTEKKLKEIF 1876
Cdd:COG5022 1407 LQLSLEGK---------DETEVHLSEIF 1425
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
678-702 |
1.30e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.30e-05
10 20
....*....|....*....|....*
gi 1039738673 678 YKESLTKLMATLRNTNPNFVRCIIP 702
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
863-1363 |
1.30e-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: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 863 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQA-----ETELFAEAEEMRARLAAK 937
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE----LDDRNMEVQRLEAllkamKSECQGQMERQMAAIQGK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 938 KQELEEI---LHDLESrvEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEakIKKMEEEVLLLEDQ 1014
Cdd:pfam15921 457 NESLEKVsslTAQLES--TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE--ITKLRSRVDLKLQE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1015 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGEttdLQDQIAE 1094
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKE---INDRRLE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1095 LQaqvdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKt 1174
Cdd:pfam15921 606 LQ----EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK- 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1175 eledtldttaaqQELRTKREqevaelkkalEDETKNHEAQIQdmrqrhataLEELSEQLEQAKrfkaNLEKNKQGleTDN 1254
Cdd:pfam15921 681 ------------RNFRNKSE----------EMETTTNKLKMQ---------LKSAQSELEQTR----NTLKSMEG--SDG 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1255 KELACEVKVLQQVKAesehKRKKLDA---QVQELHAKVSEGDRLRVELAEKANKLQNELDNVST----------LLEEAE 1321
Cdd:pfam15921 724 HAMKVAMGMQKQITA----KRGQIDAlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmageleVLRSQE 799
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1322 KK------GIKFAKDAAGLE-SQLQD-TQELLQEETRQKLNLSSRIRQLE 1363
Cdd:pfam15921 800 RRlkekvaNMEVALDKASLQfAECQDiIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1040-1449 |
1.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1040 EEKAKNLAKIRNKQEVM----ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQVDELKVQLTKKEEELQG 1115
Cdd:COG4717 52 EKEADELFKPQGRKPELnlkeLKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1116 AlargddetlhknNALKVARELQAQIAELQEDFESEKAsrnkAEKQKRDLSEELEALKTELEdtldttaaqqELRTKREQ 1195
Cdd:COG4717 128 L------------PLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELA----------ELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1196 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE------------------- 1256
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallal 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1257 --------------------------------------LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVE 1298
Cdd:COG4717 262 lglggsllsliltiagvlflvlgllallflllarekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1299 LAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEE----------- 1365
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQleellgeleel 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1366 -----KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDD--DLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDK 1438
Cdd:COG4717 422 lealdEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
490
....*....|.
gi 1039738673 1439 LEKTKNRLQQE 1449
Cdd:COG4717 502 LEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
908-1157 |
1.35e-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: 49.76 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 908 EEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegar 987
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 988 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQevmISDLEERLKKE 1067
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ---AEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1068 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQED 1147
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1039738673 1148 FESEKASRNK 1157
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1333-1818 |
1.59e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1333 GLESQLQDTQELLQEE--TRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKK---KVD 1402
Cdd:PRK04863 227 GVRKAFQDMEAALRENrmTLEAIRVTQSDRDLfkhliTESTNYVAADYMRHANERRVHLEEALELRRELYTSRRqlaAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1403 DDLGTI----ESLEEAKKKLLKDVEALSQRL---EEKVLAYDKLEktknRLQQELDDLTVDLDHQRQIVSNLekkqkkfd 1475
Cdd:PRK04863 307 YRLVEMarelAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIE----RYQADLEELEERLEEQNEVVEEA-------- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1476 qllaeekgisaryAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKsk 1555
Cdd:PRK04863 375 -------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN-- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1556 raLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQTRDEQNEEKKRLLLKQV-RELeaeLEDERKQRA 1634
Cdd:PRK04863 440 --AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIAGEVSRSEAWDVaREL---LRRLREQRH 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1635 LAvASKKKMEIDLKDLE---AQIEAANKARDEVIKQLRKLQAQMKDYQRELEEarasrdeifaqskesekklksLEAEIL 1711
Cdd:PRK04863 511 LA-EQLQQLRMRLSELEqrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---------------------LEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1712 QLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLND---RFRKTTLQVD 1788
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQlleRERELTVERD 648
|
490 500 510
....*....|....*....|....*....|
gi 1039738673 1789 tlntelaaeRSAAQKsdnarQQLERQNKEL 1818
Cdd:PRK04863 649 ---------ELAARK-----QALDEEIERL 664
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1012-1254 |
1.65e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.93 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1012 EDQNSKFIKEKKLMEdRIAECSSQLAEEEEKAKNLAKIRNKQEVmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1091
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKVSV--KSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1092 IAELQAQVDELKVqLTKKEEELQgaLARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-------AEKQKRD 1164
Cdd:PRK05771 116 IKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1165 LSEELEALKTELEDTLDTTAAQQELRTKrEQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSEQLEQAkRFKANLE 1244
Cdd:PRK05771 193 VEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIE-LERAEAL 266
|
250
....*....|
gi 1039738673 1245 KNkqGLETDN 1254
Cdd:PRK05771 267 SK--FLKTDK 274
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1067-1361 |
1.81e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1067 EEKTRQELEKAKrklDGETTDLQDQIAELQAQVDELkvqltkkeEELQGALARGDDETLHKNNALKVARELQAQIAElqe 1146
Cdd:PRK10929 25 EKQITQELEQAK---AAKTPAQAEIVEALQSALNWL--------EERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1147 dfESEKASRNKAEKQKRDLSEELEALKTELEDtlDTTAAQQElrtkreqevaelkkaledetknheaqiQDMRQRHATAL 1226
Cdd:PRK10929 91 --ERDEPRSVPPNMSTDALEQEILQVSSQLLE--KSRQAQQE---------------------------QDRAREISDSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1227 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkAESEHKRkkldAQVQELH-AKVS-----EGDRLRVELA 1300
Cdd:PRK10929 140 SQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ--AESAALK----ALVDELElAQLSannrqELARLRSELA 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1301 EK-ANKLQNELDNVSTLL--------EEAEKKGIKFAKDAAGLE----SQLQDTQELLQE--ETRQKLNL-SSRIRQ 1361
Cdd:PRK10929 214 KKrSQQLDAYLQALRNQLnsqrqreaERALESTELLAEQSGDLPksivAQFKINRELSQAlnQQAQRMDLiASQQRQ 290
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1646-1940 |
1.90e-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: 49.30 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1646 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1725
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1726 HAEQERDELADEIANsasgKSALLdekRRLEARIAQLEEELEeeqsNMELLNDRFRKTTLQVDTLNTELAAER-SAAQKS 1804
Cdd:pfam19220 101 EAEAAKEELRIELRD----KTAQA---EALERQLAAETEQNR----ALEEENKALREEAQAAEKALQRAEGELaTARERL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1805 DNARQQLERQNK----------ELKAKLQELEG----------AVKSKFKATISALEAKIGQLEEQLEQEAKERA----- 1859
Cdd:pfam19220 170 ALLEQENRRLQAlseeqaaelaELTRRLAELETqldatrarlrALEGQLAAEQAERERAEAQLEEAVEAHRAERAslrmk 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1860 --AANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEG 1937
Cdd:pfam19220 250 leALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEM 329
|
...
gi 1039738673 1938 LSR 1940
Cdd:pfam19220 330 LTK 332
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1205-1427 |
2.07e-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: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1205 EDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesehkrKKLDAQVQE 1284
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI------------------DKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1285 LHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGI-KFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLE 1363
Cdd:COG3883 77 AEAEI---EERREELGERARALYRSGGSVSYLDVLLGSESFsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1364 EEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1427
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1561-1906 |
2.10e-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: 49.97 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1561 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL--AVA 1638
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1639 SKKKMEIDLKDLEAQIEAANKARD-----EVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1713
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1714 QEELASSERARRHAEQErdeladeiansaSGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1793
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVA------------TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1794 LAAERSAAQKSDNARQQLERQNKELKaklqelegavkskfkatisaleakigQLEEQLEQEAKERAAANKLVRRTEKKLK 1873
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAE--------------------------LCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350
....*....|....*....|....*....|...
gi 1039738673 1874 EIFMQVEDERRHADQYKEQMEKANARMKQLKRQ 1906
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1609 |
3.31e-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: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1391 QSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK 1470
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1471 QKK-------FDQLLAeekgiSARYAEERDRAEAeareketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDD 1543
Cdd:COG3883 95 LYRsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1544 VGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNE 1609
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1068-1238 |
4.15e-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: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1068 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ--LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1145
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1146 EDFES--EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1223
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170
....*....|....*
gi 1039738673 1224 TALEELSEQLEQAKR 1238
Cdd:COG3206 327 AREASLQAQLAQLEA 341
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1620-1734 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1620 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEifaqSKES 1699
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR----EIRK 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1039738673 1700 EKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1734
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1334-1703 |
4.76e-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: 48.35 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1334 LESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1413
Cdd:pfam07888 36 LEECLQERAELLQAQEAAN-------RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1414 AKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL-----------EKKQKKFDQLLAEEK 1482
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaerKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1483 GISARYAEERDRAEaearEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1562
Cdd:pfam07888 189 SLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1563 EEM-RTQLEELEDELQATE------DAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRal 1635
Cdd:pfam07888 265 AQRdRTQAELHQARLQAAQltlqlaDASLALREG-RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER-- 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1636 avaskKKMEIDLkdleAQIEAANKA-RDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1703
Cdd:pfam07888 342 -----EKLEVEL----GREKDCNRVqLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1135-1284 |
4.88e-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: 46.84 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1135 RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEvaelkkALEDETKNHEAQ 1214
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRNNKEYE------ALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1215 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE 1284
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1038-1309 |
5.16e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1038 EEEEKAKNLAKIRNKQEvmisdlEERLKKEEKTRQEleKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1117
Cdd:PRK05035 442 EQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1118 ARGDDETLHKNNALKVARELQAQIAELQEDfESEKAS------RNKAEKQkrdlseELEALKTELEDTLDTTAAQQELRT 1191
Cdd:PRK05035 514 PDNSAVIAAREARKAQARARQAEKQAAAAA-DPKKAAvaaaiaRAKAKKA------AQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1192 KREQEVAELKKALEDETKNHEAQIQDMRQRHATAleelseqLEQAKRFKANLE-KNKQGLETDNKELAcevkvlqqVKAE 1270
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAA-------IARAKAKKAEQQaNAEPEEPVDPRKAA--------VAAA 651
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039738673 1271 SEHKRKKLDAQVQELHAKVSEGDRLRVELAE-----KANKLQNE 1309
Cdd:PRK05035 652 IARAKARKAAQQQANAEPEEAEDPKKAAVAAaiaraKAKKAAQQ 695
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
986-1201 |
5.22e-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: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 986 ARQKLQlekvTAEAKIKKMEEE--VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEEr 1063
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1064 LKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKKEEELQGALargddetlhkNNALKVARELQAQ 1140
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASL----------EAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1141 IAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEVAELK 1201
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1330-1510 |
5.30e-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: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1330 DAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVD------- 1402
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1403 ----------------------DDLGTIESLEEAKKKLLKDVEALSQRLEEKvlaydklektKNRLQQELDDLTVDLDHQ 1460
Cdd:COG3883 97 rsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAK----------KAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1461 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA 1510
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1294-1499 |
6.29e-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: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1294 RLRVELAEKANK-LQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLNLSSRIRQLEEEknslqeq 1372
Cdd:COG3206 167 ELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAE------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1373 qeeeeeaRKNLEKQVLALQSQLADTKKKVDDDLG--TIESLEEAKKKLLKDVEALSQRLEEK----VLAYDKLEKTKNRL 1446
Cdd:COG3206 235 -------LAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQL 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1447 QQELDDLTVDLDHQRQI----VSNLEKKQKKFDQLLAEEKGISARYAE-ERDRAEAEA 1499
Cdd:COG3206 308 QQEAQRILASLEAELEAlqarEASLQAQLAQLEARLAELPELEAELRRlEREVEVARE 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1149-1364 |
6.29e-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: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1149 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAElkkALEDETKNHEAQIQDMRQRhataLEE 1228
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEFRQKNGLV---DLSEEAKLLLQQLSELESQ----LAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1229 LSEQLEQAKRFKANLEKNKQGLETDNKELAcEVKVLQQVKAEsehkRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQN 1308
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELL-QSPVIQQLRAQ----LAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1309 ELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1364
Cdd:COG3206 306 QLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1022-1362 |
6.57e-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: 47.93 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1022 KKLMEDRIAECSSQLAEEEE--------KAKN--------LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1085
Cdd:pfam06160 55 DDIVTKSLPDIEELLFEAEElndkyrfkKAKKaldeieelLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1086 TDLQDQ-------IAELQAQVDELKVQLTKKEEELQGalarGDDETlhknnALKVARELQAQIAELQEDFESEKASRNKA 1158
Cdd:pfam06160 135 KTLLANrfsygpaIDELEKQLAEIEEEFSQFEELTES----GDYLE-----AREVLEKLEEETDALEELMEDIPPLYEEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1159 EKQKRDLSEELEALKTELED---TLDTTAAQQELRTKREQeVAELKKALED-ETKNHEAQIQDMRQRhataLEELSEQLE 1234
Cdd:pfam06160 206 KTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEIEER----IDQLYDLLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1235 QAKRFKANLEKNKQGLETD-------NKELACEVKVLQQ---VKAESEHKRKKLDAQVQELHAKVsegDRLRVELAEKA- 1303
Cdd:pfam06160 281 KEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKRY---DEIVERLEEKEv 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1304 --NKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1362
Cdd:pfam06160 358 aySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1269-1446 |
7.77e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1269 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEE 1348
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1349 TRQKLnlssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQR 1428
Cdd:COG1579 99 ESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAK 171
|
170
....*....|....*....
