|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1928 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1484.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 848 TRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 927
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 928 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDR 1007
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1008 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAK 1087
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1088 KEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1167
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1168 LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1247
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1248 AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1327
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1328 TRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQR 1407
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1408 LEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALS 1487
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1488 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1568 NMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1647
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1648 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSAL 1727
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1728 LDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGS 1807
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1808 VKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1887
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 2024363113 1888 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1450.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 339 SHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKADFCII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 2024363113 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-771 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1329.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP-GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 337 GFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK-FQKPRQLKDKADF 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgldqvtgitETAFGSAYKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 656 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 2024363113 736 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1233.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 335 IMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGsAYKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 2024363113 735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1205.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 339 SHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKADFCII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 2024363113 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1201.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 339 SHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKADFCII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 2024363113 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1184.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN----IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 335 IMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITEtaFGSAYKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 2024363113 735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1165.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASS---------HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 250 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 330 MEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKpRQL 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrIVGLDQVTgITETAFGSayKTKKGM 649
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024363113 730 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1147.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQETMEAMHIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 339 SHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKADFCII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSayKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 2024363113 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-771 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1113.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 247 RINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDN 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 326 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 566 PRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETafgsAYKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST----PKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 646 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2024363113 726 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-783 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1021.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIP 318
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGgCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 319 GQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGMNVMEFTRAIL 397
Cdd:smart00242 235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 398 TPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQ 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 558 GTHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivgldqvtgitet 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 638 afGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 534 --GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 718 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1348 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 922.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 36 VWIPSERHGFEAASIKEERGDEVLVELA---ENGKKALVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 191 VIQYLAHVASSHkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 271 AVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFSHDEILSMLKV 349
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 350 VSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATY 429
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 430 ERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 510 DFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGTHSKFQKPRQLKDKadFCIIHYAGKVDYK 587
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 588 ADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVgldqvtgitetafgsayktKKGMFRTVGQLYKESLTKLMAT 667
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 668 LRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMDG 743
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 744 KQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLSALKILQRNC 823
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 824 AAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKqtkveaeleemerkhqqlLEEKNILAEQLQAETELF 903
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKT------------------IKREKKLRETEEVEFSLK 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 904 AEAEEMRARLAAKKQELEEILHDLESRVeeeeernQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKM 983
Cdd:COG5022 844 AEVLIQKFGRSLKAKKRFSLLKKETIYL-------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLS 916
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 984 EEEILLLEDQNSKFLKEKKLMEDRIAECTS--QLAEEEEKAKNLAKLKNKQEmMITDLEERLKKEEKTRQELEKAKRKLD 1061
Cdd:COG5022 917 SDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESKLKE-TSEEYEDLLKKSTILVREGNKANSELK 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1062 G---ETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGDEEavqknnalkviRELQAQIAELQEdlesekaSRNKAE 1138
Cdd:COG5022 996 NfkkELAELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSE-----------STELSILKPLQK-------LKGLLL 1056
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1139 KQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNH--EAQIQEIRQRHATALEELSEQLEQAK 1216
Cdd:COG5022 1057 LENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLvkPANVLQFIVAQMIKLNLLQEISKFLS 1136
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1217 RFKANLEKNKQGLESDNKELACevkVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSS-- 1294
Cdd:COG5022 1137 QLVNTLEPVFQKLSVLQLELDG---LFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSki 1213
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1295 --------LLEEAEKKGI------KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1348
Cdd:COG5022 1214 fsgwprgdKLKKLISEGWvpteysTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-771 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 868.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQDKDNFQETMEA 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 333 MHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQL 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 570 KDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkdvdrivgldqvtgitetafgsayktkkgm 649
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 650 frtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024363113 730 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 785.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVA------SSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 331 EAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 491 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPR-- 567
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 568 -QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKD-VDRIVGLDQVTGITETafgsayKT 645
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENyVGSDSTEDPKSGVKEK------RK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 646 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2024363113 726 QRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 775.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSH--KGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 336 MGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPRQLKDKAD 574
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 --FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitETAFGSAYKTKKGMFRT 652
Cdd:cd14913 477 ahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--------DSGKKKVAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14913 549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2024363113 733 PNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 629 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 753.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPRQLK---DKA 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitETAFGSAYKTKKGM-FRT 652
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG--------GGEQAKGGRGKKGGgFAT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14909 549 VSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILN 628
|
650 660 670
....*....|....*....|....*....|....*....
gi 2024363113 733 PNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14909 629 PAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 741.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPRQLKDK---A 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivgldqvtgitETAFGSAYKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 2024363113 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-771 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 727.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGrkDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 418 DFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 497 EEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK--FQKPRQLKDKad 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSsdkfvaelwkdvdrivgldqvtgitetafgsayKTKKgmfRTVG 654
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------KNRK---KTVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 2024363113 735 AIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 594 KEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 719.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 337 GFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPRQLKDK--A 573
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivglDQVTGiTETAFGSAYKTKKGMFRTV 653
Cdd:cd14929 472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKKRKKGASFQTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14929 544 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 2024363113 734 NAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 624 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 708.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 336 MGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPRQLKDK-- 572
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKpe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdriVGLDqvtGITETAFGsayKTKKG-MFR 651
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGAD---APIEKGKG---KAKKGsSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 652 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14917 548 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2024363113 732 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 628 NPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-771 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 692.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 181 GAGKTENTKKVIQYLAHVASSHKGRKDHN--IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPRQLKDKAD-- 574
Cdd:cd14918 402 EYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgldqVTGITETAFGSAYKTKKGMFRTVG 654
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 2024363113 735 AIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 631 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 690.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 334 HIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPRQLKDK 572
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdriVGLDqvTGitETAFGSAYKTKKGMF 650
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASAD--TG--DSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024363113 731 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 335 IMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPRQLKDKA 573
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitETAFGSAYK--TKKG- 648
Cdd:cd14912 478 EahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--------ASAGGGAKKggKKKGs 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 649 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14912 550 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2024363113 729 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 630 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 688.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 335 IMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPRQLKDK- 572
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKv 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgldqVTGITETAFGSAYKTKKG-MF 650
Cdd:cd14910 478 eAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGKKKGsSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024363113 731 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 685.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHN---IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 335 IMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPRQLKDKA 573
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdriVGLDQVTGITETAFGsayKTKKGMFR 651
Cdd:cd14923 477 EahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---KKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 652 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14923 551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2024363113 732 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 631 NASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 677.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEaasgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 334 HIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPRQLKDK 572
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgldqvTGITETAFGSAYKTKKG-M 649
Cdd:cd14915 477 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------TAEAEGGGGKKGGKKKGsS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2024363113 730 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-771 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 652.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 337 GFSHDEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 496 QEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKADF 575
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgLDQVTGITETAFGSAYKTKKGMFR-TVG 654
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD----LLALTGLSISLGGDTTSRGTSKGKpTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*..
gi 2024363113 735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 625 ARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-771 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 650.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER-----VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 339 SHDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---RDYVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 496 QEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGTHSKFQKPRQLKD--K 572
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgldqvtgitetafgsayKTKKGMFRT 652
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 2024363113 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-771 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 648.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 339 SHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 499 YQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRqlkDKAdFCII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER---GGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSayktkkgMFRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS-------QKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 2024363113 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-771 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 614.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDK 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkDVDRIVGLDqvtgitetafgSAYKTKkgmfrT 652
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKSP-----T 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 2024363113 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-771 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 610.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVA--SSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGgrAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDNFQETMEAM 333
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 334 HIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGRD-YVQ 409
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIVTPDgIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRql 569
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgldqvtgiteTAFGSAYKtkkgm 649
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------EGTSSSSK----- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd01384 529 FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024363113 730 ILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 609 LLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-771 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 581.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQETMEAMHIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRAILTPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 486 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 566 PRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdvdrivgldqvTGITET 637
Cdd:cd01382 450 PRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------------ESSTNN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 638 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 518 NKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 718 RIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-771 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 577.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV-GRDYVQKAQT 413
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKA 573
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgLDQVTgitetafgsayktkkgMFRTV 653
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQKT----------------SKVTL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtP 733
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-V 605
|
650 660 670
....*....|....*....|....*....|....*....
gi 2024363113 734 NAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 606 KTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
2.58e-176 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 551.30 E-value: 2.58e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGeaaseaieqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 244 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 324 DNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 401
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 402 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 481
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 482 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQEQG 558
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASFG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 559 T-------------HSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdkfvaelwkdvdri 625
Cdd:cd14890 477 RksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 626 vgldqvTGITETafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 705
Cdd:cd14890 542 ------RSIREV--------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 706 EGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
2.60e-175 |
|
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: 548.58 E-value: 2.60e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHkgrkdhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQlkDKAD 574
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgLDQVTGITETAFGSAYKTKKGMFRTVG 654
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFVTMKPRTPTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*...
gi 2024363113 735 AIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 621 KLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
8.12e-171 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 536.28 E-value: 8.12e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 337 GFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGTHSKFQK----PRqlK 570
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR--T 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 571 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrIVGLDQVTGITETAFGSAYKTKKGMF 650
Cdd:cd14903 461 SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024363113 731 LTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 618 FLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
7.39e-170 |
|
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: 535.03 E-value: 7.39e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLahVASSHKGrkdHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG--SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPrQLKD 571
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 572 KAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdvdriVGLDQVT----GITETAFGSAY---- 643
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfrwAVLRAFFRAMAafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 644 ----------------------------KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLV 695
Cdd:cd01385 541 agrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 696 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
1.08e-168 |
|
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: 530.52 E-value: 1.08e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 249 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 327 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 485 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 561 SKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdvdrivgldqvtgitetafg 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 641 sayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 721 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 769
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-733 |
1.39e-166 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 525.03 E-value: 1.39e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVT---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 254 -----GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIP------------ 316
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 317 ------------IPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL--- 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 382 CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 542 PKATDKTFVEKLVQEQGTHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 622 -VDRIVGLdqvtgitetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14888 550 yLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|...
gi 2024363113 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
7.66e-166 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 522.43 E-value: 7.66e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 337 GFSHDEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR-DYVQKAQTKE 415
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDkaD 574
Cdd:cd14873 394 EQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--N 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVtgitetafGSAYKTKKgmfRTVG 654
Cdd:cd14873 468 FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTL--------KCGSKHRR---PTVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14873 537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRN 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 2024363113 735 AIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14873 617 LALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-771 |
9.75e-165 |
|
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: 518.75 E-value: 9.75e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVAsshkgrKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLAGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD--KDNFQETM 330
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNSgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 331 EAMHIMGFSHDEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA-LTSHSVVTRg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 484 QQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEKLvqEQGTHSK 562
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 563 FQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdvdrivgldqvtgitetafgsa 642
Cdd:cd01379 463 YYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 643 yktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd01379 517 ---------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFA 587
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2024363113 723 EFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 588 DFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
2.91e-160 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 506.54 E-value: 2.91e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASShkgrkdhnIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD-------KDNFQETM 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 331 EAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 487 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 567 rqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdvdrivgldqvtgitetafgsayktk 646
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 647 kgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14897 522 --------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2024363113 727 RYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
4.29e-159 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 504.29 E-value: 4.29e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 172 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 327 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 403 VGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFELNSFE 472
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KATDKTFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 552 KLVQEQ-GTHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkdvdrivgldq 630
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 631 vtgitetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 710
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 711 CRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 771
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-731 |
7.38e-147 |
|
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: 469.40 E-value: 7.38e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHV------ASSHKGRKDHNIPGelerQLLQANPILESFGNAKTVKND 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 238 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEhlksdlllegfnnyrflsngyipi 317
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 318 pGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLGMNVM 390
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 391 EFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEIF 466
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 467 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATD 546
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 547 KTFVEKLVQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSSdkfvaelwkdVDriv 626
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD--- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 627 gldqvtgitetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 706
Cdd:cd14900 509 ----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660
....*....|....*....|....*
gi 2024363113 707 GIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
8.37e-146 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 467.85 E-value: 8.37e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-----KDNFQET 329
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRevqywKKKYDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 330 MEAMHIMGFSHDEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd14889 227 CNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT-LTCTVTFTRg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 484 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF 563
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 564 QKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELW----KDVDRIVGLDQVTGITETAF 639
Cdd:cd14889 461 GKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrSRTGTLMPRAKLPQAGSDNF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 640 GSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 719
Cdd:cd14889 539 NSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRP 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 720 VFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 613 SFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
1.52e-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: 461.81 E-value: 1.52e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE-----------LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 239 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLE----GFNNYRFLSNG 313
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 314 YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 391
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 392 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 464
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 465 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 543 KATDKTFVEKLVQEQGTHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdv 622
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 623 drivglDQVTGITETAFGSAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 702
Cdd:cd14907 554 ------SGEDGSQQQNQSKQKKSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 2024363113 703 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
1.11e-142 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 458.74 E-value: 1.11e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 172 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKDHNI--------PGELERQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 242 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 319
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 320 QQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 394
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 395 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 472
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 552
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 553 LVQEQGTHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHqSSDKFvaelwkdvdrivgLDQV 631
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 632 TGITEtafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 711
Cdd:cd14891 535 QELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 712 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
3.61e-139 |
|
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: 449.01 E-value: 3.61e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 336 MGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 496 QEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGTHSKFQKPRQlkDK 572
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgldqvtGITETAFGSAYKTKKGMfRT 652
Cdd:cd14904 466 TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14904 536 LGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2024363113 733 PNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 616 PPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
6.73e-139 |
|
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: 448.07 E-value: 6.73e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL-----RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-GRDYVQKAQTK 414
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 494 LEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQlkDKA 573
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgldqvtgitetafgSAYKTKKGMfRTV 653
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAE-----------------PQYGLGQGK-PTL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTp 733
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG- 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 2024363113 734 NAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 607 SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-771 |
3.28e-135 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 438.96 E-value: 3.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE---LERQLLQANPILESFGNAKTVKNDNSSRFGKF 245
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 246 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGE--------HLKSDLLLEGFNNYRFLSNGYIPI 317
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 318 PGQ-QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLGMNVMEFT 393
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 394 RAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIFELNSF 471
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 472 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFV 550
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 551 EKLV--------QEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqssdkfvaelwkd 621
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 622 vdrivgldqvtgitetafgsayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 701
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMIRALELDPNL---- 760
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNIpedt 671
|
730
....*....|.