gi 1039738673 1429 LEEKVLA-YDKLEKTKNRL 1446
Cdd:COG1579 172 IPPELLAlYERIRKRKNGL 190
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1071-1235 |
8.01e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1071 RQEL---EKAKRKLDGETTDLQDQIA-------ELQAQVDELKVQLTKKEEE---LQGALARGDDEtlhknnalkvAREL 1137
Cdd:PRK09039 45 SREIsgkDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGA----------GAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1138 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELedtldttaaqqelrtkreQEVAELKKALEDETKNHEAQIQD 1217
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL------------------AALEAALDASEKRDRESQAKIAD 176
|
170
....*....|....*...
gi 1039738673 1218 MRQRHATALEELSEQLEQ 1235
Cdd:PRK09039 177 LGRRLNVALAQRVQELNR 194
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1550-1951 |
8.32e-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: 47.66 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDE 1629
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--------LQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1630 RKQraLAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL--- 1706
Cdd:TIGR00618 273 RAQ--EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtl 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1707 ------------EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE-----------KRRLEARIAQLE 1763
Cdd:TIGR00618 351 hsqeihirdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQReqatidtrtsaFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1764 EELEEEQSNMELLnDRFRKTTLQVDTLntELAAERSAAQKSDNARQQLerQNKELKAKLQELEGAVKSKFKATISALEAK 1843
Cdd:TIGR00618 431 KQQELQQRYAELC-AAAITCTAQCEKL--EKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1844 IGQLEEQLEQEAKERAAANKLVRRT----------EKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeee 1913
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC------- 578
|
410 420 430
....*....|....*....|....*....|....*...
gi 1039738673 1914 ATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1951
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1646-1877 |
8.54e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1646 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskeSEKKLKSLE-AEILQLQEELASSERAR 1724
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL------EAAALQPGEeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1725 RHAEQERDELADEIANSASgksaLLDE-KRRLEaRIAQleeeleeEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQk 1803
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLE- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1804 SDNAR-QQLE-RQN--------------------KELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKE---- 1857
Cdd:COG0497 293 FDPERlEEVEeRLAllrrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaa 367
|
250 260
....*....|....*....|.
gi 1039738673 1858 -RAAANKLVRRTEKKLKEIFM 1877
Cdd:COG0497 368 rKKAAKKLEKAVTAELADLGM 388
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
863-1266 |
8.89e-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: 47.20 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 863 KPLLQVTRQEEELQAKD--EELLKVKEKQTKVEGELEEMERKhqqlleekniLAEQLQAETELFAEAEEMRARLAAKKQE 940
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQE----------RAELLQAQEAANRQREKEKERYKRDREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 941 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 1020
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1021 EKKLMEDRIAECSSQLAEEEEKAKNLakirnkqEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1100
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1101 ELKvqltKKEEELQGALA--RGDDETLH--KNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALK--- 1173
Cdd:pfam07888 224 TAH----RKEAENEALLEelRSLQERLNasERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1174 ----TELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL---EKN 1246
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKE 379
|
410 420
....*....|....*....|
gi 1039738673 1247 KQGLETDNKELACEVKVLQQ 1266
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQLEQ 399
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
870-1218 |
9.19e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 870 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleEKNILAEQlqaetelfaeaeemRARLAAKkQELEEILHDLE 949
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLN--------------QARLQAL-EDLEKILTEKE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 950 SrveeeeernqiLQNEKKKMQAHIQDLEEQLdeeegarqklqleKVTAEAKIKkmeeeVLLLEDQNSKFIKEKKLMEDRI 1029
Cdd:PLN02939 167 A-----------LQGKINILEMRLSETDARI-------------KLAAQEKIH-----VEILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1030 AECSSQLAEEEE--KAKNLAkIRNKQEVM------ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIaelqAQVDE 1101
Cdd:PLN02939 218 GLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDV----SKLSP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1102 LKVQ-LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTELEDTL 1180
Cdd:PLN02939 293 LQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASD 371
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039738673 1181 DTTAAQQELRTKREQEVAELKKALEDETKNH--EAQIQDM 1218
Cdd:PLN02939 372 HEIHSYIQLYQESIKEFQDTLSKLKEESKKRslEHPADDM 411
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1264-1391 |
1.07e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1264 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAglESQLQDTQE 1343
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1039738673 1344 LLQEETRqklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1391
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
866-1080 |
1.09e-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: 47.43 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 866 LQVTRQEEelqaKDEELLKVKEKQTKVEGE-LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 944
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISrMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 945 LHDLESrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIkEKKL 1024
Cdd:pfam17380 426 RAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKEL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1025 MEDRIAecssqLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1080
Cdd:pfam17380 502 EERKQA-----MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1102-1307 |
1.11e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1102 LKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL---EALKTELED 1178
Cdd:PRK09039 44 LSREISGKDSALD---------------------RLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1179 TLDTTAAQqelRTKREQEVAELKKALEDEtknheaqiQDMRQRHATALEELSEQLEQAKRfkanleknkqgletdnkELA 1258
Cdd:PRK09039 103 LLAELAGA---GAAAEGRAGELAQELDSE--------KQVSARALAQVELLNQQIAALRR-----------------QLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039738673 1259 cevkVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQ 1307
Cdd:PRK09039 155 ----ALEAALDASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1080-1506 |
1.31e-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: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1080 KLDGETTDLQDQIAELQAQVDelkvqlTKKEEELQGALARGDDETLHKNNALKVarelqaqiaelQEDFESEKASRNKAE 1159
Cdd:NF012221 1355 EIDEVGSDLGDSLTGSVTQVE------TPDLNAMQNALNIDESVLSTQAPNLIV-----------NGDFEQGAEGWNSTY 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1160 KQKRDLS--------EELEALKTELeDTLDTTAAQQELRTKREQEVAELK----KALEDETKNHEAQIQDMRQRHATALE 1227
Cdd:NF012221 1418 GVEASHSasvyglraEGHGARVSEL-DTYTNTSLYQDLSNLTAGEVIALSfdfaRRAGLSTNNGIEVLWNGEVVFASSGD 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1228 ELSEQLEQAK----------RFKANLEKNKQGLETDNKELACEVKvlQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRV 1297
Cdd:NF012221 1497 ASAWQQKTLKltakagsnrlEFKGTGHNDGLGYILDNVVATSESS--QQADAVSKHAKQDDAAQNALADKERAEADRQRL 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1298 ElAEKanklQNELDNVSTLLEEAEkkgikfAKDAAGLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEKNSLQEQQEEE 1376
Cdd:NF012221 1575 E-QEK----QQQLAAISGSQSQLE------STDQNALETNGQAQRDAILEESRAvTKELTTLAQGLDALDSQATYAGESG 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1377 EEARKNLEKQVLA-LQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTV 1455
Cdd:NF012221 1644 DQWRNPFAGGLLDrVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG------EQNQANAEQDIDDAKA 1717
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1456 DLDHQRQivsnlEKKQKKFDQLLAEEKGiSARYAEERDRAEAEAREKETKA 1506
Cdd:NF012221 1718 DAEKRKD-----DALAKQNEAQQAESDA-NAAANDAQSRGEQDASAAENKA 1762
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1653-1933 |
1.39e-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: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1653 QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKSLEAEILQLQEElassERARRHAE 1728
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1729 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnDRFRKTTLQVDTLNtELAAERSAAQKSDNAR 1808
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1809 QQLERQNKELKAKLQELEgavKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRT-EKKLKEIFMQ-VEDERRHA 1886
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039738673 1887 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1933
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1039-1508 |
1.41e-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: 47.05 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1039 EEEKAKNLAKIRNKQEVMISDL----EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQ 1114
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1115 GALARgdDETLHKNNALKVARELQAQIAE------------LQEDFESEKAS------RNKAEKQKRDLSEELEALKTEL 1176
Cdd:pfam07111 215 AQVTL--VESLRKYVGEQVPPEVHSQTWElerqelldtmqhLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1177 EDTLD---TTAAQQELRTKREQeVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD 1253
Cdd:pfam07111 293 SDSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1254 N---KELACEVKVLQQVKAESEHKRKKLDAQVQ-----------ELHAKVSEGDRLRVELAEKANKLQNELDNVSTL--- 1316
Cdd:pfam07111 372 RmsaKGLQMELSRAQEARRRQQQQTASAEEQLKfvvnamsstqiWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIkgl 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1317 ------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ---KLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEK 1385
Cdd:pfam07111 452 markvaLAQLRQESCPPPPPAPPVDADLSLELEQLREERNRldaELQLSAHLIQQEvgRAREQGEAERQQLSEVAQQLEQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1386 QVLALQSQLADTKKKVDDDL-GTIESLEEA---KKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTVDLDHQR 1461
Cdd:pfam07111 532 ELQRAQESLASVGQQLEVARqGQQESTEEAaslRQELTQQQEIYGQALQEKV------AEVETRLREQLSDTKRRLNEAR 605
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1039738673 1462 QIVSNLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKALS 1508
Cdd:pfam07111 606 REQAKAVVSLRQIQHRATQEK----ERNQELRRLQDEARKEEGQRLA 648
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1607-1927 |
1.45e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1607 QNEEKKRLLLKQVRELEAELEDERKQRALA----VASKKKMEI---DLKDLEAQIEAA----NKARDEVI--KQLRKLQA 1673
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEqyrlVEMARELAElneAESDLEQDYQAAsdhlNLVQTALRqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1674 QMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA----------RRHAEQERDE---LADEIAN 1740
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERakqLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1741 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRkttlQVDTLNTELAAERSAAQKSDNARQqLERQNKELKA 1820
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSRSEAWDVARE-LLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1821 KLQELEgavkskfkatisALEAKIGQLEEQLEQEAkeraAANKLVRRTEKKLKeifMQVEDErrhaDQYKEQMEKANARM 1900
Cdd:PRK04863 511 LAEQLQ------------QLRMRLSELEQRLRQQQ----RAERLLAEFCKRLG---KNLDDE----DELEQLQEELEARL 567
|
330 340
....*....|....*....|....*..
gi 1039738673 1901 KQLKRQLEEAEEEATRANASRRKLQRE 1927
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQLEQLQAR 594
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1528-1863 |
1.56e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1528 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMR---TQLEELEDELQATEDAKLRLEVNMQAMKAQ------FE 1598
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDYNNLKSALNELSSLedmknrYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1599 RDLQTRDE--QNEEKKRLLLKQVRELEAELEDE----RKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQ 1672
Cdd:PRK01156 256 SEIKTAESdlSMELEKNNYYKELEERHMKIINDpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1673 AQMKDY---QRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALL 1749
Cdd:PRK01156 336 KDYNDYikkKSRYDDLNNQILEL----EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1750 DEKRR-----------LEARIAQLEEELEEEQSNMELLNDRFR-----------KTTLQVDTLNTELAAERSAAQKSDNA 1807
Cdd:PRK01156 412 NEINVklqdisskvssLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIE 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1808 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1863
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1278-1636 |
1.61e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1278 LDAQVQEL---HAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLN 1354
Cdd:pfam19220 36 IEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1355 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVL 1434
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1435 AYDKLEKTKNRLQQELDDltvdldhQRQIVSNLEKKqkkfdqlLAEEKgisaryaEERDRAEAEAREK----ETKALSLA 1510
Cdd:pfam19220 189 ELAELTRRLAELETQLDA-------TRARLRALEGQ-------LAAEQ-------AERERAEAQLEEAveahRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1511 RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE--V 1588
Cdd:pfam19220 248 MKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerA 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1589 NM-----QAMKAQFER------DLQTRDEQNE---EKKRLLLKQ-VRELEAELEDERKQRALA 1636
Cdd:pfam19220 328 EMltkalAAKDAALERaeeriaSLSDRIAELTkrfEVERAALEQaNRRLKEELQRERAERALA 390
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1554-1709 |
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 1039738673 1554 SKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQV---RELEAEL---- 1626
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERsarREAEAELerlq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1627 -------EDERKQRALAVASKKKMEIDLKDLEAQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1696
Cdd:pfam09787 121 eelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
|
170
....*....|...
gi 1039738673 1697 KESEKKLKSLEAE 1709
Cdd:pfam09787 201 ERMEQQIKELQGE 213
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1381-1905 |
1.72e-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: 46.67 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1381 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQ 1460
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1461 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSS 1540
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQ-------LAEAQKEAELLRKQLSKTQEELEAQVTLVESL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1541 KDDVGKNV--------------------HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD 1600
Cdd:pfam07111 224 RKYVGEQVppevhsqtwelerqelldtmQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1601 LQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVAS--------------------KKKMEIDL-----KDLEAQIE 1655
Cdd:pfam07111 304 CRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAElqeqvtsqsqeqailqralqDKAAEVEVermsaKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1656 AANKAR-------DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL----------KSLEAEILQLQEELA 1718
Cdd:pfam07111 384 RAQEARrrqqqqtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQ 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1719 SSERARRHAEQERDELADEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNME---------LLNDRFRKTTLQVDT 1789
Cdd:pfam07111 464 ESCPPPPPAPPVDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAErqqlsevaqQLEQELQRAQESLAS 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1790 LNTELAAERSAAQKSD----NARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLEEQLEQEAKERAAANKLV 1865
Cdd:pfam07111 543 VGQQLEVARQGQQESTeeaaSLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARREQAKAVVSLRQIQ 619
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1039738673 1866 RRT--EKKLKEIFMQVEDERRhadqyKEQMEKANARMKQLKR 1905
Cdd:pfam07111 620 HRAtqEKERNQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1041-1176 |
1.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1041 EKAK-NLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLtkkEEELQGALar 1119
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAI-- 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1120 gddetlhkNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTEL 1176
Cdd:PRK00409 580 --------KEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKKEKKK 627
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1590-1984 |
1.89e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1590 MQAMKAQFERDLQTRDEQ----NEEKKRLLLKQVRELEAELEDERKQralaVASKKKMEIDLKDLEAQIEAANKARDEVI 1665
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1666 KQLRKLQaQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGK 1745
Cdd:COG4717 116 EELEKLE-KLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1746 SA----LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE-----------LAAERSAAQKSDNARQQ 1810
Cdd:COG4717 191 EEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1811 LERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1890
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1891 EQMEKANARMKQLKRQLEEAEEEA--TRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR-GGPISFSSSRSGRRQL 1967
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEElLGELEELLEALDEEEL 430
|
410
....*....|....*..
gi 1039738673 1968 HIEGASLELSDDDTESK 1984
Cdd:COG4717 431 EEELEELEEELEELEEE 447
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
913-1233 |
1.92e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 913 LAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE-------SRVEEEEERNQILQNEKKKMQAhiqdleeqlDEEEG 985
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVASAEREIAELEAELERL---------DASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 986 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkQEVMISDLEERLK 1065
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA---------RLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1066 KEEKTRQELEKAKRkldgettdLQDQIAELQAQVDELKVQLTKKeeeLQGALARGDDETLHKNNALKVARELQAQIAELQ 1145
Cdd:COG4913 757 AALGDAVERELREN--------LEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1146 ED----FESE-KASRNKAEKQKR-DLSEELEALKTELEDTLDT-------------TAAQQELRTKREQEVAELKKALED 1206
Cdd:COG4913 826 EDglpeYEERfKELLNENSIEFVaDLLSKLRRAIREIKERIDPlndslkripfgpgRYLRLEARPRPDPEVREFRQELRA 905
|
330 340
....*....|....*....|....*..
gi 1039738673 1207 ETKNHEAQIQDMRQRHATALEELSEQL 1233
Cdd:COG4913 906 VTSGASLFDEELSEARFAALKRLIERL 932
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1527-1659 |
2.14e-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: 46.59 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1527 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDE 1606
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYE-DLETRLT 761
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1607 QNEEKKRLLLKQVRELEAELEDERKqralavaSKKKMEIDLKDLEAQIEAANK 1659
Cdd:pfam05911 762 ELEAELNELRQKFEALEVELEEEKN-------CHEELEAKCLELQEQLERNEK 807
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
922-1496 |
2.15e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 922 ELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEErnqiLQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKI 1001
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1002 KKMEEEVLLLED---QNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkqeVMISDLEERLKKEEKTRQeleKAK 1078
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKN-----------NYYKELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1079 RKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGA--LARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1156
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLsvLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1157 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL--- 1233
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNMeml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1234 ---------------EQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDA-QVQELHAKVSEGDRLRV 1297
Cdd:PRK01156 450 ngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1298 ELAEKANKLqNELDNVSTLLEEA--EKKGIKFakdaaglesqlqdtqELLQEETRQKLNLSSRIRQLEEEknSLQEQQEE 1375
Cdd:PRK01156 530 DLEDIKIKI-NELKDKHDKYEEIknRYKSLKL---------------EDLDSKRTSWLNALAVISLIDIE--TNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1376 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIE---SLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDD 1452
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEneaNNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE 671
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738673 1453 LTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1496
Cdd:PRK01156 672 ITSRIN---DIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1666-1951 |
2.18e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1666 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAE---QERDELADEIANSA 1742
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1743 SGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqvdtlntelAAERSAAQKSDNARQQLERQNKELKAKL 1822
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1823 QELEgavkskfkATISALEAKIGQLEEQLeqeaKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANaRMKQ 1902
Cdd:PRK03918 310 REIE--------KRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELER 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1039738673 1903 LKRQLeeaeeeatrANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1951
Cdd:PRK03918 377 LKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
865-1287 |
2.34e-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: 46.58 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 865 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEME---RKHQQLLEEKNI---LAEQLQAET----ELFAEAEEMRARL 934
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKndiEEQETLLGTIMPeeeSAKVCLTDVtimeRFQMELKDVERKI 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 935 AAKKQELEEIlhDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQL---EKVTAEAKIKKMEEEVLLL 1011
Cdd:TIGR00606 809 AQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQF 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1012 EDQNSKFIKEkklMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1091
Cdd:TIGR00606 887 EEQLVELSTE---VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1092 IAELQAQvdelkvQLTKKEEELQGALARGDDETLHKNnalkvarelqaqiaELQEDFESEKASRNKAEKQKRDLSEELEA 1171
Cdd:TIGR00606 964 IQDGKDD------YLKQKETELNTVNAQLEECEKHQE--------------KINEDMRLMRQDIDTQKIQERWLQDNLTL 1023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1172 LKTELEDTLDTTAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL-EKNKQGL 1250
Cdd:TIGR00606 1024 RKRENELKEVEEELKQHLKEMGQMQVLQMKQ----EHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELrEPQFRDA 1099
|
410 420 430
....*....|....*....|....*....|....*..
gi 1039738673 1251 ETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1287
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHS 1136
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1793-1905 |
2.46e-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: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1793 ELAAERSAAQKSDNARQ--QLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEK 1870
Cdd:COG2433 398 EREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|....*
gi 1039738673 1871 KLKEIfmqvEDERRHADQYKEQMEkanaRMKQLKR 1905
Cdd:COG2433 477 LEREL----EEERERIEELKRKLE----RLKELWK 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
872-1156 |
2.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 872 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETElfaEAEEMRARLAAKKQELEEilhdlesr 951
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEE-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 952 veeeeeRNQILQNEKKKMQahiqdleeqldeeegaRQKLQLEKVtaeakikkmeeEVLLLEDQNSKFIKEKKLMeDRIAE 1031
Cdd:COG3883 84 ------RREELGERARALY----------------RSGGSVSYL-----------DVLLGSESFSDFLDRLSAL-SKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1032 CSSQLAEEEEKAKnlAKIRNKQevmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEE 1111
Cdd:COG3883 130 ADADLLEELKADK--AELEAKK----AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039738673 1112 ELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1156
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1647-1905 |
2.87e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1647 LKDLEAQIEAANKARDEVIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKSLEAEILQLQEELASSERarRH 1726
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1727 AEQERDeLADEIANS-----ASGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERS 1799
Cdd:PRK11637 120 AAQERL-LAAQLDAAfrqgeHTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1800 AAQKSDNARQQLERQNKELKAKLQELEGAVKSkfkaTISALEAKIGQLEEQLEQeakeraaanklVRRTEKKLKEIFMQV 1879
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQARNERKK----TLTGLESSLQKDQQQLSE-----------LRANESRLRDSIARA 252
|
250 260
....*....|....*....|....*..
gi 1039738673 1880 EDE-RRHADQYKEQMEKANARMKQLKR 1905
Cdd:PRK11637 253 EREaKARAEREAREAARVRDKQKQAKR 279
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1550-1670 |
2.93e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD---------------LQTRDEQNEEKKRL 1614
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnnkeyeaLQKEIESLKRRISD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1615 LLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRK 1670
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
895-1493 |
3.15e-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: 46.20 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 895 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeilhdLESRVEEEEERNQILQNEKKKmqahiq 974
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIIIKEIKD------ 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 975 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED--------------------RIAECss 1034
Cdd:TIGR01612 1556 -----------AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflkisdikkKINDC-- 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1035 qLAEEEEKAKNLAKIR-NKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQVDELKVQLTKKEEEL 1113
Cdd:TIGR01612 1623 -LKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1114 QGALARGDDETLHKNNalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKR 1193
Cdd:TIGR01612 1698 EIGIIEKIKEIAIANK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGC 1772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1194 EQEVAElkkalEDETKNheaQIQDMRqrhATALEELSEQLEQAKRFKANLeknkqgletDNKELACEVKVLQQVKAESEH 1273
Cdd:TIGR01612 1773 LETVSK-----EPITYD---EIKNTR---INAQNEFLKIIEIEKKSKSYL---------DDIEAKEFDRIINHFKKKLDH 1832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1274 KRKKLDAQvqelHAKVSEG-DRL-----RVELAEKANKLQNELDNVSTLL------------EEAEKKGIKFAKDAAGLE 1335
Cdd:TIGR01612 1833 VNDKFTKE----YSKINEGfDDIsksieNVKNSTDENLLFDILNKTKDAYagiigkkyysykDEAEKIFINISKLANSIN 1908
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1336 SQLQDTQEL-------------LQEETRQKL-------NLSSRIRQLEEEKNSLQEQQEEEEEARKNlEKQVLAL---QS 1392
Cdd:TIGR01612 1909 IQIQNNSGIdlfdniniailssLDSEKEDTLkfipspeKEPEIYTKIRDSYDTLLDIFKKSQDLHKK-EQDTLNIifeNQ 1987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1393 QLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE---------------KVLAYDKLEKTKNRLQQELDDLTVDL 1457
Cdd:TIGR01612 1988 QLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKFGIDF 2067
|
650 660 670
....*....|....*....|....*....|....*...