gi 2024363113 761 YRIGQSKIFFR 771
Cdd:cd14908 672 MQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-733 |
2.28e-134 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 438.17 E-value: 2.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 169 REDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLsNGYIP----IPGQQDK 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 324 DN--FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAILT 398
Cdd:cd14902 240 YAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 399 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEIFELNS 470
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 471 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFV 550
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 551 EKLVQEQGTHSKfqkprqlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkDVDRIVGLDQ 630
Cdd:cd14902 477 TKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 631 VTGITETAFGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 708
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616
|
650 660
....*....|....*....|....*
gi 2024363113 709 RICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14902 617 RIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-732 |
1.81e-133 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 435.15 E-value: 1.81e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGElerQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 242 FGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--NYRFLSNG- 313
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 314 -YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD---------------QASMPENTV 377
Cdd:cd14895 232 cYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 378 AQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK------ 448
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 449 ----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 524
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 525 pANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDN 602
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 603 VATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKGmfrtVGQLYKESLTKLMATLRNTNPNFVRCIIPN 682
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2024363113 683 HEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-824 |
8.63e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 437.15 E-value: 8.63e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 336 MGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLK 570
Cdd:PTZ00014 500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDS 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 571 DKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitetafgsayKTKKGMF 650
Cdd:PTZ00014 577 NK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 651 rtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:PTZ00014 640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 731 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFA 807
Cdd:PTZ00014 718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
|
730
....*....|....*..
gi 2024363113 808 KKqqqlsaLKILQRNCA 824
Cdd:PTZ00014 798 KN------IKSLVRIQA 808
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
7.32e-128 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 417.08 E-value: 7.32e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 338 FSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 412
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 413 TKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFqKPRQLKD 571
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKVDS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 572 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgldqvtgITETAfgsayKTKKGMFr 651
Cdd:cd14876 468 NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV-----------VVEKG-----KIAKGSL- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 652 tVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14876 531 -IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 2024363113 732 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 769
Cdd:cd14876 610 DLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
2.42e-126 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 414.40 E-value: 2.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQA-NPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV--------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 336 MGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI------------LTPRIKV 403
Cdd:cd01386 233 LGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 404 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN------SFEQLCIN 477
Cdd:cd01386 313 SPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrgaTFEDLCHN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALLDEECWFPKAT 545
Cdd:cd01386 392 YAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEALYPGSS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 546 DKTFVEKLVQEQG--THSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQSSDKFVAelw 619
Cdd:cd01386 472 DDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKETAA--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 620 kdvdrivgldqvtgitetafgsayKTKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRCIIPNH--EKRAGK-------- 689
Cdd:cd01386 549 ------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERStsspaagd 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 690 --LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACERMIRALELDPNLYR 762
Cdd:cd01386 601 elLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYR 680
|
....*....
gi 2024363113 763 IGQSKIFFR 771
Cdd:cd01386 681 IGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-733 |
1.73e-120 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 396.53 E-value: 1.73e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKDNFQETMEAMH 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 335 IMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRIKVGRDYV--Q 409
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 490 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQL 569
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGitetafgsaykTKKGM 649
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG-----------QSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
....
gi 2024363113 730 ILTP 733
Cdd:cd14880 623 LLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
2.94e-118 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 392.42 E-value: 2.94e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 177 TGESGAGKTENTKKVIQYLAHVASS--HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 255 YIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLAGAGehlKSDLLLEGFNN----YRFL--------------SNGY 314
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissfksqsSNKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 315 IPIPGQQDKD-NFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVM 390
Cdd:cd14906 238 SNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 391 EFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQGASFIGIL 458
Cdd:cd14906 318 VFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 459 DIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEE 538
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 539 CWFPKATDKTFVEKLVQE-QGTHSKFQkpRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAE 617
Cdd:cd14906 475 CIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 618 LWKdvdrivglDQVTGITETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 697
Cdd:cd14906 552 LFQ--------QQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLS 617
|
650 660 670
....*....|....*....|....*....|....*..
gi 2024363113 698 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14906 618 QLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
4.70e-114 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 378.08 E-value: 4.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 173 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETME 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 332 AMHIMgFSHDEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILTPRIKVGRDYV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 409 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINYANERLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVeklvqeQGTHSKFQK 565
Cdd:cd14886 388 YFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFT------SSCKSKIKN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 566 PRQLKDKA---DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLdqvtgitetafgsa 642
Cdd:cd14886 459 NSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 643 yktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd14886 525 ---MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 723 EFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 600 EFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
1.39e-113 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 376.84 E-value: 1.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 176 CTGESGAGKTENTKKVIQYLAHVASSHKGR-KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD-VT 253
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 254 GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPGQ--QDKDNF 326
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 327 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILtprIKVGRD 406
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 407 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK-FQ 564
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPyFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 565 KPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdvdrivgldqvtgitetafgsaYK 644
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL------------------------LS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 645 TKKGMFR---TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14875 529 TEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 722 QEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 771
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
6.46e-106 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 356.71 E-value: 6.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 168 DREDQSILCTGESGAGKTENTKKVIQYLA-------HVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 239 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-----AGEHLKSDLLLEGFNNYRFLSN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 313 GYIPI--PGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ--------- 379
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 380 -KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT----------- 447
Cdd:cd14899 321 tKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 448 ---KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIER 524
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 525 paNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 601
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 602 NVATLLHQSSDKFVAEL-----WKDVDRIVGLDQVTGITETAFGSAYKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFV 676
Cdd:cd14899 558 SAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAV-----SVGTQFKIQLNELLSTVRATTPRYV 632
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 677 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 633 RCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
1.32e-98 |
|
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: 335.46 E-value: 1.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 251 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFlsngyipipgqqDKDNFQETM 330
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------DLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 331 EAMHIMGFSHDEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL-------GMNVMEFTRA 395
Cdd:cd14887 225 KTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclssGLKVTEASRK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 396 ILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR------ 449
Cdd:cd14887 302 HLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesds 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 450 -------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQP 517
Cdd:cd14887 382 dedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 518 CIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGTHSKFQK--PRQ 568
Cdd:cd14887 462 ASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPAL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 569 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDKFVaelwkdvdRIVGLDQVTGItetafgSAYKTKKg 648
Cdd:cd14887 542 SRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV------RAISSRR- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 649 mfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14887 606 --STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRY 683
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2024363113 729 EILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 684 ETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
1.68e-98 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 332.59 E-value: 1.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 245 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGY--IPIPGQ 320
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 321 QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMNVMEFtRAIL 397
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 398 TPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIF---ELN 469
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 470 SFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALLDEEC-WFPK 543
Cdd:cd14879 386 SLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDDQTrRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 544 ATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSSDkFVAelwk 620
Cdd:cd14879 458 KTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN---- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 621 dvdrivgldqvtgitetafgsayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14879 523 ----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIR 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSKIFF 770
Cdd:cd14879 574 SLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
2.54e-97 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 326.85 E-value: 2.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQETMEAMHIMGFS 339
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 340 HdeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 419
Cdd:cd14898 220 N--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 420 AVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 499
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 500 QREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgthSKFQKPRqLKDKADFCII- 578
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-INTKARDKIKv 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 579 -HYAGKVDYKADEWLMKNMDplndnvatllhqssdkfvaelwkdvdrivgldqvtGITETAFGSAYKTKKGMFRTVGQLY 657
Cdd:cd14898 440 sHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDEGSKEDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 658 KESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
1.98e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 318.30 E-value: 1.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQQDKDNFQETM 330
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 331 EAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 488 NHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATDKTFVEKL--- 553
Cdd:cd14878 393 NEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLqsl 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 554 VQEQGTHSKFQKPRQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdvdriv 626
Cdd:cd14878 460 LESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 627 gldqvtgitetafgsaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 706
Cdd:cd14878 532 ----------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 707 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKIFFR 771
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
2.87e-92 |
|
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: 314.26 E-value: 2.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAhvasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 339 sHDEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 494 LEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKa 573
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITetafgsaYKtkkgmfrtv 653
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLIT-------FK--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 654 gqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 2024363113 734 NAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
1.19e-81 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 284.88 E-value: 1.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT---ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 251 D---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-AGEHLKSDLLLEGFNNYRFL---------- 310
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 311 ----------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKkerntdqasmpentvaqK 380
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------A 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 381 LCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 453 ---SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpanpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 530 gVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGTHSK-FQKPR--------QLKDKADFCIIHYAGKVDYKADE 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 591 WLMKNMDPLNDNVATLLHQSSDKFVAElwkdvdrivgldqvtgitetafgSAYKTKKGMFRTVGQLYKESLTKLMATLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 671 TNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-758 |
9.78e-79 |
|
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: 274.68 E-value: 9.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 173 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhnipGELE----RQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG-----------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 249 NFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 326
Cdd:cd14881 139 QV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 327 QETMEAMHIMGFshdEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiLTPRIK- 402
Cdd:cd14881 218 QAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-LTTRTHn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 403 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFELNSFEQL 474
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 475 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKTFVEKL 553
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 554 VQEQGTHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdkfvaelwkdvdrivgldqvtg 633
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 634 iteTAFGsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 713
Cdd:cd14881 499 ---CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAG 566
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2024363113 714 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 758
Cdd:cd14881 567 GYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-736 |
3.96e-73 |
|
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: 257.88 E-value: 3.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgelerqllQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSS----------AIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIE-TYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 337 GFSHDEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKVGrdyvqKAQT 413
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSEDG-----TTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 494 LEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQlKDK 572
Cdd:cd14874 373 DQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KER 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdvdrivgldqvtgitetaFGSAYKTKKGMFRT 652
Cdd:cd14874 450 LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESYSSNTSDMIVS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 2024363113 733 PNAI 736
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-771 |
1.60e-70 |
|
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: 251.55 E-value: 1.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnipgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY---------ILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 337 GFSHDEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAqtkeq 416
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 417 adfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14905 304 -----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 497 EEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF-QKPRQlkdkad 574
Cdd:cd14905 377 REYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKF-------------VAELWKDVD----------RIVGL--- 628
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakksplSIVKVlls 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 629 ------DQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14905 524 cgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14905 604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-770 |
2.53e-68 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 246.81 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 172 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgEH---LKSDLLL-EGFNNYRFLSNGyIPIPGQ--Q 321
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPLATNfaL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 322 DKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------LGMNVME 391
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilLAAKLLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 392 FTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG----ASF 454
Cdd:cd14893 322 VEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 455 IGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIDLIERP 525
Cdd:cd14893 402 VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEDK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 526 anPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD------------FCIIHYAGKVDYKADEWLM 593
Cdd:cd14893 482 --PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 594 KNMDPLNDNVATLLHQSSDKfvaelwkdVDRIVGLDQVT--------------GITETAFG----SAYKTKKGMFRTVGQ 655
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAaassekaakqteerGSTSSKFRksasSARESKNITDSAATD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 656 LYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYeiltpna 735
Cdd:cd14893 632 VYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------- 703
|
730 740 750
....*....|....*....|....*....|....*....
gi 2024363113 736 ipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 770
Cdd:cd14893 704 --KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-731 |
2.18e-64 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 232.71 E-value: 2.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 180 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERqllqANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLAG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG----------QQDKDN 325
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyrrddpEGNVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 326 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14882 229 YKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNSFEQLCINYTN 480
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 481 EKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDKTFVEKLVQEQ 557
Cdd:cd14882 384 EQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 558 gtHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivglDQVTGItet 637
Cdd:cd14882 456 --HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 638 afgsayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 714
Cdd:cd14882 521 ------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKG 588
|
650
....*....|....*..
gi 2024363113 715 FPNRIVFQEFRQRYEIL 731
Cdd:cd14882 589 FSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-769 |
4.55e-59 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 218.55 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 179 ESGAGKTENTKKVIQYLAHVA----------SSHKGRKDHNIP-----GELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrrlptnlNDQEEDNIHNEEntdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 244 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 324 DNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 378 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 455 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 535 LDEECWFPKATDKTFVEKL-VQEQGTHSKF-QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 612
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSiIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 613 KFVAELWKDVDrivgLDQVTGITET----AFGSAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHE 684
Cdd:cd14938 558 EYMRQFCMFYN----YDNSGNIVEEkrrySIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNES 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 685 KRA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRI 763
Cdd:cd14938 634 KRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 2024363113 764 GQSKIF 769
Cdd:cd14938 706 GNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
1.01e-58 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 200.26 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 200 SSHKGRKDHN-------IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01363 81 FNGINKGETEgwvylteITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1016-1861 |
4.82e-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: 146.74 E-value: 4.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1016 AEEEEKAKNL-AKLKNKQ-EMMITDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEELQ 1093
Cdd:TIGR02168 209 AEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1094 AALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKRE 1173
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1174 QEVAELKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQAKRFKANLEKNKQGLESDNkelacevkvlqqvkaeSEHK 1253
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI----------------EELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1254 RKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEetrqKLN 1333
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1334 LSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVdddlgtiegLEENKKKLLKDMESLSQRLEEKAM 1413
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV---------VVENLNAAKKAIAFLKQNELGRVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1414 AYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAeekNISARYAEERDRAEAEAREKETKAL------- 1486
Cdd:TIGR02168 575 FLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNALELAKKLRPGyrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1487 --------SLARALEEALEAKEEFERQNKQLRADMEdlmsskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQAT 1558
Cdd:TIGR02168 652 gdlvrpggVITGGSAKTNSSILERRREIEELEEKIE--------------ELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1559 EDAKLRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANK 1638
Cdd:TIGR02168 718 RKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1639 ARDEAIKQLRKLQAQ--------------MKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARR 1704
Cdd:TIGR02168 797 ELKALREALDELRAEltllneeaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1705 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSA----- 1779
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleea 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1780 ---AQKSENARQQLERQNKELKAKLQELeGSVK----SKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLK 1852
Cdd:TIGR02168 957 ealENKIEDDEEEARRRLKRLENKIKEL-GPVNlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
....*....
gi 2024363113 1853 EVFMQVEDE 1861
Cdd:TIGR02168 1036 DTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1120-1835 |
6.78e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 143.27 E-value: 6.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1120 IAELQEDLESEKASRNKAEKQKrDLSEELEALKTELEdTLDTTAAQQELRTKREQEvaelkkaieeetknheAQIQEIRQ 1199
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1200 RHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELA 1279
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1280 EKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR 1359
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1360 KNLEKQMLALQAQLAEAKKK-VDDDLGTIEGLEENKKKLLKDM----ESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMV 1434
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLeealEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1435 DLDHQRQI---VSNLEKKQKKF--------DQMLAEEKNISARYAEERDRAEAEAREKETKAL----SLARALEEALEAK 1499
Cdd:TIGR02168 497 LQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaiaFLKQNELGRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1500 EEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKL---------------- 1563
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgdlvr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1564 --------RLEVNMQAMKAQFE-RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE 1634
Cdd:TIGR02168 657 pggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1635 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1714
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1715 DEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGE--------------RSAA 1780
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerasleealallRSEL 896
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1781 QKSENARQQLERQNKELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAK 1835
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
977-1858 |
1.70e-32 |
|
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: 138.66 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 977 EAKIKKMEEEIllleDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEmmitDLEERLKKEEKtrQELEKA 1056
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1057 KRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV-IRELQAQIAELQEDLESEKASRN 1135
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1136 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEEtknhEAQIQEIRQRHATALEELS---EQL 1212
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1213 EQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNV 1292
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1293 SSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLQEQQEEEEEARKN---L 1362
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNRLNnvvV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1363 EKQMLALQA-QLAEAKKkvdddLGTIEGLEENKkklLKDMESLSQRLEEKA---MAYDKLE---KTKNRLQQELDDLMV- 1434
Cdd:TIGR02169 555 EDDAVAKEAiELLKRRK-----AGRATFLPLNK---MRDERRDLSILSEDGvigFAVDLVEfdpKYEPAFKYVFGDTLVv 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1435 -DLDHQRQIVSN----------LEKKQKKFDQMLAEEKNISaRYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFE 1503
Cdd:TIGR02169 627 eDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSELRRIE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1504 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQAR 1583
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1584 DEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEE 1663
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1664 ARASRDEIFAQSKESEKKLKGLEAEILQLQEEfaaserarrhaeqeRDELADEIansasgkSALLDEKRRLEARIAQLEE 1743
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKE--------------RDELEAQL-------RELERKIEELEAQIEKKRK 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1744 ELEEEQSNMELLNERfrkttlqvdtlNSELAGERSAAQKSENARQQLERQNKELKAKLQELE--GSVKSKFKATISTLEA 1821
Cdd:TIGR02169 918 RLSELKAKLEALEEE-----------LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLK 986
|
890 900 910
....*....|....*....|....*....|....*..
gi 2024363113 1822 KIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQV 1858
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1185-1934 |
2.02e-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: 131.72 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1185 EETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA--NLEKNKQG--LESDNKELACEVKVLQQVKAESEHKRKKLDAQ 1260
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1261 VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1340
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1341 LEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEkamaydkLEK 1420
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-------LED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1421 TKNRLQQElddlmvdldhQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKE 1500
Cdd:TIGR02168 415 RRERLQQE----------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1501 EFERQNKqlrADMEDLMSSKDDVGKNVHELEKSKRTLEQQV----------EEMRTQLEE-LEDELQA-----TEDAKLR 1564
Cdd:TIGR02168 485 AQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEAaLGGRLQAvvvenLNAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1565 LE---------VNMQAMKAQFERDLQARDEQNEEKKRM-------LVKQVRELEAELED--------ERKQRALAVAAKK 1620
Cdd:TIGR02168 562 IAflkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGflgvakdLVKFDPKLRKALSYllggvlvvDDLDNALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1621 KMEMDLKDLEGQ-------------------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1675
Cdd:TIGR02168 642 RPGYRIVTLDGDlvrpggvitggsaktnssilerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1676 KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1755
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1756 NERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkFKATISTLEAKIAQLEEQLEQEAK 1835
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1836 ERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA---- 1910
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAeale 960
|
810 820
....*....|....*....|....*..
gi 2024363113 1911 ---TEANEGLSREVSTLKNRLRRGGPI 1934
Cdd:TIGR02168 961 nkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1054-1740 |
1.17e-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: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1054 EKAKRKLDGETTDL---QDQIAELQAQIEELKIQ--LAKKEEELQAALARGDEEAvqknnALKVIRELQAQIAELQEDLE 1128
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPLERQaeKAERYRELKEELKELEAEL-----LLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1129 SEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEvAELKKAIEEETKNHEAQIQEIRQRhATALEEL 1208
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELE------ELELELEEAQAEE-YELLAELARLEQDIARLEERRREL-EERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1209 SEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1288
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1289 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlqeqqeeeeearKNLEKQMLA 1368
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--------------EALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1369 LQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAydKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEk 1448
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA--LLLAGLRGLAGAVAVLIGVEAAYEAALEAAL- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1449 kqkkfdqMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRA-DMEDLMSSKDDVGKNV 1527
Cdd:COG1196 545 -------AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvDLVASDLREADARYYV 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1528 HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELED 1607
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1608 ERKQRALAVAAKKkmEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSkESEKKLKGLEA 1687
Cdd:COG1196 698 ALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE-ELERELERLER 774
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1688 EILQLQ-------EEFAAserarrhAEQERDELADEIANsasgksaLLDEKRRLEARIAQ 1740
Cdd:COG1196 775 EIEALGpvnllaiEEYEE-------LEERYDFLSEQRED-------LEEARETLEEAIEE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1623 |
3.52e-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: 127.87 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 849 RQEEELQakdeeLMKVKEKQTKVEAELEEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKK-QELEEILHDL 927
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALLVLRlEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 928 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDR 1007
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1008 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAK 1087
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1088 KEEELQAALARGDE-----EAVQKNNALKVIRELQAQIAELQ---EDLESEKASRNKAEKQKRDLSEELEALKTELEDTL 1159
Cdd:TIGR02168 405 LEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEELEeelEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1160 DTTAAQQELRTKREQEVAELKKAIEEETKNHE---------AQIQEIRQRHATALEE---------LSEQLEQAKRFKAN 1221
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAF 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1222 LEKNKQG--------------LESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKV------TEGERLRVELAE- 1280
Cdd:TIGR02168 565 LKQNELGrvtflpldsikgteIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddlDNALELAKKLRPg 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1281 -------------------KANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1341
Cdd:TIGR02168 645 yrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1342 EEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKT 1421
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1422 KNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEE 1501
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1502 FERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVNMQAMKAQF 1576
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEEAEALENKIE 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1577 ERDLQARDEQNEEKKR---------MLVKQVRELEAELEDERKQRALAVAAKKKME 1623
Cdd:TIGR02168 965 DDEEEARRRLKRLENKikelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1719 |
5.23e-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: 124.01 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 844 LLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFaeaeemrarlaakkQELEEI 923
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL--------------YALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 924 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQldeeegaRQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKL 1003
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESK-------LDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1004 MEDRIAECtsqlaeeeekaknlaklknkqemmitdleerlkkeektRQELEKAKRKLDgettDLQDQIAELQAQIEELKI 1083
Cdd:TIGR02168 370 LESRLEEL--------------------------------------EEQLETLRSKVA----QLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1084 QLakkeEELQAALARGDEEAVQKNNALKvirelQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttA 1163
Cdd:TIGR02168 408 RL----ERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEELREELE------E 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1164 AQQELRTKREQevaelkkaiEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNK-ELACE--- 1239
Cdd:TIGR02168 473 AEQALDAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaal 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1240 --------VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK--KGIKFAKD 1309
Cdd:TIGR02168 544 ggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1310 AASLESQLQDTQELlqeetRQKLNLSSRIRQLEEEK-----------NNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1378
Cdd:TIGR02168 624 GVLVVDDLDNALEL-----AKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1379 KVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQML 1457
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1458 AEEKNIsaryaeERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadMEDLMSSKDDVGKNVHELEKSKRTL 1537
Cdd:TIGR02168 779 EAEAEI------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--LESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1538 EQQVEEMRTQLEELEDELQATEDAklrLEVNMQAMKAQFERDLQARDEQNEekkrmLVKQVRELEAELEDERKQRALAVA 1617
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESE---LEALLNERASLEEALALLRSELEE-----LSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1618 AKKKMEMDLKDLEGQIEaankardeaikqlRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQL----- 1692
Cdd:TIGR02168 923 KLAQLELRLEGLEVRID-------------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnl 989
|
890 900
....*....|....*....|....*....
gi 2024363113 1693 --QEEFAASERARRHAEQERDELADEIAN 1719
Cdd:TIGR02168 990 aaIEEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
807-1449 |
4.13e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 120.81 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 807 AKKQQQLSA-LKILQrncaAYLKLRHWQWWRvftkvkplLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQL 885
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELE--------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 886 LEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdlesrveeeeeRNQILQNEKKKMQGHIQDLEEQLDEEEGA 965
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------------RLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 966 RQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKK 1045
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1046 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE 1125
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1126 DLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATAL 1205
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1206 EELSEQLEQAKRFKANLeknkqGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKL 1285
Cdd:COG1196 586 AALAAALARGAIGAAVD-----LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1286 QNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQ 1365
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1366 MLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLS---QR-LEEkamaYDKLEKTKNRLQQELDDLMVDLDHQRQ 1441
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaIEE----YEELEERYDFLSEQREDLEEARETLEE 816
|
....*...
gi 2024363113 1442 IVSNLEKK 1449
Cdd:COG1196 817 AIEEIDRE 824
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1544 |
4.17e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.93 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 846 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 925
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 926 DLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKK------------MEEEILLLEDQ 993
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 994 NSKFLKEKKLMEDRIAECTSQLAEEEEKaknLAKLKNKQEMMiTDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI-- 1071
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERE---LAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsv 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1072 -AELQAQIEelkiqlAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE----DLESEKASRNKAEKQKRDLSE 1146
Cdd:TIGR02168 532 dEGYEAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAK 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1147 ELEALKTELEDTLD------------TTAAQQELRTKREQEVAELKK-------AIEEETKNHEAQIQEIRQRhataLEE 1207
Cdd:TIGR02168 606 DLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGdlvrpggVITGGSAKTNSSILERRRE----IEE 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1208 LSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQN 1287
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1288 ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQML 1367
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1368 ALQAQLAEAKKKVDDDLGTIEGLEENK-------KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQR 1440
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIeeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1441 QIVSNLEKKQKKFDQMLAE-EKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1519
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
730 740
....*....|....*....|....*
gi 2024363113 1520 KDDVGKNVHELEKSKRTLEQQVEEM 1544
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1740 |
1.25e-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: 119.40 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 859 EELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlAAKKQELEEILHDLEsrVEEEEERN 938
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 939 QILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEIllledqnskflkeKKLMEDRIAECTSQLAEE 1018
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI-------------KDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1019 EEKAKNLaklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALAR 1098
Cdd:TIGR02169 300 EAEIASL-------ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1099 GDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1178
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1179 LKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLqqvkaesEHKRKKLD 1258
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEE-YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1259 AQVQELtAKVTEGERLRVELAekankLQNELDNVSSLLEEAEKKGIKFAKdaaslESQLQDTQELLQEETRQKLNLSSRI 1338
Cdd:TIGR02169 525 GTVAQL-GSVGERYATAIEVA-----AGNRLNNVVVEDDAVAKEAIELLK-----RRKAGRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1339 R------------QLEEEKNNLQEQQEEEEEARKNLEK--------QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLL 1398
Cdd:TIGR02169 594 SedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAarrlmgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1399 KDMESLSQRLEEkamaydkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNISARYAEERDRA 1474
Cdd:TIGR02169 674 AELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1475 EAEAREKETKALSLARaleeALEAKEEFERQNKQLRADMEDLMSSKDDVGknVHELEKSKRTLEQQVEEMRTQLEELEDE 1554
Cdd:TIGR02169 747 SSLEQEIENVKSELKE----LEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQK 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1555 LQATEDAKLRLEVNMQAMKAQfERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE 1634
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1635 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE------SEKKLKGLEAEILQLQEEFAASERARRHAEQ 1708
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
890 900 910
....*....|....*....|....*....|..