gi 1039738673 1458 DHQ--RQIVSNLEKKQKKFDQLLAEEKGISARYAEERD 1493
Cdd:TIGR01612 2068 DVKamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1092-1369 |
3.33e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.62 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1092 IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKnnalkVARELQAQIAE------LQEDFESEKASRNKAEKQK--- 1162
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK-----LKKEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1163 -RDLSEELEALKTELEDTLDTTAAQQELRTKRE--QEVAELKKALEDETKNHEAQiQDMRQRHATALE--ELSEQLEQAK 1237
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFKEVMDrpEIKEKMEALK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1238 RFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELD----- 1311
Cdd:PLN03229 585 AEVASSGASSGDeLDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINkkier 664
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1312 --NVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1369
Cdd:PLN03229 665 viRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1661-1826 |
3.44e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1661 RDEVIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkSLEAEILQLQEELASSERARRHAEQERDELADEiAN 1740
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1741 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttlQVDTLNTELAAERSAAQKSDNARQQLERQ------ 1814
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 1039738673 1815 --NKELKAKLQELE 1826
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1558-1949 |
3.69e-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: 45.78 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1558 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF------ERDLQTRDEQNEEKKRLLLKQVRELEAELEDERK 1631
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIkileqqIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1632 QralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQSKESEKKLKSLEAEIL 1711
Cdd:TIGR04523 118 Q-------KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-------ELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1712 QLQEELASSERARRHAEQerdeladeianSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLN 1791
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLEL-----------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1792 TELaaersaaqksDNARQQLERQNKELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKERAAAnklvrrTEKK 1871
Cdd:TIGR04523 253 TQL----------NQLKDEQNKIKKQLSEKQKELEQN-----NKKIKELEKQLNQLKSEISDLNNQKEQD------WNKE 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1872 LKEIFMQVEDERRhadQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1949
Cdd:TIGR04523 312 LKSELKNQEKKLE---EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1278-1946 |
4.22e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1278 LDAQVQELHakvSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnLSS 1357
Cdd:pfam10174 1 LQAQLRDLQ---RENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQH---LQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1358 RIRQLEEEKnslqeqqeeeeEARKNLEKqvlALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDvealsqrleekvlaYD 1437
Cdd:pfam10174 75 TIQALQDEL-----------RAQRDLNQ---LLQQDFTTSPVDGEDKFSTPELTEENFRRLQSE--------------HE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1438 KLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaEEKGISARYAEERDR-----AEAEAREKETKALSLARA 1512
Cdd:pfam10174 127 RQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML-QSKGLPKKSGEEDWErtrriAEAEMQLGHLEVLLDQKE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1513 LEEALEAKEEFER-QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEE--------------------------- 1564
Cdd:pfam10174 206 KENIHLREELHRRnQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhtedreeeikqmevykshsk 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1565 -MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRD------EQNEEKKRLLLKQVRELEAELEdeRKQRALAV 1637
Cdd:pfam10174 286 fMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkeslTAKEQRAAILQTEVDALRLRLE--EKESFLNK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1638 ASKKKMEI---------DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEa 1708
Cdd:pfam10174 364 KTKQLQDLteekstlagEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1709 EILQLQEELAssERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1788
Cdd:pfam10174 443 EALSEKERII--ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1789 TLNTELAAERSAAQKsdnarqqLERQNKelkaKLQELEGAVKSKfkatiSALEAKIGQLEEQLEQEAKERAAANKLVRRt 1868
Cdd:pfam10174 521 SLEIAVEQKKEECSK-------LENQLK----KAHNAEEAVRTN-----PEINDRIRLLEQEVARYKEESGKAQAEVER- 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1869 ekkLKEIFMQVEDERRHADQYKEQMEKANARmkQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLK 1946
Cdd:pfam10174 584 ---LLGILREVENEKNDKDKKIAELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1550-1718 |
4.28e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQ-----NEEKKRLLLKQVRELEA 1624
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-KWEEKARLalekgREDLAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1625 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQ---------------------MKDYQRELE 1683
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvnealsgidsddatsalerMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1039738673 1684 EARASRDEIfAQSKESEKKLKSLEAEIlQLQEELA 1718
Cdd:COG1842 179 ARAEAAAEL-AAGDSLDDELAELEADS-EVEDELA 211
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1436-1878 |
4.40e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1436 YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEAREKETKALsLARALEE 1515
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1516 ALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1595
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1596 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1675
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1676 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1755
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1756 EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1835
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1039738673 1836 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQ 1878
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
864-1237 |
4.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 864 PLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNI-LAEQLQAETElfaeaEEMRArLAAKKQELE 942
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPE-----AELRQ-LNRRRVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 943 EILHDLESrvEEEEERNQILQnekkkmqahiqdleeqldeeegARQKLQLekvtaeakIKKMEEEVLLLEDQNskfikek 1022
Cdd:PRK04863 851 RALADHES--QEQQQRSQLEQ----------------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1023 klMEDRIAECSSQLAEEEEKA-------KNLAKIRNKQEVMISDLE--ERLKKE-EKTRQELEKAKRKLDGETTDLQ--- 1089
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDPEqfEQLKQDyQQAQQTQRDAKQQAFALTEVVQrra 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1090 ----DQIAELQAQVDELKVQLTKKEEELQGALARGDDEtlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDL 1165
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ----------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1166 SEELEALKTELEDTLDTTAA------QQELRTKREQEvAELKKALEDETKNHEAQiqdmrQRHATALEE----LSEQLEQ 1235
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARarrdelHARLSANRSRR-NQLEKQLTFCEAEMDNL-----TKKLRKLERdyheMREQVVN 1113
|
..
gi 1039738673 1236 AK 1237
Cdd:PRK04863 1114 AK 1115
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1555-1709 |
4.75e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1555 KRALEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQTRDEQNEEKKRLLLKQVRELEAELED 1628
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1629 ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKs 1705
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 1039738673 1706 LEAE 1709
Cdd:PRK12704 184 EEAD 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1604-1874 |
5.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1604 RDEQNEEKKRLLLKQVRELEAELEDERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1682
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLrKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1683 EEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1762
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1763 EEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEA 1842
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270
....*....|....*....|....*....|..
gi 1039738673 1843 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1874
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1548-1949 |
5.22e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1548 VHELEKSKrALEQQVEEMRTQLEELEDELQATEDAKLR----LEVN---MQAMKAQFERdLQTRDEQNEEKKRLLLKQVR 1620
Cdd:pfam05701 31 IQTVERRK-LVELELEKVQEEIPEYKKQSEAAEAAKAQvleeLESTkrlIEELKLNLER-AQTEEAQAKQDSELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1621 ELEAELEDErkqraLAVASKKKMEIDLKDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESE 1700
Cdd:pfam05701 109 EMEQGIADE-----ASVAAKAQLEVAKARHAAAVAELKSVKEE----LESLRKEYASLVSERDIAIKRAEEAVSASKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1701 KKLKSLEAEILQLQEELASSERARRHAEQERDELA-----DEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNMEL 1775
Cdd:pfam05701 180 KTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1776 LNDrfrkttlqvdtLNTELAAERSAAQKSDNARQQLERQ-NKELKAKL----QELEGAVKSKFKAT--ISALEAKIGQLE 1848
Cdd:pfam05701 259 LLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALasakKELEEVKANIEKAKdeVNCLRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1849 EQLEQEAKERAAanklVRRTEKKLKEIFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKL 1924
Cdd:pfam05701 328 SELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAA 403
|
410 420
....*....|....*....|....*
gi 1039738673 1925 QRELDDATEANEGLSREVSTLKNRL 1949
Cdd:pfam05701 404 REELRKAKEEAEQAKAAASTVESRL 428
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
996-1323 |
5.37e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 996 TAEAKIKKMEEEVLLL---EDQNSKFIKE---------KKLMEDR------IAECSSQLAEEEE---KAKNLAKIRNKQE 1054
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEefsQFVELTESGDYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1055 --VMISDLEERLKKEEKTRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQ------------LTKKEEELQGALArg 1120
Cdd:PRK04778 196 arEILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeIQDLKEQIDENLA-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1121 DDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE---LRTKREQEV 1197
Cdd:PRK04778 271 LLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsytLNESELESV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1198 AELKKALEDETKNHEAQIQDMRQRHATA------LEELSEQLEQAKRFKANLEKNKQGLETDnkELACEVKVLQQVKAES 1271
Cdd:PRK04778 351 RQLEKQLESLEKQYDEITERIAEQEIAYselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKD--ELEAREKLERYRNKLH 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1272 EHKRK------------------KLDAQVQELHAKVSEGdRLRVElaekanKLQNELDNVSTLLEEAEKK 1323
Cdd:PRK04778 429 EIKRYleksnlpglpedylemffEVSDEIEALAEELEEK-PINME------AVNRLLEEATEDVETLEEE 491
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1550-1688 |
6.03e-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: 44.28 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ-NEEKKRLLLKQVRELEAELED 1628
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1629 ERKqrALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAS 1688
Cdd:cd22656 191 LNE--EYAAKLKAKID-ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1045-1277 |
6.64e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1045 NLAKIR-NKQEVMISDLEERLKKEE-KTRQELEKAKRKLDGE-TTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1121
Cdd:PHA02562 172 NKDKIReLNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1122 DETlhknNALKVARELQAQIAelqedfeSEKASRNKAEKQ----------KRDLSEElEALKTELEDTLDTTAAQQELRT 1191
Cdd:PHA02562 252 DPS----AALNKLNTAAAKIK-------SKIEQFQKVIKMyekggvcptcTQQISEG-PDRITKIKDKLKELQHSLEKLD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1192 KREQEVAELKKALEDETKNheaqIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAE- 1270
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKK----LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTk 395
|
....*..
gi 1039738673 1271 SEHKRKK 1277
Cdd:PHA02562 396 SELVKEK 402
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1016-1174 |
6.82e-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: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1016 SKFIK-EKKLMEDR---------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1085
Cdd:COG2433 350 NKFERvEKKVPPDVdrdevkarvIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1086 TDLQDQIAELQAQVDELKVQLTK-KEEELQGALARgddetlhknnalkvaRElqaqIAELQEDFESEKASRNKAEKQKRD 1164
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEaRSEERREIRKD---------------RE----ISRLDREIERLERELEEERERIEE 490
|
170
....*....|
gi 1039738673 1165 LSEELEALKT 1174
Cdd:COG2433 491 LKRKLERLKE 500
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
872-1234 |
6.82e-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: 44.75 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 872 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESR 951
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 952 VEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAE 1031
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1032 CSSQLAEEEEKAKN-----LAKIRNKQEVMISDLEERLKKEEKTRqeLEKAKRKLDgettDLQDQIAELQAQVDE-LKVQ 1105
Cdd:pfam09731 244 LVDQYKELVASERIvfqqeLVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREID----QLSKKLAELKKREEKhIERA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1106 LTKKEEELqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKrdLSEELEALKTELEDTLDTTAA 1185
Cdd:pfam09731 318 LEKQKEEL---------DKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--LRTELERQAEAHEEHLKDVLV 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039738673 1186 QQELRTKREQEvAELKKALEDETKNHEAQIQDMrqrhATALEELSEQLE 1234
Cdd:pfam09731 387 EQEIELQREFL-QDIKEKVEEERAGRLLKLNEL----LANLKGLEKATS 430
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1331-1932 |
7.27e-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: 44.94 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1331 AAGLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQladtkKKVD---DDLGT 1407
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMA---RELEELSARESDLEQDYQAASDHLNLVQTALRQQ-----EKIEryqEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1408 IES-LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL---QQELDDLTVDLDHQRQIVSNLEKKQKkfdqlLAEEKG 1483
Cdd:COG3096 359 LTErLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyQQALDVQQTRAIQYQQAVQALEKARA-----LCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1484 ISARYAEERdRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD--DVGKNVHELEKSKRALEQ 1560
Cdd:COG3096 434 LTPENAEDY-LAAFRAKEQQaTEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1561 QVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQTRDEQNEEKKrlllkqvrELEAELEDERKQRALAVASK 1640
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLA--------ELEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1641 KKMEIDLKDLEAQI--------------EAANKARDEVIKQLRKLQAQMKDYQRELE---EARASRDEIFAQSKESEKKL 1703
Cdd:COG3096 581 SELRQQLEQLRARIkelaarapawlaaqDALERLREQSGEALADSQEVTAAMQQLLErerEATVERDELAARKQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1704 KSL-------EAEILQLQEELA---------------------------------------------------------- 1718
Cdd:COG3096 661 ERLsqpggaeDPRLLALAERLGgvllseiyddvtledapyfsalygparhaivvpdlsavkeqlagledcpedlyliegd 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1719 ---------------------SSERARR-----------------HAEQ---ERDELADEIANSASGKSALLDEKRRLEA 1757
Cdd:COG3096 741 pdsfddsvfdaeeledavvvkLSDRQWRysrfpevplfgraarekRLEElraERDELAEQYAKASFDVQKLQRLHQAFSQ 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1758 RIAQLEEELEEEQSNMELLNDRFRKTTLQvDTLNTELAAERSAAQKSDNARQQLERQNK------------------ELK 1819
Cdd:COG3096 821 FVGGHLAVAFAPDPEAELAALRQRRSELE-RELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrleELR 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1820 AKLQELEGAVKS--KFKATISALEAKIGQL------EEQLEQEAKERAAANKLVRRTEKKLKEIFmqvedERRHADQYKE 1891
Cdd:COG3096 900 EELDAAQEAQAFiqQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVV-----QRRPHFSYED 974
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1039738673 1892 --QMEKANARM-KQLKRQLEEAEEEATRANASRRKLQRELDDAT 1932
Cdd:COG3096 975 avGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYN 1018
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1634-1850 |
7.42e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1634 ALAVASKKKMEIDLKDLEAqieAANKARDEVIKQL---------RKLQAQ-MKDYQRELEE----ARASRDEIFAQSKE- 1698
Cdd:PRK10929 19 AATAPDEKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1699 ----SEKKLKSLEAEILQLQEELAssERARRhAEQERDElADEIANSASGKSALLDEKRRL----EARI-AQLEEELEEE 1769
Cdd:PRK10929 96 rsvpPNMSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1770 QSNMELLNDRFRKTTLQVDTLntELAaersaaQKSDNARQQLER--------QNKELKAKLQELEGAVKS-KFKATISAL 1840
Cdd:PRK10929 172 QAQLTALQAESAALKALVDEL--ELA------QLSANNRQELARlrselakkRSQQLDAYLQALRNQLNSqRQREAERAL 243
|
250
....*....|
gi 1039738673 1841 EaKIGQLEEQ 1850
Cdd:PRK10929 244 E-STELLAEQ 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
986-1125 |
9.18e-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: 42.99 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 986 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR---------NKQEVM 1056
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1057 ISDLEERLK----KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETL 1125
Cdd:COG1579 105 ISDLEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1550-1761 |
9.87e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDE 1629
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1630 RKQRALAVASKKKMEidlkdleaqiEAANKARDEVIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKSLEAE 1709
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1710 ILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1761
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1135-1323 |
1.03e-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: 42.99 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1135 RELQAQIAELQEdFESEKAsrnKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQevaelKKALEDETKNHEAQ 1214
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELA------ALEARLEAAKTE-----LEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1215 IQDMRQRhataLEELSEQLEQAKRFK--ANLEKNKQGLETDNKELAcevKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1292
Cdd:COG1579 68 IEEVEAR----IKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|.
gi 1039738673 1293 DRLRVELAEKANKLQNELDNVSTLLEEAEKK 1323
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1057-1214 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1057 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARE 1136
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1137 -LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELKKALEDETKNHEAQ 1214
Cdd:pfam12795 160 aLKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1599-1905 |
1.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1599 RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLK-------DLEAQIEAANKARDEVIKQLRKL 1671
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelaQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1672 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELA----DEIANSASGKSA 1747
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldelLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1748 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1827
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1828 AVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKR 1905
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1618-1808 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1618 QVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1697
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1698 ESEKKLKSLEA--------------------------EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE 1751
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1752 KRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNAR 1808
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1036-1432 |
1.27e-03 |
|
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: 44.04 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1036 LAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQD-------QIAELQAQVDELKVQLTK 1108
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerKINVLQKKIENLQEQLRD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1109 KEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdlsEELEALKTELEDTLDTTAAQQE 1188
Cdd:pfam10174 413 KDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL---EELESLKKENKDLKEKVSALQP 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1189 LRTKREQEVAELKkaledETKNHEAQIQDMRQRHATALE-ELSEQLEQAKRFKANLEKNKQGLETD--NKELACEVKVLQ 1265
Cdd:pfam10174 490 ELTEKESSLIDLK-----EHASSLASSGLKKDSKLKSLEiAVEQKKEECSKLENQLKKAHNAEEAVrtNPEINDRIRLLE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1266 QvkaesEHKRKKLDAQVQElhakvSEGDRLRVELAEkankLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELL 1345
Cdd:pfam10174 565 Q-----EVARYKEESGKAQ-----AEVERLLGILRE----VENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1346 QEETRQKLNLSSRiRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDV--- 1422
Cdd:pfam10174 631 KKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEIlem 709
|
410
....*....|..
gi 1039738673 1423 --EALSQRLEEK 1432
Cdd:pfam10174 710 kqEALLAAISEK 721
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
867-1221 |
1.27e-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: 43.96 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEELLKVKEKqtkvegeLEEMERKHQQLleekNILAEQLQAETELFAEAEEMRARLAAKKQELE---E 943
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEqdsE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 944 ILHDLESRVeeeeERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEAKIK-----KMEEEVLLLEDQNSKF 1018
Cdd:pfam05557 188 IVKNSKSEL----ARIPELEKELERLREHNKHLNENI------ENKLLLKEEVEDLKRKlereeKYREEAATLELEKEKL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1019 IKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMI---SDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1095
Cdd:pfam05557 258 EQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKeenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1096 QAQVDEL--KVQLTKKEEELQGALARGDDETLHKNNA----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL 1169
Cdd:pfam05557 338 KALVRRLqrRVLLLTKERDGYRAILESYDKELTMSNYspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQA 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039738673 1170 EALKTELeDTLDTTAAQQELRTKREqEVAELKKALEDetknHEAQIQDMRQR 1221
Cdd:pfam05557 418 QTLEREL-QALRQQESLADPSYSKE-EVDSLRRKLET----LELERQRLREQ 463
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1138-1503 |
1.34e-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: 43.57 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1138 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEalkteledtldttaaqqelrtkREQEVAELKKALEDETkNHEAQIQD 1217
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----------------------RRRKLEEAEKARQAEM-DRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1218 MRQRHATALEELSEQLEQAKRfKANLEKNKQgletdnKELACEVKVLQQVKAESEHKRKKLDAQVQELHA----KVSEGD 1293
Cdd:pfam17380 338 EQERMAMERERELERIRQEER-KRELERIRQ------EEIAMEISRMRELERLQMERQQKNERVRQELEAarkvKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1294 RLRvelaeKANKLQNELDNVSTLLEEAEKKGIKFakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQ 1373
Cdd:pfam17380 411 RQR-----KIQQQKVEMEQIRAEQEEARQREVRR------LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1374 EEEEEARKNLEKQ-VLALQSQLADTKKKVDDdlgtieslEEAKKKLLKdvealsQRLEEKVLAYdkLEKTKNRLQQELDD 1452
Cdd:pfam17380 480 EKEKRDRKRAEEQrRKILEKELEERKQAMIE--------EERKRKLLE------KEMEERQKAI--YEEERRREAEEERR 543
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039738673 1453 LTVDLDHQRQIVSNLEKKqkkfdqllaeekgisaryAEERDRAEAEAREKE 1503
Cdd:pfam17380 544 KQQEMEERRRIQEQMRKA------------------TEERSRLEAMERERE 576
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
914-1507 |
1.44e-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: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 914 AEQLQAETELfaeaEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQdleeqldeeegarqKLQLE 993
Cdd:pfam05557 2 AELIESKARL----SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR--------------LLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 994 KVTAEAKIKKMEEEVLLL---EDQNSKFIKEKKLMEDRIAECSSQLAEEeekaknLAKIRNKQEVMISDLEERLKKEEKT 1070
Cdd:pfam05557 64 EAEAEEALREQAELNRLKkkyLEALNKKLNEKESQLADAREVISCLKNE------LSELRRQIQRAELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1071 RQELEKAKRKLdgetTDLQDQIAELQAQVDELKVQLTK-KEEELQGALARGDDETlhknnaLKVARELQAQIAELQEDFE 1149
Cdd:pfam05557 138 QERLDLLKAKA----SEAEQLRQNLEKQQSSLAEAEQRiKELEFEIQSQEQDSEI------VKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1150 SEKASRNKAEKQKRD---LSEELEALKTELEdtldttaaqQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATA 1225
Cdd:pfam05557 208 RLREHNKHLNENIENkllLKEEVEDLKRKLE---------REEKYREEAATLELEKEkLEQELQSWVKLAQDTGLNLRSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1226 lEELSEQLEQAKRFKANLEKNKQGLETDnkelaceVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1305
Cdd:pfam05557 279 -EDLSRRIEQLQQREIVLKEENSSLTSS-------ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1306 LQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEearknLEK 1385
Cdd:pfam05557 351 LTKERDGYRAILESYDKE-LTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE-----REL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1386 QVLALQSQLAD---TKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYD--------------KLEKTKNRLQQ 1448
Cdd:pfam05557 425 QALRQQESLADpsySKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDydpkktkvlhlsmnPAAEAYQQRKN 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1449 ELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERdRAEAEAREKETKAL 1507
Cdd:pfam05557 505 QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESAELKNQRL 562
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1635-1889 |
1.53e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1635 LAVASKKKMEIDLKDLE--AQIEAANKARDEVIKQ--------LRKLQAQMKDYQRELEEARASRDEIFA--QSK--ESE 1700
Cdd:PHA02562 147 LSAPARRKLVEDLLDISvlSEMDKLNKDKIRELNQqiqtldmkIDHIQQQIKTYNKNIEEQRKKNGENIArkQNKydELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1701 KKLKSLEAEILQLQEELAsserarrhaeqerdELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSN-------- 1772
Cdd:PHA02562 227 EEAKTIKAEIEELTDELL--------------NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctq 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1773 -MELLNDRFRKTTLQVDTLNTELaaersaaQKSDNARQQLERQNKELKA---KLQELEGAVkSKFKATISALEAKIGQLE 1848
Cdd:PHA02562 293 qISEGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEIMDEFNEqskKLLELKNKI-STNKQSLITLVDKAKKVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039738673 1849 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQY 1889
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1258-1506 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1258 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1337
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1338 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSlqeqqeeeeearKNLE---KQVLALQSQLADTKKKVDDDLGTIESLEEA 1414
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGS------------ESFSdflDRLSALSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1415 KKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDR 1494
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|..
gi 1039738673 1495 AEAEAREKETKA 1506
Cdd:COG3883 229 AAAAAAAAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
988-1161 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 988 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLE------ 1061
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1062 --------------------ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1121
Cdd:COG3883 113 sfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039738673 1122 DETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQ 1161
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1608-1944 |
1.66e-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: 43.79 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1608 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDL-------KDLEAQIEAANKARDEVIKQLRkLQAQMKDYQR 1680
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVEMARELeelsareSDLEQDYQAASDHLNLVQTALR-QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1681 ELEEArasrdeifaqskesEKKLKSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAria 1760
Cdd:COG3096 355 DLEEL--------------TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL----------KSQLADYQQALDV--- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1761 QLEEELEEEQSNMELLNDRfrkTTLQVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQeLEGAVKSKFKATISAL 1840
Cdd:COG3096 408 QQTRAIQYQQAVQALEKAR---ALCGLPDLTPENAEDYLAAFRAK--EQQATEEVLELEQKLS-VADAARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1841 EAKIGQLE-EQLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRhadQYKEqMEKANARMKQLKRQLEEAEEEATRANA 1919
Cdd:COG3096 482 CKIAGEVErSQAWQTARE-------LLRRYRSQQALAQRLQQLRA---QLAE-LEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
330 340
....*....|....*....|....*
gi 1039738673 1920 SRRKLQRELDDATEANEGLSREVST 1944
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAE 575
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1098 |
1.83e-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: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKKQELEEILH 946
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 947 D--------------LESR-----VEEEEERNQILQNEKKKMQAHIQdleeqldeeegARQKLQLEKVTAEAKIKKMEEE 1007
Cdd:COG3883 94 AlyrsggsvsyldvlLGSEsfsdfLDRLSALSKIADADADLLEELKA-----------DKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1008 VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD 1087
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250
....*....|.