gi 2024363113 1709 ERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-712 |
2.37e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 117.92 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 218 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHIFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 287 LLAGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHDEILSMLKVVS 351
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 352 SVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVEALA 425
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 426 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQlfnh 489
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 490 tmfileqEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVEKLVQEQGt 559
Cdd:cd14894 565 -------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDRNS- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 560 hSKFQKPRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgL 628
Cdd:cd14894 637 -SRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ---L 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 629 DQVTGITETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 708
Cdd:cd14894 713 GWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQM 791
|
....
gi 2024363113 709 RICR 712
Cdd:cd14894 792 EICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1097-1917 |
9.11e-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: 116.71 E-value: 9.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1097 ARGDEEAVQKNnalkvIRELQAQIAELQEDLESEKASRNKAEKQKrDLSEELEalktELEDTLdTTAAQQELRTKREQEV 1176
Cdd:TIGR02169 175 ALEELEEVEEN-----IERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKR----EYEGYE-LLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1177 AELKkAIEEETKNHEAQIQEIRQRHATALEELSEQleqAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKK 1256
Cdd:TIGR02169 244 RQLA-SLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1257 LDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSS 1336
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1337 RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYD 1416
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1417 KLEKTKNRLQQELDdlmvDLDHQRQIVSNLEKKQKKFDQMLaeEKNISARYAEERDRAEAEarEKETKALSLAraleeal 1496
Cdd:TIGR02169 480 RVEKELSKLQRELA----EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA------- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1497 eakeeferqnkqLRADMEDLMSSKDDVGKNVHELEKSK---RTLEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMK 1573
Cdd:TIGR02169 545 ------------AGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1574 AQFERDLQ--ARDE---QNEEKKRMLVKQVR--ELEAELEDE--------RKQRALAVAAKKKMEmDLKDLEGQIEAANK 1638
Cdd:TIGR02169 610 PKYEPAFKyvFGDTlvvEDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1639 ARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIA 1718
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1719 NSASGKSALLDEKRRLEARIAQLEEELEEEQsnMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELK 1798
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1799 AKLQELEGSV------KSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQM 1872
Cdd:TIGR02169 847 EQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 2024363113 1873 EKANARMKQLKRqLEEAEEEATRANASRRKLQRELDDATEANEGL 1917
Cdd:TIGR02169 927 EALEEELSEIED-PKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1706 |
2.02e-25 |
|
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: 115.55 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 844 LLQVTRQEEELQAKDEElmkVKEKQTKVEAELEEMERkHQQLLEEKNILA--EQLQAETELFAEAEEMRARLAAKKQELE 921
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 922 EILHDLESRVEEEEERNQILQNEKKKMqghiqdleEQLDEEEGARQKLQLEKVTAEakIKKMEEEILLLEDQNSKFLKEK 1001
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI--------KDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1002 KLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEEL 1081
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1082 KIQLAKKEEELQaalaRGDEEAVQKNNALKVIRE-----------LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1150
Cdd:TIGR02169 405 KRELDRLQEELQ----RLSEELADLNAAIAGIEAkineleeekedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1151 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE------AQIQEIRQRHATALEELS--------------- 1209
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvAQLGSVGERYATAIEVAAgnrlnnvvveddava 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1210 -EQLEQAKRFKAN----LEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELtakvteGERLRVELAEKANK 1284
Cdd:TIGR02169 561 kEAIELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF------GDTLVVEDIEAARR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1285 LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqklNLSSRIRQLEEEKNNLQEQqeeeeeaRKNLEK 1364
Cdd:TIGR02169 635 LMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQSE-------LRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1365 QMLALQAQLAEAKKKvdddlgtIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1444
Cdd:TIGR02169 703 RLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1445 NLEKKQKKFDQMLAEEKNISARyaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG 1524
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1525 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqferDLQARDEQNEEKKRMLVKQVRELEAE 1604
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQ 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1605 LEDERKQRALAVAAKKKMEMDLKDLEGQIeAANKARDEAIKQLRKLQAQMKDYQRELEE-------ARASRDEIFAQSKE 1677
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDE 990
|
890 900
....*....|....*....|....*....
gi 2024363113 1678 SEKKLKGLEAEILQLQEEFAASERARRHA 1706
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
911-1612 |
4.10e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 911 ARLAAKKQELEEILHDLESrveeeeernQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLL 990
Cdd:COG1196 209 AEKAERYRELKEELKELEA---------ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 991 EDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRkldgettDLQDQ 1070
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-------EAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1150
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1151 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQrhataLEELSEQLEQAKRFKANLEKNKQGLE 1230
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-----LLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1231 SDNKELacevkvlqqvkaeseHKRKKLDAQVQELTAKVTEGERLRVELAEkanKLQNELDNVSSLLEEAEKKGIKFAKDA 1310
Cdd:COG1196 508 EGVKAA---------------LLLAGLRGLAGAVAVLIGVEAAYEAALEA---ALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1311 ASLEsqlqDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKkkvDDDLGTIEGL 1390
Cdd:COG1196 570 KAGR----ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL---EAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1391 EENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmLAEEKNISARYAEE 1470
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE----------------LELEEALLAEEEEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1471 RDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelEKSKRTLEQQVEEMRTQLEE 1550
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE--------PPDLEELERELERLEREIEA 778
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1551 LEDelqatedaklrleVNMQAMkAQFERdLQARDEQNEEKKRMLVKQVRELE---AELEDERKQR 1612
Cdd:COG1196 779 LGP-------------VNLLAI-EEYEE-LEERYDFLSEQREDLEEARETLEeaiEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1321-1886 |
7.37e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1321 QELLQEETRQKLNLSS-RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLK 1399
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1400 DMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAR 1479
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1480 EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1559
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1560 DAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRAlAVAAKKKMEMDLKDLEGQIEAANKA 1639
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG-VKAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1640 RDEAIKQLRkLQAQMKDYQRELEEARasrdeifAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN 1719
Cdd:COG1196 535 AYEAALEAA-LAAALQNIVVEDDEVA-------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1720 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKA 1799
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1800 KLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQM---EKAN 1876
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdlEELE 766
|
570
....*....|
gi 2024363113 1877 ARMKQLKRQL 1886
Cdd:COG1196 767 RELERLEREI 776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1106-1939 |
2.05e-24 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 112.13 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1106 KNNALKVIRELQAQIAELQEDLESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEE 1185
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1186 ETKNHEAQiqeiRQRHATALEELSEQLEQAKRFKANLEKNKQGLESD--NKELACEVKVLQQVKAESEHKR--------- 1254
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvDFEEASGKKIYEHDSMSTMHFRslgsaiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1255 -KKLDAQVQELTAKVTEGE-RLRVELAEKANK----LQNELDNVSSLLEEAEKKGIKFAKDAASLESQ---LQDTQELLQ 1325
Cdd:pfam15921 226 lRELDTEISYLKGRIFPVEdQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1326 EETRQKLnlSSRIRQLEEeknnlqeqqeeeeearknLEKQMLALQAQLAEAKKKVDDDLgtieglEENKKKLLKDMESLS 1405
Cdd:pfam15921 306 EQARNQN--SMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI------EELEKQLVLANSELT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1406 QRLEEKamayDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKNISARYAEERDR-AEAEAREKE 1482
Cdd:pfam15921 360 EARTER----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1483 TKALSlARALEEALEAKEEFERQNKQLR---ADMEDLMSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQ 1556
Cdd:pfam15921 435 LKAMK-SECQGQMERQMAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1557 AT--EDAKLRLEVNMQAMKAQFERdlqardeqNEEKkrmlvkQVRELEAELEDERKQRAlavAAKKKMEMDLKDLEGQIE 1634
Cdd:pfam15921 514 ATnaEITKLRSRVDLKLQELQHLK--------NEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQ 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1635 -AANKARDEAIKQLRK--LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERD 1711
Cdd:pfam15921 577 lVGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1712 ELADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELLNERFRKTTLQVDTLNSELAGERSAAQ----KSENAR 1787
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETTTNKLKMQLKSAQseleQTRNTL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1788 QQLERQNKELKAKLQELEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERaaanKLVRRTEKKLKEVFMQVEDERrhaDQ 1867
Cdd:pfam15921 716 KSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEK---NK 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1868 YKEQMEKANARMKQLKRQLEEAEEEATRAN----------------ASRRKLQRELDDATEANEGLSREvSTLKNRLRRG 1931
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASlqfaecqdiiqrqeqeSVRLKLQHTLDVKELQGPGYTSN-SSMKPRLLQP 866
|
....*...
gi 2024363113 1932 GPITFSSS 1939
Cdd:pfam15921 867 ASFTRTHS 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
966-1555 |
1.01e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 106.30 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 966 RQKLQLEKV-TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLK 1044
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1045 KEEKTRQELEKAKR---KLDGETTDLQDQIAELQAQIEELKiqlaKKEEELQAALARgdeeavqknnaLKVIRELQAQIA 1121
Cdd:PRK03918 232 ELEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1122 ELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ---EVAELKKAIE--EETKNHEAQIQE 1196
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1197 IRQRHA-TALEELSEQLEQAKRFKANLEKN-------KQGLESDNKELACEVKVLQQVKAE--------SEHKRKKLdaq 1260
Cdd:PRK03918 377 LKKRLTgLTPEKLEKELEELEKAKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKEL--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1261 VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK--KGIKFAKDAASLESQLQD-TQELLQEETRQKLNLSSR 1337
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1338 IRQLEEEKNNLQEQQEEEeearKNLEKQMLALQAQLAEAKKKVDDDLGTiegLEENKKKLLKDMESLSQRLEEKAMAYDK 1417
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKELEPFYNEYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1418 LEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEErdraeaEAREKETKALSLARALEEALE 1497
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRA 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1498 AKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1555
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1314-1930 |
5.00e-21 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 101.02 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1314 ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEeeeeARKNLEKQMLALQAQLAEAKKKVDDDLGTIE----- 1388
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETELCAEAEEMRARLAARKQELEEILHELEsrlee 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1389 ------GLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEekn 1462
Cdd:pfam01576 87 eeersqQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1463 isaryaeerdrAEAEAREKETKALSLARALEealeakeeferQNKQLRADMEDLMSSKDdvgKNVHELEKSKRTLEQQVE 1542
Cdd:pfam01576 164 -----------FTSNLAEEEEKAKSLSKLKN-----------KHEAMISDLEERLKKEE---KGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1543 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKM 1622
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1623 EMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASER 1701
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1702 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQ 1781
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1782 KSENARQQLERQNKELKAKLQElEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDE 1861
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1862 RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
847-1734 |
1.32e-20 |
|
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: 99.66 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 847 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlAAKKQELEEILHD 926
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 927 LESRVEEEEERNQILQNEKKKMQGHIqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1006
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1007 RIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRkldgettDLQDQIAELQAQIEELKIQLA 1086
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE-------ELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1087 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaqQ 1166
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1167 ELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQV 1246
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1247 KAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQE 1326
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1327 ETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQ 1406
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1407 RLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKnisaryaeerdrAEAEAREKETKAL 1486
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE------------EEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1487 SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE 1566
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1567 VNMQAMKAQFE-RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIK 1645
Cdd:pfam02463 845 EQKLEKLAEEElERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1646 QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERD-----ELADEIANS 1720
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYnkdelEKERLEEEK 1004
|
890
....*....|....
gi 2024363113 1721 ASGKSALLDEKRRL 1734
Cdd:pfam02463 1005 KKLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1720 |
4.05e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 849 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMR----ARLAAKKQELEEIL 924
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKkaeaARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 925 HDLESRVEEEEERnqiLQNEKKkmqghiqdleeqLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM 1004
Cdd:PTZ00121 1195 KAEDARKAEAARK---AEEERK------------AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1005 EDRIAECTSQLAEEEEKAKNLAKLKNKQEmmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELK-- 1082
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEE--KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkk 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1083 IQLAKKEEELQAALARGDEEAVQKNnalkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTT 1162
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAA-------EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1163 AAQQELRTKREqevaELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKelACEVKV 1242
Cdd:PTZ00121 1411 KKAAAAKKKAD----EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKK 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1243 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNEldnvssllEEAEKKGIKFAKDAASLESQLQDTQE 1322
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEAKKAEEKKKADELKKAEE 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1323 LLQEETRQKLNLSSRirqlEEEKNNLQEQQEEEEearKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDME 1402
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKK----AEEDKNMALRKAEEA---KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1403 SLSQRLEEKAMAYDKLEKTKNRLQQElddlmvdlDHQRQIVSNLEKKQKKFDQMLAEEknisARYAEERDRAEAEAREKE 1482
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKA--------EEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKE 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1483 TKAlslARALEEALEAKEEFERQNKQLRADMEDLMSskddvgkNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1562
Cdd:PTZ00121 1698 AEE---AKKAEELKKKEAEEKKKAEELKKAEEENKI-------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1563 LRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmdlkdlegqieaankarDE 1642
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-----------------DS 1830
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1643 AIKQLRKLQAQMKDYQRELEEARASRDEIfaqSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANS 1720
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNE---NGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
850-1426 |
1.06e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 96.29 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 850 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEqLQAETElfaEAEEMRARLAAKKQELEEILHDLES 929
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 930 RVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEILLLEDQNSkflkEKKLMEDRIA 1009
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1010 ECTSQLAEEEEKAKNLAKLKNKQEMM-----------ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQI 1078
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1079 EELKiqLAKKEEELQAALARGDEEAvqknnalKVIRELQAQIAELQEDLEsekasrnKAEKQKRDLSEELEALKTELEdt 1158
Cdd:PRK03918 429 EELK--KAKGKCPVCGRELTEEHRK-------ELLEEYTAELKRIEKELK-------EIEEKERKLRKELRELEKVLK-- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1159 ldttaaqQELRTKREQEVAELKKAIEEETKNHEAQiqeirqrhatALEELSEQLEQAKRFKANLEKNKQGLESD---NKE 1235
Cdd:PRK03918 491 -------KESELIKLKELAEQLKELEEKLKKYNLE----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1236 LACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgikfakdAASLES 1315
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE-------LKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1316 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARknLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKK 1395
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590
....*....|....*....|....*....|.
gi 2024363113 1396 KllkdmeslsqrLEEKAMAYDKLEKTKNRLQ 1426
Cdd:PRK03918 705 E-----------REKAKKELEKLEKALERVE 724
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1020-1401 |
1.23e-19 |
|
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: 96.66 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1020 EKAKNLAKLKNKQEMM---ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1096
Cdd:TIGR02168 674 ERRREIEELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1097 ARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEV 1176
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1177 AELKKAIEEETKNHEaQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKK 1256
Cdd:TIGR02168 834 AATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1257 LDAQVQELTAKV----TEGERLRVELAEKANKLQNEldnVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKL 1332
Cdd:TIGR02168 913 LRRELEELREKLaqleLRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1333 NLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQaqlAEAKKKVDDdlgTIEGLEENKKKLLKDM 1401
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID---REARERFKD---TFDQVNENFQRVFPKL 1052
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
980-1798 |
1.33e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.75 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 980 IKKMEEeiLLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAK-- 1057
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEea 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1058 RKLDGETTDLQDQIAELQAQIEEL-KIQLAKKEEEL-QAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1135
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDArKAEEARKAEDArKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1136 KAEKQKRDlseelEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQA 1215
Cdd:PTZ00121 1184 AEEVRKAE-----ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1216 KRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRvELAEKANKLQNELDNVSSL 1295
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1296 LEEAEKKGIKFAKDAASLESQLQDTQEllqEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAE 1375
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEE---KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1376 AKKKVDDDLgtiegleENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQEldDLMVDLDHQRQIVSNLEKKQKKFDQ 1455
Cdd:PTZ00121 1415 AAKKKADEA-------KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKA 1485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1456 MLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlmSSKDDVGKNVHELEKSKR 1535
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE---KKKADELKKAEELKKAEE 1562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1536 TleQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQ--NEEKKRMLVKQVRELEAELEDERKQRA 1613
Cdd:PTZ00121 1563 K--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1614 LAVAAKKKMEMDLKDlegqiEAANKARDEAIKQlrklqaQMKDYQRELEEARASRDEifaqSKESEKKLKGLEAEILQLQ 1693
Cdd:PTZ00121 1641 KEAEEKKKAEELKKA-----EEENKIKAAEEAK------KAEEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAE 1705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1694 EEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSEL 1773
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
810 820
....*....|....*....|....*
gi 2024363113 1774 agersaAQKSENARQQLERQNKELK 1798
Cdd:PTZ00121 1786 ------DEEDEKRRMEVDKKIKDIF 1804
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
864-1481 |
1.58e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 95.90 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 864 VKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH---DLESRVEEEEERNQI 940
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 941 LQNEKKKMQGHiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEIllledqnskflkekKLMEDRIAECTSQLAEEEE 1020
Cdd:PRK03918 226 LEKEVKELEEL-----------KEEIEELEKELESLEGSKRKLEEKI--------------RELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1021 KAKNLAKLKNKQEMMITdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGD 1100
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1101 EEAvqknNALKVIRELQAQIaelqEDLESEKASRNKaEKQKRDLsEELEALKTELEDTLDTTAAQqelRTKREQEVAELK 1180
Cdd:PRK03918 359 ERH----ELYEEAKAKKEEL----ERLKKRLTGLTP-EKLEKEL-EELEKAKEEIEEEISKITAR---IGELKKEIKELK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1181 KAIEEETKNH-----------EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLE---SDNKELACEVKVLQQV 1246
Cdd:PRK03918 426 KAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESELIKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1247 KaESEHKRKKLDaqVQELTAKVTEGERLRvelaEKANKLQNELDNVSSLLEEAEkkgiKFAKDAASLESQLQDTQELLQE 1326
Cdd:PRK03918 506 K-ELEEKLKKYN--LEELEKKAEEYEKLK----EKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1327 ETRQKLN--------LSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLaLQAQLAEAKKKVDDDLGTIEGLEENKKKLL 1398
Cdd:PRK03918 575 LLKELEElgfesveeLEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELDKAFEELAETEKRLEELRKELEELE 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1399 K-----DMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK---KFDQMLAEEKNISARYAEE 1470
Cdd:PRK03918 654 KkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKeleKLEKALERVEELREKVKKY 733
|
650
....*....|.
gi 2024363113 1471 RDRAEAEAREK 1481
Cdd:PRK03918 734 KALLKERALSK 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1159-1928 |
1.88e-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: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1159 LDTTAAQQELRTKREQEVAELKkAIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKAnLEKNKQGLESdnKELAC 1238
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDEKRQQ----LERLRREREKAERYQA-LLKEKREYEG--YELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1239 EVKVLqqvkaesEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEE-AEKKGIKFAKDAASLESQL 1317
Cdd:TIGR02169 231 EKEAL-------ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1318 QDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKL 1397
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1398 LKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqmlaeeknisaryaEERDRAEAE 1477
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1478 AREKETKALSLAraleealEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1557
Cdd:TIGR02169 450 IKKQEWKLEQLA-------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1558 T-----------EDAKLRLEV----NMQAMKAQFERDLQARDEQNEEKK--RMLVKQVRELEAEledERKQRALAVAAKK 1620
Cdd:TIGR02169 523 VhgtvaqlgsvgERYATAIEVaagnRLNNVVVEDDAVAKEAIELLKRRKagRATFLPLNKMRDE---RRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1621 KMEMDLKDLEGQIEAANKA--RD----EAIKQLRKL--QAQMKDYQRELEE--------ARASRDEIFAQSKESEKkLKG 1684
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKYvfGDtlvvEDIEAARRLmgKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1685 LEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTL 1764
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1765 QVDTLNSELAGERSAAQKSENARQQLER-----QNKELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAKERAA 1839
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEV-SRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1840 ANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSR 1919
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
....*....
gi 2024363113 1920 EVSTLKNRL 1928
Cdd:TIGR02169 918 RLSELKAKL 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1596-1934 |
2.84e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1596 KQVRELEAELEdeRKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAqmkdyqrELEEARASRDEIFAQS 1675
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1676 KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQSNMELL 1755
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-------ELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1756 NERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgsvkskfkATISTLEAKIAQLEEQLEQEAK 1835
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE--------EAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1836 ERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRAnASRRKLQRELDDATEANE 1915
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFL 507
|
330
....*....|....*....
gi 2024363113 1916 GLSREVSTLKNRLRRGGPI 1934
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAV 526
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1484 |
3.27e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 95.59 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 845 LQVTRQEEELQaKDEELMKVKEKQTKVEAELEEMERKHQQLLE-EKNILAEQLQAETELFAEAEEmrARLAAKKQELEEI 923
Cdd:PTZ00121 1178 AEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 924 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-----ARQKLQLEKVTAEAK----IKKMEEEILLLEDQN 994
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaeeKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 995 SKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKK--EEKTRQELEKAKRKLDGETTDLQDQIA 1072
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1073 ELQAQIEEL--KIQLAKKEEEL--QAALARGDEEAVQKNNALKVIREL--QAQIAELQEDLESEKASRNKAEKQKRDlSE 1146
Cdd:PTZ00121 1415 AAKKKADEAkkKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKAEEAkkKAEEAKKADEAKKKAEEAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1147 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRhataleelSEQLEQAKRFKANLEKNK 1226
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--------ADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1227 qgleSDNKELACEVKVLQQVKAESEHKRKKldAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSllEEAEKKGIKF 1306
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQ 1637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1307 AKDAAslESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNlekqmlalqaqlAEAKKKVDDDLGT 1386
Cdd:PTZ00121 1638 LKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA------------AEALKKEAEEAKK 1703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1387 IEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISAR 1466
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 2024363113 1467 YAEERDRAEAEAREKETK 1484
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1656 |
8.92e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.88 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 845 LQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIL 924
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 925 HDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM 1004
Cdd:pfam02463 268 AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1005 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKtRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1084
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK-LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1085 LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT--- 1161
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkar 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1162 ------TAAQQELRTKREQEVAELKKAIEEETKNHEAQI--QEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESD- 1232
Cdd:pfam02463 507 sglkvlLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIstAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPk 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1233 -------------NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA 1299
Cdd:pfam02463 587 lklplksiavleiDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1300 EKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKK 1379
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1380 VDDDlgtiEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1459
Cdd:pfam02463 747 EEEE----EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1460 EKNISArYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQ 1539
Cdd:pfam02463 823 LIEQEE-KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1540 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQN--EEKKRMLVKQVRELEAELEDERKQRALAVA 1617
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
810 820 830
....*....|....*....|....*....|....*....
gi 2024363113 1618 AKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKD 1656
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1136-1717 |
1.49e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.82 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1136 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR--QRHATALEELSEQLE 1213
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEklEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1214 QAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDaQVQELTAKVTEGERLRVELAEKANKLQNELDNVS 1293
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1294 SLLEEAEKKGIKFAKDAASLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLQEQQ------------EEEEEAR 1359
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekelEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1360 KNLEKQMLALQAQLAEAKKKVDDDLGTIEGL---------------EENKKKLLKD-MESLSQRLEEKAMAYDKLEKTKN 1423
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreltEEHRKELLEEyTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1424 RLqqelddlmVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFE 1503
Cdd:PRK03918 481 EL--------RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1504 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQAR 1583
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1584 DEQNEEKKR--MLVKQVRELEAELEDERKQRAlaVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQ---MKDYQ 1658
Cdd:PRK03918 633 EELAETEKRleELRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEleeREKAK 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1659 RELEEARASRDEIfaqsKESEKKLKGLEAEilqlqeefaaserARRHAEQERDELADEI 1717
Cdd:PRK03918 711 KELEKLEKALERV----EELREKVKKYKAL-------------LKERALSKVGEIASEI 752
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
942-1761 |
3.23e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 91.96 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 942 QNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLA-EEEE 1020
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRdEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1021 KAKNLAKLKNKQEMMITDLEER------LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQA 1094
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENkeeekeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1095 ALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLdTTAAQQELRTKREQ 1174
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL-ELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1175 EVAELKKAIEEETKNHEAQIQEIRQRHATALEE-LSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHK 1253
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1254 RKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAE-----KKGIKFAKDAASLESQLQDTQELLQEET 1328
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVenykvAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1329 RQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLAlqAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRL 1408
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA--TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1409 EEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSL 1488
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1489 AraleEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR-LEV 1567
Cdd:pfam02463 730 A----QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEeLRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1568 NMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1647
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1648 RKLQaQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASErarrhaEQERDELADEIANSASGKSAL 1727
Cdd:pfam02463 886 DELE-SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP------EELLLEEADEKEKEENNKEEE 958
|
810 820 830
....*....|....*....|....*....|....