gi 1039738673 1088 LQDQIAELQAQ 1098
Cdd:COG3883 243 AASAAGAGAAG 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1676-1874 |
1.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1676 KDYQRELEEARASRDEIFAQSK---ESEKKLKSLEAeilqlQEELassERARRHAEQERDELADEIAnsasgksalldek 1752
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKkeaEAIKKEALLEA-----KEEI---HKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1753 rRLEARIAQLEeeleeeqsnmELLNDRFRkttlQVDTLNTELaaersaaqksDNARQQLERQNKELKAKLQELEGAVKSK 1832
Cdd:PRK12704 86 -KLEKRLLQKE----------ENLDRKLE----LLEKREEEL----------EKKEKELEQKQQELEKKEEELEELIEEQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039738673 1833 FKA--TISAL---EAKiGQLEEQLEQEAKERAAanKLVRRTEKKLKE 1874
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 ... |
1618-1755 |
1.99e-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: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1618 QVRELEAELEDERKQRALAVASKKKMEIdlkdLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR---------AS 1688
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarrrvlAP 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1689 RDEIFAQSKESEKKL-KSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1755
Cdd:pfam00529 135 IGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
987-1231 |
2.09e-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: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 987 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE--KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERL 1064
Cdd:COG5391 306 FEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVfaKRLEQNQNSILNEGVVQAETLRSSLKELLTQLQDEIKSRESLI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1065 KkeekTRQELEKAKrkldgettdlqdqiAELQAQVDELKVQLTKKEEElqgalargDDETLHKNNALKVARELQAQIAE- 1143
Cdd:COG5391 386 L----TDSNLEKLT--------------DQNLEDVEELSRSLRKNSSQ--------RAVVSQQPEGLTSFSKLSYKLRDf 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1144 LQEDFESEKasRNKAEKQKRDLSEELEALKTELEDTldTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1223
Cdd:COG5391 440 VQEKSRSKS--IESLQQDKEKLEEQLAIAEKDAQEI--NEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWK 515
|
....*...
gi 1039738673 1224 TALEELSE 1231
Cdd:COG5391 516 SVKEQLDR 523
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1065-1444 |
2.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1065 KKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAEL 1144
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELE---------------------QAREELEQL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1145 QEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKK---ALEDETKNHEAQIQDMRQR 1221
Cdd:COG4372 65 EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1222 HATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1301
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1302 KANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK 1381
Cdd:COG4372 225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1382 NLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKN 1444
Cdd:COG4372 305 AALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1664-1907 |
2.22e-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: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1664 VIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEE----LASSERARRHAE---QERDELAD 1736
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtLAKAQQVNAESErtlGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1737 EIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTlntelaAERSAAQKSDNarqQL 1811
Cdd:pfam06008 90 AIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE------AELKAAQDLLS---RI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1812 ERQNKELKAKLQELEGAVKSKfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKE 1891
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
250
....*....|....*.
gi 1039738673 1892 QMEKANARMKQLKRQL 1907
Cdd:pfam06008 237 TLKTARDSLDAANLLL 252
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
998-1990 |
2.30e-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: 43.12 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 998 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQlAEEEEKAKNLAKIRNKQEVMISDLE--------ERLKKEEK 1069
Cdd:TIGR01612 578 EKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDK-NEYIKKAIDLKKIIENNNAYIDELAkispyqvpEHLKNKDK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1070 TRQELEKAKRKL-DGETTDLQDQIA-----------ELQAQVDELKVQLTKKEEELQGAlargDDET--LHKNNALKVAR 1135
Cdd:TIGR01612 657 IYSTIKSELSKIyEDDIDALYNELSsivkenaidntEDKAKLDDLKSKIDKEYDKIQNM----ETATveLHLSNIENKKN 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1136 ELQAQIAELQEDFESEKAsrnkaekqkRDLSEELEALKT---ELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1212
Cdd:TIGR01612 733 ELLDIIVEIKKHIHGEIN---------KDLNKILEDFKNkekELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDN 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1213 AQIQDMRQRHATALE----------ELSEQLEQAKRFK----------ANLEKN-KQGLETDNKELAcevKVLQQVKAES 1271
Cdd:TIGR01612 804 IKDEDAKQNYDKSKEyiktisikedEIFKIINEMKFMKddflnkvdkfINFENNcKEKIDSEHEQFA---ELTNKIKAEI 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1272 EhkrkklDAQVQELHAKVSEGDRLrveLAEKANKLQNELDNVSTLLEEAEKkgIKFAKDAAGLESQLQDTQELLQEETRQ 1351
Cdd:TIGR01612 881 S------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTLKKVDEY--IKICENTKESIEKFHNKQNILKEILNK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1352 KLNLSsrirqleEEKNSLQeqqeeeeearKNLEKQvlaLQSQLADTKKKVDDDL--GTIESLEEAKKKLLKDVEALSQRL 1429
Cdd:TIGR01612 950 NIDTI-------KESNLIE----------KSYKDK---FDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANL 1009
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1430 ---EEKVL--AYDKLEKTKNRLQQELDDLTVDLDH-QRQIVSNLEKKQKKFDQLLAeeKGISARYAEERDRAEA------ 1497
Cdd:TIGR01612 1010 gknKENMLyhQFDEKEKATNDIEQKIEDANKNIPNiEIAIHTSIYNIIDEIEKEIG--KNIELLNKEILEEAEInitnfn 1087
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1498 EAREKetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ 1577
Cdd:TIGR01612 1088 EIKEK----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1578 AT---EDAKlRLEVNMQAMKAQFERDLQTRDEQNEekkrlLLKQVRELEAELEDERKQRALAVA---------------S 1639
Cdd:TIGR01612 1161 KAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEEVKGINLSygknlgklflekideE 1234
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1640 KKKMEIDLKDLEAQIEAAnkarDEVIKQLRKLQAQM---KDYQRELEEARASRDE-----IFAQSKES------EKKLK- 1704
Cdd:TIGR01612 1235 KKKSEHMIKAMEAYIEDL----DEIKEKSPEIENEMgieMDIKAEMETFNISHDDdkdhhIISKKHDEnisdirEKSLKi 1310
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1705 ----SLEAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEKRRLEARIAQLEEELEEEQSNMEL 1775
Cdd:TIGR01612 1311 iedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEK 1390
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1776 LNDRFR------------KTTL----------QVDTLNTELAAERSaaqKSDNARQQLERQNKELKAKLQELEGA----- 1828
Cdd:TIGR01612 1391 LIKKIKddinleeckskiESTLddkdidecikKIKELKNHILSEES---NIDTYFKNADENNENVLLLFKNIEMAdnksq 1467
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1829 --VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKlKEIFMQVEDE-------------RRHADQYKEQM 1893
Cdd:TIGR01612 1468 hiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDvtellnkysalaiKNKFAKTKKDS 1546
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1894 EKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE-------GLSREVSTLKNRLRRGGPISFSSSRSGRRQ 1966
Cdd:TIGR01612 1547 EIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDksnkaaiDIQLSLENFENKFLKISDIKKKINDCLKET 1626
|
1130 1140
....*....|....*....|....
gi 1039738673 1967 LHIEGASLELSDDDTESKTSDVND 1990
Cdd:TIGR01612 1627 ESIEKKISSFSIDSQDTELKENGD 1650
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1563-1949 |
2.34e-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: 43.09 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1563 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFerdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1642
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1643 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSKESEKKLKSLEAEILQLQEElasser 1722
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-------KIKELEKQLNQLKSEISDLNNQ------ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1723 arrhAEQERD-ELADEIANSAsgksallDEKRRLEARIAQLeeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAA 1801
Cdd:TIGR04523 304 ----KEQDWNkELKSELKNQE-------KKLEEIQNQISQN-------NKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1802 QKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVED 1881
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQ-INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738673 1882 ERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1949
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1643-1805 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1643 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ---RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAs 1719
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1720 seRARRHAEQE---RDELADEIANSASGKSALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAA 1796
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
....*....
gi 1039738673 1797 ERSAAQKSD 1805
Cdd:pfam00529 203 AKLDLERTE 211
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1088-1352 |
2.40e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1088 LQDQIAELQAQVDELKVQLTKKEEELQgalargddetLHKNNaLKVARELQAQ-IAELQEDFESEKASRNKAEKQKRDLS 1166
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIK----------TYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1167 EELEALKTELEdtlDTTAAQQELRTKReqevAELKKALEDETKNHEaqiqdMRQRHA---TALEELSEQLEQakrfkanL 1243
Cdd:PHA02562 241 DELLNLVMDIE---DPSAALNKLNTAA----AKIKSKIEQFQKVIK-----MYEKGGvcpTCTQQISEGPDR-------I 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1244 EKNKQGLetdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTL------- 1316
Cdd:PHA02562 302 TKIKDKL------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLvdkakkv 363
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039738673 1317 ---LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQK 1352
Cdd:PHA02562 364 kaaIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1051-1326 |
2.41e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1051 NKQEVMISDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHK 1127
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1128 NNALKVARELQAQIAELQEdfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK---REQEVAELKKAL 1204
Cdd:COG1340 81 DELNEKLNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKikeLEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1205 EDETKNHE--AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKElacevkvlqqvkaesehkRKKLDAQV 1282
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE------------------ADELHKEI 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039738673 1283 QELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIK 1326
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1336-1595 |
3.06e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1336 SQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAK 1415
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1416 KKLLKDVEALSQRLEEKVLAYDKLEKTK---NRLQQELDDL-------TVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-- 1483
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLewrqqteVLSPEEEKELVEKIKELEKELEKAKKALEKne 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1484 ----ISARYAEERDRAEAEAREKETkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1559
Cdd:COG1340 161 klkeLRAELKELRKEAEEIHKKIKE----LAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1039738673 1560 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1595
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1802-1950 |
3.07e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1802 QKSDNARQQLERQNKELKAKLQELEGAVkSKFKA---------TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1872
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL-EEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1873 KEIFMQVEDERRHAdqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA-NEGLSREVSTLKNRLR 1950
Cdd:COG3206 250 GSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELE 323
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
992-1119 |
3.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 992 LEKVTAEAKIKKMEEEVllledqnSKFIKE-KKLMEDRIAECSSQLAEEEEKAKNLA----KIRNKQevmISDLEERLK- 1065
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-------KRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFekelRERRNE---LQKLEKRLLq 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1066 KEEKTRQELEKAKRKlDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1119
Cdd:PRK12704 94 KEENLDRKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
857-965 |
3.32e-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: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 857 RVFTKVKPLLQVTRQEEELQAKDEELlkVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAA 936
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 1039738673 937 KKQELEEILHDLESRVEEEEERNQILQNE 965
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1535-1685 |
3.35e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.44 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1535 EDLMSSKD-DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQT---------- 1603
Cdd:COG1193 506 RELLGEESiDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAREEAEEilrearkeae 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1604 ------RDEQNEEKK-RLLLKQVRELEAELEDERKQRA-----------------------------LAVASKK------ 1641
Cdd:COG1193 586 elirelREAQAEEEElKEARKKLEELKQELEEKLEKPKkkakpakppeelkvgdrvrvlslgqkgevLEIPKGGeaevqv 665
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1642 ---KMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL-------EEA 1685
Cdd:COG1193 666 gilKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSKASTVSPELdlrgmrvEEA 719
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1541-1716 |
3.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1541 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqamkaQFERDLQTRDEQNEEKKrlllkqvR 1620
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE---------------KLKEELEEKKEKLQEEE-------D 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1621 ELEAELEDERKQRalavaskkkmeidlkdleaqIEAANKARDEVIKQLRKLQAQMKDYQ--RELEEARASRDEIfAQSKE 1698
Cdd:PRK00409 566 KLLEEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKGGYASVkaHELIEARKRLNKA-NEKKE 624
|
170
....*....|....*...
gi 1039738673 1699 SEKKLKSLEAEILQLQEE 1716
Cdd:PRK00409 625 KKKKKQKEKQEELKVGDE 642
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
867-1019 |
3.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEellkVKEKQTKVEGELEEMERKHQQ----LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELE 942
Cdd:PRK12704 52 EAIKKEALLEAKEE----IHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 943 EILHDLEsrveeeeernQILQNEKKKMQaHIQDLEEQLdeeegARQKLqLEKVTAEAK------IKKMEEEVLLLEDQNS 1016
Cdd:PRK12704 128 KKEEELE----------ELIEEQLQELE-RISGLTAEE-----AKEIL-LEKVEEEARheaavlIKEIEEEAKEEADKKA 190
|
...