gi 2024363113 1728 LDEKRRLEARIAQLEEELEEEQSNMELLNERFRK 1761
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1073-1694 |
4.49e-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: 90.85 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1073 ELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKasrNKAEKQKRDLSEELEALK 1152
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1153 TEledtldttaaqQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHaTALEELSEQLEQAKRFKANLEKNKQGLESD 1232
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1233 NKELACEVKVLQQVKAESEHKRKKLDAQVQ---ELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKD 1309
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1310 AASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR-----KNLEKQMLALQAQLAEAKKKVDDDL 1384
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1385 GTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDdlmvdldhqrqivsNLEKKQKKFDQMLAEEKNIS 1464
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK--------------NLESQINDLESKIQNQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1465 ARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1544
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1545 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQVRELEAELE--DERKQRALAVAAKKKM 1622
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE-KESKISDLEDELNkdDFELKKENLEKEIDEK 566
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 1623 EMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQE 1694
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1429 |
6.06e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.87 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 850 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 929
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 930 RveeeeernqilqnekkkmqghiqdleeqldeEEGARQKLQLEKVTAEAkikkmeeeillLEDQNSKFLKEKKLMEDRIA 1009
Cdd:PRK02224 294 E-------------------------------RDDLLAEAGLDDADAEA-----------VEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1010 ECTSQLAEEEEKAKNLAKlknkqemMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE 1089
Cdd:PRK02224 332 ECRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1090 EELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLES-----------------EKASRNKAEKQKRDLSEELEALK 1152
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1153 TELEDTLDTTAAqqelRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQakrfkanLEKNKQGLEsd 1232
Cdd:PRK02224 485 EDLEEEVEEVEE----RLERAEDLVEAEDRIERLEERREDLEELIAERRET-IEEKRERAEE-------LRERAAELE-- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1233 nkelacevkvlqqvkAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNeLDNVSSLLEEAEKKGikfaKDAAS 1312
Cdd:PRK02224 551 ---------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE----DEIER 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1313 LESQLQDTQElLQEETRQKL-NLSSRIRQLEEE--KNNLQEQQEEEEEARKNLEKQMLALQaQLAEAKKKVDDDLGTIEG 1389
Cdd:PRK02224 611 LREKREALAE-LNDERRERLaEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLD-ELREERDDLQAEIGAVEN 688
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2024363113 1390 LEENKKKLLKDMESLSQRLEEKAMAYDK---LEKTKNRLQQEL 1429
Cdd:PRK02224 689 ELEELEELRERREALENRVEALEALYDEaeeLESMYGDLRAEL 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1363-1930 |
7.69e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.48 E-value: 7.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1363 EKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAmaydklEKtknrlQQELDDLMVDLDHQRQI 1442
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1443 VSNLEKKQKKFDQMLAEEKNISARYAEERD--RAEAEAREKETKALSLARALEEaleakeefeRQNKQLRADMEDLMSSK 1520
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARREELE---------DRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1521 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAklrlevnmqamkaqferdlqaRDEQNEEkkrmlvkqVRE 1600
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA---------------------VEDRREE--------IEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1601 LEAELEDERKQRALAvaakkkmEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDE---------- 1670
Cdd:PRK02224 389 LEEEIEELRERFGDA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpv 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1671 ----IFAQSKESEKKLKGLEAEILQLQEEFAASErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELE 1746
Cdd:PRK02224 462 egspHVETIEEDRERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1747 EEQSNMELLNERfrkttlqVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkfKATISTLEAKIAQL 1826
Cdd:PRK02224 534 EKRERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES--LERIRTLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1827 EEQLEqeakeraaanklvRRTEKklKEVFMQVEDERRhadqykEQMEKANARMKQLKRQLEEAEEEATRANASR-----R 1901
Cdd:PRK02224 605 EDEIE-------------RLREK--REALAELNDERR------ERLAEKRERKRELEAEFDEARIEEAREDKERaeeylE 663
|
570 580
....*....|....*....|....*....
gi 2024363113 1902 KLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1114-1721 |
7.71e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 90.74 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1114 RELQAQIAELQEDLESEKASRNKAEK--QKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEEtknHE 1191
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA---EL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1192 AQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKE-LACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTE 1270
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1271 GERlrvELAEKANKLQNELDNVSSLLEEAEKkgikfakDAASLESQLQDTQEllqeetrqklnlssRIRQLEEEKNNLQE 1350
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEE-------ALAEAEAALRDLRR--------------ELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1351 QqeeeeeaRKNLEKQMLALQAQLAEAKKKVDDDL-----------------GTIEGL----------------------E 1391
Cdd:COG4913 434 R-------KSNIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvppehyaaalrwvN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1392 ENKKKLLKDMESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMV------------DLDHQR-------QIVSN 1445
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPrldpdslAGKLDFKPHPFRAWLEAELGrrfdyvcvdspeELRRHPraitragQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1446 LEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKEtKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK 1525
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1526 NVHELEKSKRTLEQ------QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVR 1599
Cdd:COG4913 666 AEREIAELEAELERldassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1600 ELEAELEDERKQRALAVAAKKKMEmdlkDLEGQIEAANKARDEAIKQLRKLqaqMKDYQRELEEARASRDEIFAQSKESE 1679
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYL 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2024363113 1680 KKLKGLEAEIL-QLQEEFAasERARRHAEQERDELADEIANSA 1721
Cdd:COG4913 819 ALLDRLEEDGLpEYEERFK--ELLNENSIEFVADLLSKLRRAI 859
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1482 |
8.71e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 828 KLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAElEEMERKHQQLLEEKNILAEQLQAETELFAEAE 907
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 908 EMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAK-----IKK 982
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaeeDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 983 MEEEILLLEDQNSKFLKEKKLMED-RIAECTSQLAEEEEKAKnlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLD 1061
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1062 GETTDLQDQIAELQAQIEELKiqlAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1141
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1142 RDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATAleelsEQLEQAKRFKAN 1221
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-----EELKKAEEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1222 LEKNKQGLESDNKElACEVKVLQQ---VKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEE 1298
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK-AEELKKAEEenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1299 AEKKGIKFAKDAASLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALqaqlaeAKK 1378
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV------IEE 1783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1379 KVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYdkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1458
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENG 1861
|
650 660
....*....|....*....|....
gi 2024363113 1459 EEKNISARYAEERDRAEAEAREKE 1482
Cdd:PTZ00121 1862 EDGNKEADFNKEKDLKEDDEEEIE 1885
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
990-1802 |
9.31e-18 |
|
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: 90.18 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 990 LEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLkkeEKTRQELEKAKrkldgetTDLQD 1069
Cdd:pfam15921 94 LNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQL---QNTVHELEAAK-------CLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1070 QIAELQAQIEELKIQLAKKE---EELQAALARGDEEAVQK---NNALKVI--RELQAQIAELQEDLESEKASrnkAEKQK 1141
Cdd:pfam15921 164 MLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyeHDSMSTMhfRSLGSAISKILRELDTEISY---LKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1142 RDLSEELEALKTELEDTLDTTAAQQELRtkreqevaelkkaIEEETKNHEAQIQEIRQRHATALEE---LSEQL----EQ 1214
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLLQQHQDR-------------IEQLISEHEVEITGLTEKASSARSQansIQSQLeiiqEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1215 AKRFKANLEKNKQGLESDNKELACEvkvLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSS 1294
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSE---LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1295 LLEEAEKKgikfakdaASLESqlQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARK----NLEKQMLALQ 1370
Cdd:pfam15921 385 DLHKREKE--------LSLEK--EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1371 AQlAEAKKKVDDDLGTIEGLEENKKKLLKDmeslsqrLEEKAMAYDKLEKTknrlqqeLDDLMVDLDHQRQIV----SNL 1446
Cdd:pfam15921 455 GK-NESLEKVSSLTAQLESTKEMLRKVVEE-------LTAKKMTLESSERT-------VSDLTASLQEKERAIeatnAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1447 EKKQKKFDQMLAEEKNISaryaEERDRAEAEAREKETKALSLARALEEALEakeeferqnkqLRADMEDLMSSKDDVGKN 1526
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLK----NEGDHLRNVQTECEALKLQMAEKDKVIEI-----------LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1527 VHELEKSKRTLEQQVEEMRTQLEELEdELQATEDAKLrlevnmqamkaqfeRDLQARDEQNEEKKRMLVKQVRELEAELE 1606
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDAKI--------------RELEARVSDLELEKVKLVNAGSERLRAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1607 DERKQRALAVAAKKKMEMDLKDLEGQIEAANK----ARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1682
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1683 KGLEAEIlqlqeefaASERARRHAEQERDELADE-IANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRK 1761
Cdd:pfam15921 730 MGMQKQI--------TAKRGQIDALQSKIQFLEEaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR 801
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 2024363113 1762 ttLQVDTLNSELAGERSAAQKSEnARQQLERQNKE-LKAKLQ 1802
Cdd:pfam15921 802 --LKEKVANMEVALDKASLQFAE-CQDIIQRQEQEsVRLKLQ 840
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
899-1737 |
1.60e-17 |
|
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: 89.51 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 899 ETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKkmqghiQDLEEQLDEEEGARQKLQLEKVTAEA 978
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 979 KIKKMEEEILLLEDQNSKFLKEkklmedriaectsqlaeeeekakNLAKLKNKQEMmitdleerlkkEEKTRQELEKAKR 1058
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1059 KLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKviRELQAQIAELQEDLESEKASRNKAE 1138
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1139 KQkrdLSEELEALKTEledtLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQ--IQEIRQRHATALEELSEQLEQAK 1216
Cdd:pfam12128 440 YR---LKSRLGELKLR----LNQATATPELLLQLENFDERIERAREEQEAANAEVerLQSELRQARKRRDQASEALRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1217 RFkanLEKNKQGLEsdnkelacEVKVLQQVKAESEHKRKKLDAQV-QELTAKVTEGERL-RVELAEKANKlqneldnvSS 1294
Cdd:pfam12128 513 RR---LEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDwEQSIGKVISPELLhRTDLDPEVWD--------GS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1295 LLEEAEKKGIKFAKDAASLESQLQDTQELlqeetRQKLNLSSRIRQLEEEKnnlqeqqeeeeeaRKNLEKQMLALQAQLA 1374
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEEL-----RERLDKAEEALQSAREK-------------QAAAEEQLVQANGELE 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1375 EAKKKVDDDLGTIEGLEENKKKLLKDMESLSqrleekamayDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKFD 1454
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWL 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1455 QMLAEEKnISARYAEERDRAEAEarekETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1534
Cdd:pfam12128 703 EEQKEQK-REARTEKQAYWQVVE----GALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1535 RTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFERDLQardEQNEEKKRMLVKQVRELEAELEDERKQRAL 1614
Cdd:pfam12128 778 RTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQLAR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1615 AVAAKKkmeMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARASRDEIFAQSKESEKKLKGLEAEI 1689
Cdd:pfam12128 833 LIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSESV 909
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1690 LQLQEEFAASERARRHAEQER--DELADEIANSASGKSALLDEKRRLEAR 1737
Cdd:pfam12128 910 KKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1113-1738 |
5.48e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1113 IRELQAQIAELQEDLESEKAsrnkaEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEVAELKKAieeetknhea 1192
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIE-----EKEEKDLHERLNGLESELAEL---DEEIERYEEQREQARETRDEA---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1193 qiQEIRQRHATALEELSEqleqakrfkanleknkqglesdnkeLACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGE 1272
Cdd:PRK02224 240 --DEVLEEHEERREELET-------------------------LEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1273 RLRVELAEKANKLQNELDNVSSLLEEaekkgikFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlqeqq 1352
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1353 eeeeearKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEEnkkkllkDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1432
Cdd:PRK02224 359 -------EELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1433 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS-ARYAEERDRAEAEAREKETKAlslaraleealeakeeferqnkQLRA 1511
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGKCPEcGQPVEGSPHVETIEEDRERVE----------------------ELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1512 DMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELqatedaklrlevnmqamkAQFERDLQARDEQNEEKK 1591
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELI------------------AERRETIEEKRERAEELR 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1592 rmlvKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEI 1671
Cdd:PRK02224 544 ----ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1672 FAQSKESEKKLKGLEAEILQLQEEFaasERARRHAEQERDELADEIANSASGKSALLDEKR-RLEARI 1738
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEI 683
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
977-1566 |
7.92e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.00 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 977 EAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKA 1056
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1057 KRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEEL---QAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKAS 1133
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1134 RNKAEKQKRDLSEELEALKTELEDTldttaAQQELRTKREQEvaELKKAIEEETKnheaqiqeirqrhataleelseQLE 1213
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNT-----QTQLNQLKDEQN--KIKKQLSEKQK----------------------ELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1214 QAKRFKANLEKNKQGLESdnkelacEVKVLQQVKAESEHKR-----KKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1288
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKS-------EISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1289 LDNVSSlleEAEKKGIKFAKDAASLESQLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLA 1368
Cdd:TIGR04523 351 LTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1369 LQAQLAEAKKKVDDDLGTIEGLEENK-------KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQ 1441
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDsvkeliiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1442 IVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSS 1519
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieELKQTQKSLKKK 583
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2024363113 1520 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE 1566
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1203-1922 |
1.12e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.89 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1203 TALEELSEQLEQAKRFKANLEKNKQglesdnkelacEVKVLQQVKAESEhkrkKLDAQVQELTAKVTEGERLRVELAE-K 1281
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELAE----RYAAARERLAELEYLRAALRLWFAQrR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1282 ANKLQNELDNVSSLLEEAEKKgikfakdAASLESQLQDTQELLQEETRQKLNLS-SRIRQLEEEKNNLQEQQEEEEEARK 1360
Cdd:COG4913 290 LELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1361 NLEKQMLALQAQLAEakkkvdddlgTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQR 1440
Cdd:COG4913 363 RLEALLAALGLPLPA----------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1441 QIVSNLEKKQKKFDQMLAEEKNISA---RYA------EERDRAEAEAREKE--TKALSLARALEEALEAKEEFERQNKQL 1509
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEaelPFVgelievRPEEERWRGAIERVlgGFALTLLVPPEHYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1510 RADMEDLMSSkddvGKNVHELEKSKRTLEQQVE----EMRTQLEEL------------EDELQATEDAkLRLEVNMQAMK 1573
Cdd:COG4913 513 RLVYERVRTG----LPDPERPRLDPDSLAGKLDfkphPFRAWLEAElgrrfdyvcvdsPEELRRHPRA-ITRAGQVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1574 AQFERDLQARDEQ-------NEEKKRMLVKQVRELEAELEDerkqralAVAAKKKMEMDLKDLEGQIEAANKARD--EAI 1644
Cdd:COG4913 588 TRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAE-------AEERLEALEAELDALQERREALQRLAEysWDE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1645 KQLRKLQAQMKDYQRELEEARASRDEifaqskesekkLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAnsasgk 1724