gi 1039738673 1017 KFI 1019
Cdd:PRK12704 191 KEI 193
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
987-1245 |
3.41e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 987 RQKlQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKlMEDRIAECssqlaEEEEKAKNLAKI-RNKQEVMISDLEERLK 1065
Cdd:pfam02029 85 RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEK-RDSRLGRY-----KEEETEIREKEYqENKWSTEVRQAEEEGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1066 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1145
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1146 EDFESEKASRNKAEKQKRDL----SEELEALKTEledtldttaaQQElrtkREQEVAELKKALEDETKNHEAQIQDMRQr 1221
Cdd:pfam02029 238 EEAEVFLEAEQKLEELRRRRqekeSEEFEKLRQK----------QQE----AELELEELKKKREERRKLLEEEEQRRKQ- 302
|
250 260
....*....|....*....|....
gi 1039738673 1222 hATALEELSEQlEQAKRFKANLEK 1245
Cdd:pfam02029 303 -EEAERKLREE-EEKRRMKEEIER 324
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1052 |
3.58e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 867 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLL------EEKNILAEQLQAETelFAEAEEMRARLAAKKQE 940
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlGRQPPLALLLSPED--FLDAVRRLQYLKYLAPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 941 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 1020
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEE-------ERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
170 180 190
....*....|....*....|....*....|..
gi 1039738673 1021 EKKLMEDRIAECSSQLAEEEEKAKNLAKIRNK 1052
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1180-1453 |
3.74e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1180 LDTTAAQQELRTK-RE--QEVAELKKALEdETKNHEAQIQDMRQRHATALEELS---------EQLEQAKRFKANLEKNK 1247
Cdd:COG0497 147 LDAFAGLEELLEEyREayRAWRALKKELE-ELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1248 QGLETDNKELA-CEVKVLQQV-KAESE-HKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNVSTlleeaekkg 1324
Cdd:COG0497 226 EALQEALEALSgGEGGALDLLgQALRAlERLAEYDPSLAELAERLES---ALIELEEAASELRRYLDSLEF--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1325 ikfakdaaglesqlqDTQELlqEETRQKLNLssrIRQLeeeknslqeqqeeeeeARK---NLEkQVLALQSQLADTKKKV 1401
Cdd:COG0497 294 ---------------DPERL--EEVEERLAL---LRRL----------------ARKygvTVE-ELLAYAEELRAELAEL 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1402 DDDLGTIESLEEAKKKLLKDVEALSQRLEEK-VLAYDKLEKtknRLQQELDDL 1453
Cdd:COG0497 337 ENSDERLEELEAELAEAEAELLEAAEKLSAArKKAAKKLEK---AVTAELADL 386
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
999-1237 |
3.80e-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: 42.45 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 999 AKIKKMEEEVLLLEDqnskFIKEKKLMEDRIAECSSQLAEEEEKAkNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1078
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEKKL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1079 RKLDGETTDLQDQiAELQAQVDELKVQLTKKEEELQGALArgddetlHKNNALKVARELQAQIAELQEDFESEKAS---- 1154
Cdd:pfam18971 638 ESKSGNKNKMEAK-AQANSQKDEIFALINKEANRDARAIA-------YTQNLKGIKRELSDKLEKISKDLKDFSKSfdef 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1155 RNKAEKQKRDLSEELEALKTELED----------TLDTTAAQQELRTKREQEVAELKKALEDetknHEAQIQD--MRQRH 1222
Cdd:pfam18971 710 KNGKNKDFSKAEETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSD----LENSVKDviINQKV 785
|
250
....*....|....*
gi 1039738673 1223 ATALEELSEQLEQAK 1237
Cdd:pfam18971 786 TDKVDNLNQAVSVAK 800
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1647-1740 |
3.88e-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: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1647 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES--EKKLKSLEAEILQLQEELAsserar 1724
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAiaRKEIKDLQKELEKLNEEYA------ 196
|
90
....*....|....*.
gi 1039738673 1725 RHAEQERDELADEIAN 1740
Cdd:cd22656 197 AKLKAKIDELKALIAD 212
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1638-1739 |
4.35e-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: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1638 ASKKKMEID-----LKDLEAQIEAANKARDEVIK-----------QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1701
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039738673 1702 KLKSLEAEILQLQEELAS-SERARRHAEQERDEL-ADEIA 1739
Cdd:COG0542 479 ELEQRYGKIPELEKELAElEEELAELAPLLREEVtEEDIA 518
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
868-1231 |
4.58e-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: 42.04 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 868 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELeeilHD 947
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEN----SS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 948 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV------LLLEDQNSKFIKE 1021
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILesydkeLTMSNYSPQLLER 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1022 KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKeeKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1101
Cdd:pfam05557 382 IEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA--LRQQESLADPSYSKEEVDSLRRKLETLELERQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1102 LKVQLTKKEEELQGALARGDDET-------LHKNNALKVARELQAQIAELQEDFESekasrnkaekqkrdLSEELEALKT 1174
Cdd:pfam05557 460 LREQKNELEMELERRCLQGDYDPkktkvlhLSMNPAAEAYQQRKNQLEKLQAEIER--------------LKRLLKKLED 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1175 ELEDTLdttAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSE 1231
Cdd:pfam05557 526 DLEQVL---RLPETTSTMNFKEVLDLRKELESA----ELKNQRLKEVFQAKIQEFRD 575
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1044-1399 |
4.66e-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: 41.92 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1044 KNLAKIRNKQEVMISDLEERLKKE--EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKKEEELQGALARGD 1121
Cdd:NF033838 91 KKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAE----KKAKDQKEEDRRNY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1122 DETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKAE-KQKRDLSEELEALKTELEDtLDTTAAQQELRTKREQEvAE 1199
Cdd:NF033838 167 PTNTYKTLELEIAEsDVEVKKAELELVKEEAKEPRDEEKiKQAKAKVESKKAEATRLEK-IKTDREKAEEEAKRRAD-AK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1200 LKKALEDETKNHEAQIQDMRQRHAtALEELSEqlEQAKRFKANLEKNKQGLET--------DNKELACEVKVLQQVKA-- 1269
Cdd:NF033838 245 LKEAVEKNVATSEQDKPKRRAKRG-VLGEPAT--PDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVEEAKKKak 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1270 --ESEHKR-------KKLDAQVQELHAKVSEGDrlrVELA-EKANKLQNElDNVSTLLEEAEKKgikfAKDAAGLESQLQ 1339
Cdd:NF033838 322 dqKEEDRRnyptntyKTLELEIAESDVKVKEAE---LELVkEEAKEPRNE-EKIKQAKAKVESK----KAEATRLEKIKT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1340 DTQELlQEETRQKLNLSSRIRQLEEEK-------------------------NSLQEQQEEEEEARKNLEKQVLALQSQL 1394
Cdd:NF033838 394 DRKKA-EEEAKRKAAEEDKVKEKPAEQpqpapapqpekpapkpekpaeqpkaEKPADQQAEEDYARRSEEEYNRLTQQQP 472
|
....*
gi 1039738673 1395 ADTKK 1399
Cdd:NF033838 473 PKTEK 477
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1238-1503 |
4.81e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1238 RFKANLEKNKQgLETDNKELACEVKVLQQVK-AESEHKRKKLDAQVQELHAKVsegdrlrVELAEKANKLQNELDNVSTL 1316
Cdd:pfam00038 12 RLASYIDKVRF-LEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQL-------DTLTVERARLQLELDNLRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1317 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLqeqqeeeeeaRKNLEKQVLALQSQLAD 1396
Cdd:pfam00038 84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFL----------KKNHEEEVRELQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1397 TKKKVD------DDLGTI-----ESLEEAKKKLLKDVEAL-SQRLEEKVLAYDK----LEKTKNRLQQ---ELDDLTVDL 1457
Cdd:pfam00038 154 TQVNVEmdaarkLDLTSAlaeirAQYEEIAAKNREEAEEWyQSKLEELQQAAARngdaLRSAKEEITElrrTIQSLEIEL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039738673 1458 DHQRQIVSNLEKKqkkfdqlLAEEKgisARYAEERDRAEAEAREKE 1503
Cdd:pfam00038 234 QSLKKQKASLERQ-------LAETE---ERYELQLADYQELISELE 269
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1097-1215 |
5.42e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1097 AQVDELKVQLTKKEEELQgALARGDDETLHKNnalkvARELQAQIAELQEDFESEKAsRNKAEKQkrdLSEELEALKTEL 1176
Cdd:COG0542 411 EELDELERRLEQLEIEKE-ALKKEQDEASFER-----LAELRDELAELEEELEALKA-RWEAEKE---LIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039738673 1177 EDTLDTTAAQQELRTKREQEVAELKKALEDE-TKNHEAQI 1215
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAEV 520
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1066-1109 |
5.42e-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: 5.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1039738673 1066 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKK 1109
Cdd:cd23165 60 SLEEAQERLEKAKEELEEEIEKLEEEIDEIEEEMKELKVQLYAK 103
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1033-1277 |
5.46e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1033 SSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL----------------Q 1096
Cdd:pfam15905 72 SKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellkakfsedgtQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1097 AQVDELKVQLTKKEEEL----QGALARGDDETLHKNNALKVARELQAQIAELQE---DFESEKASRNKAEKQKRDLSEEL 1169
Cdd:pfam15905 152 KKMSSLSMELMKLRNKLeakmKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEKIEEKSETEKLLEYITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1170 EALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQg 1249
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD--------LNEKCKLLESEKEELLREYEEKE- 302
|
250 260
....*....|....*....|....*...
gi 1039738673 1250 lETDNKELACEVKVLQQVKAESEHKRKK 1277
Cdd:pfam15905 303 -QTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1427-1894 |
5.58e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1427 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL---LAEEKGISARYAEERDRAEAEAREKE 1503
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1504 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKR-----------------ALEQQVEEMR 1566
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1567 TQLEELEDELQATEDAKLRLEVnMQAMKAQFERDLQTRDEQNEEKKRL---------LLKQVRELEAELEDERKQRALAV 1637
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELegyemdynsYLKSIESLKKKIEEYSKNIERMS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1638 ASKKKMeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKSLEAEIL------ 1711
Cdd:PRK01156 391 AFISEI---LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL-------SRNMEMLNGQSVcpvcgt 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1712 QLQEElaSSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARiaqleeELEEEQSNMELLNDRFRKTTLQVDTLN 1791
Cdd:PRK01156 461 TLGEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR------KEYLESEEINKSINEYNKIESARADLE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1792 TELAAERSAAQKSDNARQQLERQNKelkAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQeakeraaANKLVRRTEKK 1871
Cdd:PRK01156 533 DIKIKINELKDKHDKYEEIKNRYKS---LKLEDLDSKRTSWLNALAVISLIDIETNRSRSNE-------IKKQLNDLESR 602
|
490 500
....*....|....*....|...