Cdd:COG4913 661 IDVASAEREIAELEAELERLDASSDD-----------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELE------ 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1725 sALLDEKRRLEARIAQLEEELEEEQSnmELLNERFRkttlqvdtlnsELAGERSAAQKSENARQQLERQNKELKAKLQEL 1804
Cdd:COG4913 724 -QAEEELDELQDRLEAAEDLARLELR--ALLEERFA-----------AALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1805 EGSV---KSKFKATISTLEAKIAQLEE------QLEQE---AKERAAANKLVRRTEKKLKEVFMQVEDERRHAdqyKEQM 1872
Cdd:COG4913 790 ERAMrafNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREI---KERI 866
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1873 EKANARMKQLK----RQLeeAEEEATRANASRRKLQRELDDATEANEGLSREVS 1922
Cdd:COG4913 867 DPLNDSLKRIPfgpgRYL--RLEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-1910 |
2.45e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1626 LKDLEGQIEAANKAR----DEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASER 1701
Cdd:COG1196 202 LEPLERQAEKAERYRelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1702 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeLEEEQsnmELLNERFRKTTLQVDTLNSELAGERSAAQ 1781
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEEL---AELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1782 KSENARQQLERQNKELKAKLQELEGSVKSKFKA------TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVF 1855
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEEllealrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1856 MQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDA 1910
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
852-1567 |
4.76e-16 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 84.78 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 852 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRARLAAKK---QELEEILHDLE 928
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 929 srveeeeernqilQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEkvtAEAKIKKMEEEILLLEDQNSKFLKEKK------ 1002
Cdd:pfam15921 198 -------------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkiell 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1003 --LMEDRIAECTSQ-------LAEEEEKAKNLA------------KLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLD 1061
Cdd:pfam15921 262 lqQHQDRIEQLISEheveitgLTEKASSARSQAnsiqsqleiiqeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1062 GettdlqdqiaelqaQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1141
Cdd:pfam15921 342 D--------------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRD 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1142 RDLSEELEALKTELED------TLDT--TAAQQELRTKREQEVAELKKAIE--EETKNHEAQIQEIRQRHATALEELSEQ 1211
Cdd:pfam15921 408 TGNSITIDHLRRELDDrnmevqRLEAllKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1212 ---LEQAKR----FKANLEKNKQGLESDNKELA-------CEVKVLQQVKAESEHKRkkldaQVQeltakvTEGERLRVE 1277
Cdd:pfam15921 488 kmtLESSERtvsdLTASLQEKERAIEATNAEITklrsrvdLKLQELQHLKNEGDHLR-----NVQ------TECEALKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1278 LAEKANK---LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEE 1354
Cdd:pfam15921 557 MAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVK 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1355 EEEARknlEKQMLALQaqlaEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAmayDKLEKTKNRLQQELDDLMV 1434
Cdd:pfam15921 637 LVNAG---SERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQS 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1435 DLDHQRQIVSNLEKKQ-KKFDQMLAEEKNISARyaeerdRAEAEAREKETKALSLAraLEEALEAKEEFERQNKQLRADM 1513
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLEEA--MTNANKEKHFLKEEKNKLSQEL 778
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 1514 EDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1567
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
999-1594 |
5.03e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 999 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL-----------------EKAKRKLD 1061
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELetleaeiedlretiaetEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1062 GETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1141
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1142 RDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKAIEEETKnheaqiqeirqrhatALEELSEQLEQAKRFKAN 1221
Cdd:PRK02224 359 EELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRE---------------RFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1222 LEKNKQGLESDNKELACEVKVLQQVKAESEhkrKKLDA-QVQELTAKVTEGERLRV--ELAEKANKLQNELDNVSSLLEE 1298
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAE---ALLEAgKCPECGQPVEGSPHVETieEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1299 AEKKgIKFAKDAASLESQLQDTQEllqeetrQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1378
Cdd:PRK02224 494 VEER-LERAEDLVEAEDRIERLEE-------RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1379 KVDDDLGTIEGLEenkkkllkdmeslsQRLEEKAMAYDKLEKtknrlqqeLDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1458
Cdd:PRK02224 566 EAEEAREEVAELN--------------SKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1459 EEKNisaRYAEERDRAEAEAREKETKALSlaraleealeakeeferqnkQLRADMEDLMSSKDDVGKNVHELEKSKRTLE 1538
Cdd:PRK02224 624 ERRE---RLAEKRERKRELEAEFDEARIE--------------------EAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1539 QQ---VEEMRTQLEELEDELQATEDAKLRLEV------NMQAMKAQFERDLQARDEqnEEKKRML 1594
Cdd:PRK02224 681 AEigaVENELEELEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQRNV--ETLERML 743
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
985-1716 |
6.25e-16 |
|
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: 84.25 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 985 EEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEeeKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKaKRKLDGET 1064
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-KREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1065 TDLQDQIAELQAQIEELKIQLAKKEE-----ELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEK 1139
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1140 QKRDLSEELEALKTELedtldttaaQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEE---LSEQLEQAK 1216
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLH---------SQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKlqsLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1217 RFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNeLDNVSSLL 1296
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1297 EEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknnLQEQQEEEEEARKNLEKQMLALQAQLAEA 1376
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR----GEQTYAQLETSEEDVYHQLTSERKQRASL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1377 KKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQrQIVSNLEKKQKKFDQM 1456
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE-QDLQDVRLHLQQCSQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1457 LAEEKNISARYAEERdraeaeAREKETKALSLARALEEaleakeeferQNKQLRADMEDLMSSKddvgknVHELEKSKRT 1536
Cdd:TIGR00618 641 LALKLTALHALQLTL------TQERVREHALSIRVLPK----------ELLASRQLALQKMQSE------KEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1537 LEQQVEEMRTQLEELEdelqatEDAKLRLEVNMQAMKAQfeRDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAV 1616
Cdd:TIGR00618 699 LAQCQTLLRELETHIE------EYDREFNEIENASSSLG--SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1617 AAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK----KLKGLEAEILQL 1692
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQ 850
|
730 740
....*....|....*....|....
gi 2024363113 1693 QEEFAASERARRHAEQERDELADE 1716
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1515 |
1.48e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 82.85 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 859 EELMKVKEKQTKVEAELEEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD----------LE 928
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 929 SRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLE----KVTAEAKIKKMEEEILLLEDQNSKFLKEKklm 1004
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQaenaRLEMHFKLKEDHEKIQHLEEEYKKEINDK--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1005 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTD----LQDQIAELQAQIEE 1080
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1081 LKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1160
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1161 TTAAQ----QELRT-----------------------KREQEVAELKKAIEEETKNHEAQIQEIR---QRHATALEELSE 1210
Cdd:pfam05483 399 FKNNKevelEELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1211 QLEQAKRFKANLEKNKQGLESDNKEL-------ACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerLRVELAEKAN 1283
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELtqeasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN---LRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1284 KLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLE 1363
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1364 KQMLALQAQLAEAKKKVDDDLGTIEGLEENKK----KLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQ 1439
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1440 rqivsnLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1515
Cdd:pfam05483 716 ------YDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1056-1431 |
2.61e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1056 AKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1135
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1136 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIE----EETKNHEAQIQEIRQRHATALEELSEQ 1211
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1212 LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDN 1291
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1292 VSSLLEEAEKKgikfAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK----QML 1367
Cdd:TIGR02169 901 LERKIEELEAQ----IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNML 976
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1368 ALQaQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAM-AYDKLEKTKNRLQQELDD 1431
Cdd:TIGR02169 977 AIQ-EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMeAFEAINENFNEIFAELSG 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
847-1277 |
3.05e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 847 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQELEE 922
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 923 ILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEakIKKMEEEILLLEDQNSKFLKEKK 1002
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAE--LKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1003 LMEDRIAEcTSQLAEEEEKAKNLAKLKNK-QEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQdQIAELQAQIEEL 1081
Cdd:PRK03918 484 ELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAEL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1082 KIQLAKKEEELQAALARGDEEavqknnALKVIRELQAQIAELqEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT 1161
Cdd:PRK03918 562 EKKLDELEEELAELLKELEEL------GFESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1162 TA-AQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLEsDNKELACEV 1240
Cdd:PRK03918 635 LAeTEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKEL 713
|
410 420 430
....*....|....*....|....*....|....*..
gi 2024363113 1241 KVLQQVKAESEHKRKKldaqVQELTAKVTEGERLRVE 1277
Cdd:PRK03918 714 EKLEKALERVEELREK----VKKYKALLKERALSKVG 746
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
851-1437 |
4.26e-15 |
|
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: 81.22 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 851 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKnilaEQLQAETELFaeaeemrarlaakKQELEEILHDLESR 930
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK----EELENELNLL-------------EKEKLNIQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 931 VEEEEERNQILQNEKKKMQGH------IQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEkklm 1004
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNkslesqISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ---- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1005 edrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEErlKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1084
Cdd:TIGR04523 269 ---LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1085 LAKKEEELQAALARG---DEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN----KAEKQKRDLSEELEALKTELED 1157
Cdd:TIGR04523 344 ISQLKKELTNSESENsekQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiqNQEKLNQQKDEQIKKLQQEKEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1158 TLDTTAAQQELRTKREQEVAELKKAI---EEETKNHEAQIQEIRQrhataleELSEQLEQAKRFKANLEKNKQGLESDNK 1234
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDsvkELIIKNLDNTRESLET-------QLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1235 ELacevKVLQQVKAESEHKRKKLDAQVQELTAKVtegERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLE 1314
Cdd:TIGR04523 497 EL----KKLNEEKKELEEKVKDLTKKISSLKEKI---EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1315 -SQLQDTQELLQEETRQKLNLssrIRQLEEEKNNLQEQQEeeeearkNLEKQMLALQAQLAEAKKKVdddlgtiEGLEEN 1393
Cdd:TIGR04523 570 iEELKQTQKSLKKKQEEKQEL---IDQKEKEKKDLIKEIE-------EKEKKISSLEKELEKAKKEN-------EKLSSI 632
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2024363113 1394 KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLD 1437
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1243-1929 |
5.04e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1243 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVEL--AEKANKLQNELDNV-----SSLLEEAEKKGIKFAKDAASLES 1315
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1316 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR-KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENK 1394
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1395 KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqrqiVSNLEKKQKKFDQMLAEEKnisaryaEERDRA 1474
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL----------RAELEEVDKEFAETRDELK-------DYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1475 EAEAREKEtkalSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1554
Cdd:TIGR02169 395 EKLKREIN----ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1555 LQATEDAKLRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELEAELE------------DERKQRALAVAAKKKM 1622
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1623 EMDLKDLEGQIEaankardEAIKQLRKLQA---------QMKDYQRELEEAR------------------------ASRD 1669
Cdd:TIGR02169 550 NNVVVEDDAVAK-------EAIELLKRRKAgratflplnKMRDERRDLSILSedgvigfavdlvefdpkyepafkyVFGD 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1670 EIFAQSKESEKKLKG------LEAEILQ---------LQEEFAASERARRHAEQERdeLADEIANSASGKSALLDEKRRL 1734
Cdd:TIGR02169 623 TLVVEDIEAARRLMGkyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQR--LRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1735 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgSVKSKFKA 1814
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1815 TISTLEAKIA-----QLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEA 1889
Cdd:TIGR02169 780 ALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2024363113 1890 EEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLR 1929
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1280-1854 |
1.42e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1280 EKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR 1359
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1360 KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKL--LKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLD 1437
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1438 HQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAeaREKETKALSLARALEEaleakeeferQNKQLRADMEDLm 1517
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKE----------ELERLKKRLTGL- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1518 sSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQARDEQNEEKKRMLvkq 1597
Cdd:PRK03918 385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL--- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1598 vRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARASRDEIFAQ 1674
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1675 SKESEKKLKGLEAEILQLQE---EFAASERARRHAEQERDELADEIANSASGKSALLDEK-------------------- 1731
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaeke 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1732 -RRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGErsaaqKSENARQQLERQNKELKAKLQELEGsVKS 1810
Cdd:PRK03918 614 lEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-----EYEELREEYLELSRELAGLRAELEE-LEK 687
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2024363113 1811 KFKATISTLeakiaqleEQLEQEAKERAAANKLVRRTEKKLKEV 1854
Cdd:PRK03918 688 RREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERV 723
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1130-1875 |
1.89e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.63 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1130 EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1209
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1210 EQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKAN-KLQNE 1288
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKkKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1289 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDtQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLA 1368
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1369 LQAQLAEAKKKVDDDLGTIEglEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1448
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEE--LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1449 KQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEferqnKQLRADMEDLMSSKDDVGKNVH 1528
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE-----NYKVAISTAVIVEVSATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1529 ELEKSKRTLEQQVEEMRTQLEELEDELqateDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1608
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLK----LPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1609 RKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFA---QSKESEKKLKGL 1685
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKkkeQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1686 EAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTL- 1764
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLk 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1765 -QVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAAnKL 1843
Cdd:pfam02463 798 aQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL-KE 876
|
730 740 750
....*....|....*....|....*....|..