gi 1039738673 1872 LKEIFMQVEDERRHADQYKEQME 1894
Cdd:PRK01156 603 LQEIEIGFPDDKSYIDKSIREIE 625
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1550-1758 |
5.60e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1550 ELEKSKRALEQQVEEMRTQLEELEdeLQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELE 1623
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLpdflehAKEQNKELK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1624 AELEderkqralavASKKKMEIDLKDLEAQieaankarDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1703
Cdd:PRK04778 331 EEID----------RVKQSYTLNESELESV--------RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1704 KSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAR 1758
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERY----------RNKLHEIKRYLEKS 437
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1658-1904 |
6.08e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1658 NKARDEVIKQLRKLQA-QMKDYQRE-----LEEARASRDEI------FAQSKESEKKLKSLEAEIlqlqeELASSERARR 1725
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEElsnerLRKLRSLLTKLsealdkLRSYLPKLNPLREEKKKV-----SVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1726 HAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQ------SNMELLNDrFRKTTLQVDTLNTELAAERS 1799
Cdd:PRK05771 90 DVEEELEKIEKEI-------KELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLG-FKYVSVFVGTVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1800 AAQKSDNA-----------------RQQLERQNKELK-AKLQELEGAVKSKFKATISALEAKIGQLEEQLEqeakeraaa 1861
Cdd:PRK05771 162 LESDVENVeyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039738673 1862 nklvrRTEKKLKEIFMQVEDERRHADQYKEQM-EKANARMKQLK 1904
Cdd:PRK05771 233 -----SLLEELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1088-1279 |
6.47e-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: 40.49 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1088 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD--ETL----HKNNAL--------KVARELQAQIAELQEDFESEKA 1153
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKflENLaslkHENDNLssmlnrkeRRLKDLEDQLSELKNSYEELTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1154 SRNKAEKQKRDLSEELEALKTELE------DTLdtTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQR---HAT 1224
Cdd:pfam17078 88 SNKQLKKRLENSSASETTLEAELErlqiqyDAL--VDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRissNDK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1225 ALEELSEQLEQAKRFKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLD 1279
Cdd:pfam17078 166 DIDTKLDSYNNKFKNLDNIYVNKnNKLLTKLDSLAQLLDLPSWLNLYPESRNKILE 221
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1060-1234 |
6.79e-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: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1060 LEERLKKEEKTRQELEK-----AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARgddetlhknNALKVA 1134
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQ---------NVEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1135 RELQAQIAELQEDFesekasRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELKKALEDETK 1209
Cdd:pfam01442 73 QRLEPYTEELRKRL------NADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*....
gi 1039738673 1210 NHEAQ----IQDMRQRHATALEELSEQLE 1234
Cdd:pfam01442 147 EVQAQlsqrLQELREKLEPQAEDLREKLD 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
903-1112 |
7.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 903 HQQLLEEKNILAEQLQAE-----TELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQahiqdle 977
Cdd:PHA02562 200 YNKNIEEQRKKNGENIARkqnkyDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 978 eqldeeegarqklQLEKV-----------TAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNL 1046
Cdd:PHA02562 273 -------------QFQKVikmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738673 1047 AKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE 1112
Cdd:PHA02562 340 LELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1136-1439 |
7.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1136 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAledetknheaqi 1215
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1216 qdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVlQQVKAESEHKRKKLDAQVQELHAkvsegdrl 1295
Cdd:COG1340 80 ---RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-QQTEVLSPEEEKELVEKIKELEK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1296 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1375
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKELRKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738673 1376 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKllKDVEALSQRLEEKVLAYDKL 1439
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKKGEKL 282
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1651-1752 |
7.50e-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: 39.00 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1651 EAQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKslEAEILQLQEELAS-SERARRHAEQ 1729
Cdd:COG0711 37 ADGLAEAERAKEE-------AEAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAEIEQ 107
|
90 100
....*....|....*....|...
gi 1039738673 1730 ERDELADEIANSASGKSALLDEK 1752
Cdd:COG0711 108 ERAKALAELRAEVADLAVAIAEK 130
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
871-1078 |
7.62e-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: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 871 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQ-QLLEEKNILAEQLQAETELFAE--AEEMRARlaakKQELEEilhd 947
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQrRLQQEQLERAEKMREELELEQQrrFEEIRLR----KQRLEE---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 948 lESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQnskfikeKKLM- 1025
Cdd:pfam15709 399 -ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAeKQRQKELEMQLAEEQ-------KRLMe 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738673 1026 --EDRIAECSSQLAEEEEKAKNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1078
Cdd:pfam15709 471 maEEERLEYQRQKQEAEEKARLEAEERRQKE----EEAARLALEEAMKQAQEQAR 521
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
1467-1659 |
7.74e-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: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1467 LEKKQKKFDQLLAEEKGISARYAEERDRAEAeAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD-DVG 1545
Cdd:COG5414 202 IEEVEKKVDDLLEKDMKAESVSVVLKDEKEL-ARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGMSEEDlDVG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1546 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLrlevnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAE 1625
Cdd:COG5414 281 AAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEI-----------GEEKEEDDENEENERHTELLADELNELEKG 349
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039738673 1626 LEDERKQ--RALAVASKKKMEIDLKDLEAQIEAANK 1659
Cdd:COG5414 350 IEEKRRQmeSATNPILQKRFESQLNVLLKELELKRK 385
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
861-1101 |
7.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 861 KVKPLLQVTRQEEELQAKDEELLKVK------------------EKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETE 922
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKelaeqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 923 LFAEAEEMRARLAAKKQELEEILHDLESR----VEEEEERNQILQ----------NEKKKMQAHIQDLEEQLDEEEGARQ 988
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 989 KLQLekvtAEAKIKKMEEEvllLEDQNSKFIKEK-KLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKE 1067
Cdd:PRK03918 634 ELAE----TEKRLEELRKE---LEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
250 260 270
....*....|....*....|....*....|....
gi 1039738673 1068 EKTRQELEKAKRKLDgETTDLQDQIAELQAQVDE 1101
Cdd:PRK03918 707 EKAKKELEKLEKALE-RVEELREKVKKYKALLKE 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
962-1117 |
7.93e-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: 40.29 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 962 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFikEKKLMEDRIAECSSQLAEEEE 1041
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738673 1042 KAKNLAKIRNKQEVMISDLEERLKKE-EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1117
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEElAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1198-1469 |
7.93e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1198 AELKKALEDETK--NHEAQIQDMRQRHATaleelsEQLEQAKRFKANLEKnKQGLETDNKELacevKVLQQVKAESEHKr 1275
Cdd:PHA02562 166 SEMDKLNKDKIRelNQQIQTLDMKIDHIQ------QQIKTYNKNIEEQRK-KNGENIARKQN----KYDELVEEAKTIK- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1276 kkldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAA---GLESQLQDTQELLQEETRQK 1352
Cdd:PHA02562 234 ----AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcpTCTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1353 LNLSSRIRQLEEEKNSLQEQQEEEEEARKNLekqvLALQSQLADTKkkvdddlGTIESLEEAkkklLKDVEALSQRLEEK 1432
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKL----LELKNKISTNK-------QSLITLVDK----AKKVKAAIEELQAE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039738673 1433 VLAYDK-LEKtknrLQQELDDLTVDLD------HQRQIVSNLEK 1469
Cdd:PHA02562 374 FVDNAEeLAK----LQDELDKIVKTKSelvkekYHRGIVTDLLK 413
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1702-1951 |
8.04e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1702 KLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1781
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1782 KTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATisALEAKIGQLEEQLEqEAKERAAA 1861
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK--ELVEKIKELEKELE-KAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1862 NKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSRE 1941
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|
gi 1039738673 1942 VSTLKNRLRR 1951
Cdd:COG1340 239 LRELRKELKK 248
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1402-1942 |
8.08e-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: 41.25 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1402 DDDLGTIESLEEAKKKLLKDVEALSQ--------------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL 1467
Cdd:pfam05483 67 DSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkqkenKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1468 EKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlMSSKDDVGKN 1547
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1548 VHELEKSKRAL---EQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKaQFERDLQTRDEQNEEkkrlLLKQVRELEA 1624
Cdd:pfam05483 225 QHLEEEYKKEIndkEKQVSLLLIQITEKENKMK---DLTFLLEESRDKAN-QLEEKTKLQDENLKE----LIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1625 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE----SE 1700
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1701 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANsasgKSALLDEKRRLEaRIAQLEEELEeeQSNMELLNDRF 1780
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEKKQFE-KIAEELKGKE--QELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1781 RkttlQVDTLNTELAAERSAaqksdnaRQQLERQNKELKAKLQelegavKSKFKAT-ISALEAKIGQLEEQLEQEA---- 1855
Cdd:pfam05483 450 K----EIHDLEIQLTAIKTS-------EEHYLKEVEDLKTELE------KEKLKNIeLTAHCDKLLLENKELTQEAsdmt 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1856 ----KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDA 1931
Cdd:pfam05483 513 lelkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570
....*....|.
gi 1039738673 1932 TEANEGLSREV 1942
Cdd:pfam05483 593 ENKCNNLKKQI 603
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1092-1244 |
8.31e-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: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1092 IAELQAQVDELKVQLTKKEEELQGALARGDD-ETLHKNNALkvareLQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1170
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRlQALESELAI-----SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1171 ALKTELED------TLDTT-AAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL 1243
Cdd:pfam00529 128 RRRVLAPIggisreSLVTAgALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDL 207
|
.
gi 1039738673 1244 E 1244
Cdd:pfam00529 208 E 208
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
872-1115 |
8.80e-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: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 872 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEK----NILAEQLQA-------ETELFAEAEEMRARLAAKKQE 940
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvNAGSERLRAvkdikqeRDQLLNEVKTSRNELNSLSED 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 941 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGA-------RQKLQLEKVTAEAKIKKMEEEVLLLED 1013
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghamkvAMGMQKQITAKRGQIDALQSKIQFLEE 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1014 QNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAkirNKQEVMISdlEERLKKEEKTRQELEKAKRKLdgETTDLQDQIA 1093
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA---GELEVLRS--QERRLKEKVANMEVALDKASL--QFAECQDIIQ 828
|
250 260
....*....|....*....|..
gi 1039738673 1094 ELQAQVDELKVQLTKKEEELQG 1115
Cdd:pfam15921 829 RQEQESVRLKLQHTLDVKELQG 850
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1186-1397 |
8.82e-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: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1186 QQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1265
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1266 QVKAESEHKRKKLDAQ-VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEL 1344
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039738673 1345 LQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADT 1397
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
878-1095 |
8.99e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 878 KDEELLKVKEKQTKVEGELEEMErkhqQLLEEKNILAEQLQAETelFAEAEEMRarlaakkQELEEILHDLESRVEEEEE 957
Cdd:PRK05771 41 SNERLRKLRSLLTKLSEALDKLR----SYLPKLNPLREEKKKVS--VKSLEELI-------KDVEEELEKIEKEIKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 958 RNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKFIKEKKLME---------- 1026
Cdd:PRK05771 108 EISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgTVPEDKLEELKLESDVENVEYISTDKGyvyvvvvvlk 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738673 1027 DRIAECSSQLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1095
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
995-1199 |
9.13e-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: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 995 VTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKaknLAKIRNKQEVMISDLEERLKKEEKTRQEL 1074
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1075 EKAKRKL--DGETTD-----------------------LQDQIAELQAQVDELKVQLTKKEEELQGALARGDDEtlhKNN 1129
Cdd:COG3883 89 GERARALyrSGGSVSyldvllgsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEAL---KAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1130 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1199
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1226-1627 |
9.20e-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: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1226 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1305
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1306 LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEK 1385
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR-------KEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1386 QVLALQSQLADTKKKVdddlgtiesleeakkkllkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1465
Cdd:pfam07888 193 EFQELRNSLAQRDTQV-------------------------LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1466 NLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKeTKALSLARALEEALEAKEEFERQNKQLRADMEdlmssKDDVG 1545
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL-TLQLADASLALREGRARWAQERETLQQSAEAD-----KDRIE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1546 KNVHELEKskraLEQQVEEMRTQLEELEDELQATEDAKL----RLEVNMQAMKAQFeRDLQTRDEQNEEKKRLLLKQVRE 1621
Cdd:pfam07888 322 KLSAELQR----LEERLQEERMEREKLEVELGREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQ 396
|
....*.
gi 1039738673 1622 LEAELE 1627
Cdd:pfam07888 397 LEQRLE 402
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
986-1289 |
9.48e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.04 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 986 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEE-EKAKNLAKIRNK--QEVMISDLEE 1062
Cdd:pfam15964 390 LRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEmDVTKVCGEMRYQlnQTKMKKDEAE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1063 RLKKEEKTR---------QELEKAKRKLDGETTDL-QDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHK---NN 1129
Cdd:pfam15964 470 KEHREYRTKtgrqleikdQEIEKLGLELSESKQRLeQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQsfsNE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1130 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-QELRTKREQEVAELKKaledET 1208
Cdd:pfam15964 550 AKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKlEEITQKSRSEVEQLSQ----EK 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738673 1209 KNHEAQIQDMRQRHatalEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAK 1288
Cdd:pfam15964 626 EYLQDRLEKLQKRN----EELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
.
gi 1039738673 1289 V 1289
Cdd:pfam15964 702 V 702
|
|
| |