gi 2024363113 1844 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKA 1875
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
803-1449 |
3.46e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 803 RKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEaeleemERKH 882
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 883 QQLLEEKnilAEQLQAETELFAEAEEMRARLAAKKQELEeilhdlesrveeeeernqilqnekkkmqghiqdleeqldee 962
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKKAEE----------------------------------------- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 963 egARQKLQLEKVTAEAkiKKMEEEILLLEDQNSKFLKEKKLMEDRIAEcTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1042
Cdd:PTZ00121 1482 --AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1043 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQIEELKIQ----LAKKEEELQAALARGDEEAVQKNNALKVIRELQA 1118
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1119 QIAELQEDLESEKasrNKAEKQKRdlSEELEALKTELEdtldttaAQQELRTKREQEvaELKKAIEEETKNHEAQIQEir 1198
Cdd:PTZ00121 1634 KVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE-- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1199 qrhatalEELSEQLEQAKRFKAnlEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKvtEGERLRVEL 1278
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK--KIAHLKKEE 1766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1279 AEKANKLQNELDNV--SSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEET----RQKLNLSSRIRQLEEEKN---NLQ 1349
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEDSAIKEVADSKNmqlEEA 1846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1350 EQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESlsqRLEEKAMAYDKLEKTKNRLQQEl 1429
Cdd:PTZ00121 1847 DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER---EIPNNNMAGKNNDIIDDKLDKD- 1922
|
650 660
....*....|....*....|
gi 2024363113 1430 DDLMVDLDHQRQIVSNLEKK 1449
Cdd:PTZ00121 1923 EYIKRDAEETREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
917-1693 |
3.77e-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: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 917 KQELEEILHDLESRVEEEEER----NQILQNEKKKMQGHIQDLEEQLdeeegarQKLQLEKvTAEAKIKKME---EEILL 989
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRlnesNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRREsqsQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 990 LEDQNS--KFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL------------EK 1055
Cdd:pfam15921 145 NQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1056 AKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAlargdeeavQKNNALKVIRELQAQIAELqedleSEKASrn 1135
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ---------HQDRIEQLISEHEVEITGL-----TEKAS-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1136 KAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQA 1215
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1216 KRF---KANLEKNKQGLESD----NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1288
Cdd:pfam15921 366 DQFsqeSGNLDDQLQKLLADlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1289 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQqeeeeearknlEKQMLA 1368
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1369 LQAQLAEAKKKVDDDLGTIEGLeENKKKLLKDMESLSQRLEEKAMAYDKLEKTknrLQQELDDLMVDLDHQRQIVSNLEK 1448
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHL-KNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1449 KQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM----SSKDDVG 1524
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELN 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1525 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVK--QVRELE 1602
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS---AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgQIDALQ 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1603 AELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1682
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDII 827
|
810
....*....|.
gi 2024363113 1683 KGLEAEILQLQ 1693
Cdd:pfam15921 828 QRQEQESVRLK 838
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
979-1805 |
4.91e-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: 78.16 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 979 KIKKMEEEILLLEDQNSKFLKEKKLMEDRiaecTSQLAEEEEKA-----KNLAKLKNKQEMMITDLEERLKKEEKTRQEL 1053
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKD----NSELELKMEKVfqgtdEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1054 EKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQA--------ALARGDEEAVQKNNALKVIRELQAQIAELQE 1125
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1126 DLESEKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELKKAIEEETKNHEAQIQEIRQR 1200
Cdd:TIGR00606 412 QLCADLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1201 HATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESehkRKKLDAQVQELTAKVTEGERLRVELAE 1280
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGY 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1281 KANK--LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRI------RQLEEEKNNLQEQQ 1352
Cdd:TIGR00606 569 FPNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEI 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1353 EEEEEARKNLEKQMLALQAQLAEAKKK-------VDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRL 1425
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1426 QQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQ 1505
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1506 NKQL-RADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQARd 1584
Cdd:TIGR00606 809 AQQAaKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL----KSEKLQIGTNLQRR- 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1585 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKardeaikqlrKLQAQMKDYQRELEEA 1664
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1665 RASRDEIFAQSKES-EKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEE 1743
Cdd:TIGR00606 954 HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 1744 ELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELE 1805
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1101-1919 |
5.36e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1101 EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELK 1180
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETG 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1181 KaIEEETKNHEA--QIQEIRQRHATALEELSEQLEQAKRfkanleknkqglESDNKELACEVKVLQQVKAESehKRKKLD 1258
Cdd:PTZ00121 1110 K-AEEARKAEEAkkKAEDARKAEEARKAEDARKAEEARK------------AEDAKRVEIARKAEDARKAEE--ARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1259 AQVQELTAKVTEGER-LRVELAEKANKLQ--NELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqKLNLS 1335
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKaEELRKAEDARKAEaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE---EERNN 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1336 SRIRQLEEEKNNLQEQQEEEEEArknlEKQMLALQAQLAEAKKKVDddlgtieglEENKKKLLKDMESLSQRLEEKAMAy 1415
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKA----EEARKADELKKAEEKKKAD---------EAKKAEEKKKADEAKKKAEEAKKA- 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1416 DKLEKTKNRLQQELDDLMvdldhqrqivSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETkalslARALEEA 1495
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAK----------KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-----AKKKADA 1382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1496 LEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRtLEQQVEEMRT--QLEELEDELQATEDAKLRLEvnmqamk 1573
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKadEAKKKAEEAKKADEAKKKAE------- 1454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1574 aqferdlQARDEQNEEKKRMLVKQVRELEAELEDERKqralAVAAKKKMEMDLKDLEgQIEAANKARDEAIKQLRKLQAQ 1653
Cdd:PTZ00121 1455 -------EAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAEEAK 1522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1654 MKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAASERARRhAEQERDELADEIANSASGKSALLDEKRR 1733
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELK--KAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1734 LEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQlERQNKELKAKLQELEGSVKSKFK 1813
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKAE 1678
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1814 ATISTLEAKiAQLEEQLEQEAKERAAANKLVRRTEKKLK----------EVFMQVEDERRHADQYKEQMEKANARMKQLK 1883
Cdd:PTZ00121 1679 EAKKAEEDE-KKAAEALKKEAEEAKKAEELKKKEAEEKKkaeelkkaeeENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
810 820 830
....*....|....*....|....*....|....*.
gi 2024363113 1884 RQLEEAEEEATRANASRRKLQRELDDATEANEGLSR 1919
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1301 |
5.75e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 840 KVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQE 919
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 920 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEdqnsKFLK 999
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1000 EKKLMEDRIAECTSQLAEEEEKaknlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIA--ELQAQ 1077
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1078 IEELKIQLAKKEEELQAALARGDEEAVQKnnalkvIRELQAQIAELQEDLESEKASRNKA---EKQKRDLSEELEALKTE 1154
Cdd:PRK03918 505 LKELEEKLKKYNLEELEKKAEEYEKLKEK------LIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1155 LEDTLDTTAAQQELRTKreqevaELKKAIEE--ETKNHEAQIQEIRQRhataLEELSEQLEQAkrfkanlEKNKQGLESD 1232
Cdd:PRK03918 579 LEELGFESVEELEERLK------ELEPFYNEylELKDAEKELEREEKE----LKKLEEELDKA-------FEELAETEKR 641
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1233 NKELACEVKVLQQVKAESEHKRK-----KLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1301
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1693 |
6.28e-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: 77.78 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 850 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 929
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 930 RVEEEEERN-QILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEK---KLME 1005
Cdd:TIGR00606 277 RKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1006 DRIAE-------------CTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIA 1072
Cdd:TIGR00606 357 DRHQEhirardsliqslaTRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1073 ELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELqedlesEKASRNKAEKQKRDLSEELEALK 1152
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1153 TELEDTLDTTAAQQElRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA---NLEKNKQGL 1229
Cdd:TIGR00606 511 ADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQT 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1230 ESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerlrvelAEKANKLQNELDNVSSLLEEAEKKGIKFAKD 1309
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1310 AASLESQLQDTQE-------LLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1382
Cdd:TIGR00606 662 TAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1383 DLGTIEGLEENKKKLLKDMESLSQRLEEKamayDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKN 1462
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1463 ISARYAEERDRAEAEarEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEleksKRTLEQQVE 1542
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLV 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1543 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQN---EEKKRMLVKQVRELEAELED-ERKQRALAVAA 1618
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDY 971
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1619 KKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQM--KDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQ 1693
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1592 |
9.64e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.32 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 844 LLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQE 919
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 920 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFL 998
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 999 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGettdlqdqiaeLQAQI 1078
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-----------LLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1079 EELKIQLAKKEEELQAALARGDE-EAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELED 1157
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVEnYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1158 TLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1237
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1238 CEVKVLQQVKAESEHKRKKLDAQVQELTA--KVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLES 1315
Cdd:pfam02463 677 EIQELQEKAESELAKEEILRRQLEIKKKEqrEKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1316 QLQDTQEllQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKK 1395
Cdd:pfam02463 757 LKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1396 KLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAE 1475
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1476 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDEL 1555
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-----------EEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750
....*....|....*....|....*....|....*..
gi 2024363113 1556 QATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKR 1592
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1205-1859 |
1.06e-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: 76.60 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1205 LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1284
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1285 LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK 1364
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1365 QMLALQAQLAEAKKKVDDdlgtIEGLEENKKKLLKDMESLSQRLEEKAmayDKLEKTKNRLQQELDDlmvdldhQRQIVS 1444
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1445 NLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKE---TKAL-SLARALEEALEAKEEFERQNKQLRADMEDLMSsk 1520
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwNKELkSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1521 dDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlqardeQNEEKKRMLVKQVRE 1600
Cdd:TIGR04523 346 -QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ--------NQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1601 LEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1680
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1681 KLKGLEAEILQLqeefaaserarrhaEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFR 1760
Cdd:TIGR04523 497 ELKKLNEEKKEL--------------EEKVKDLTKKI-------SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1761 KTTL--QVDTLNSELagersaaQKSENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERA 1838
Cdd:TIGR04523 556 KENLekEIDEKNKEI-------EELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660
....*....|....*....|.
gi 2024363113 1839 AANKLVRRTEKKLKEVFMQVE 1859
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVK 648
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
976-1486 |
5.35e-13 |
|
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: 74.47 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 976 AEAKIKKMEeeiLLLEDQNSKFLKEKKLMEDRiaectSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEktrQELEK 1055
Cdd:pfam10174 190 AEMQLGHLE---VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQM 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1056 AKRKLDGETTDLQDQIAELQA----------QIEELKIQLAKKEEELQAALARGDEEAVQKNNA---LKVIRE------- 1115
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETLTNQNSDCkqhIEVLKEsltakeq 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1116 ----LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELKKAIE---EETK 1188
Cdd:pfam10174 339 raaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1189 NHEAQIQEIRQRHA----------TALEELSEQLEQAKRFKANLEKNKqglESDNKELACEVKVLQQvkaesehKRKKLD 1258
Cdd:pfam10174 412 DKDKQLAGLKERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK-------ENKDLK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1259 AQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELlQEETRQKLNLSSRI 1338
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRI 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1339 RQLEEEknnLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvDDDLGTIEGL------EENKKKL-LKDMESLSQR---- 1407
Cdd:pfam10174 561 RLLEQE---VARYKEESGKAQAEVERLLGILREVENEKNDK-DKKIAELESLtlrqmkEQNKKVAnIKHGQQEMKKkgaq 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1408 -LEEKAMAYDklEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKAL 1486
Cdd:pfam10174 637 lLEEARRRED--NLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
807-1432 |
5.99e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 807 AKKQQQLSALKILqRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELmkvkekqTKVEAELEEMERKHQQLL 886
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-------RAQEAVLEETQERINRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 887 EEKNILAEQlQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGAR 966
Cdd:TIGR00618 291 KAAPLAAHI-KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 967 QKLQleKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKE 1046
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1047 EKTRQ-------ELEKAKRKLDGETTDLQDQ-----------------IAELQAQIEELKIQLAKKEEELQAA------- 1095
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1096 --LARGDEEAVQKNNALKVIR----ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR 1169
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1170 TKREQEVAELKKAIEEETKN-----HEAQIQEIRQRHATALEELSEQLEQAKRFKANL---EKNKQGLESDNKELACEVK 1241
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLqdvrlHLQQCSQELALKLTALHALQLTLTQERVREHALsirVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1242 VLQQVKAESEHKRKKLDAqVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDA--ASLESQLQD 1319
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTL-LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1320 TQELL------QEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLgtiegleEN 1393
Cdd:TIGR00618 767 NEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL-------EE 839
|
650 660 670
....*....|....*....|....*....|....*....
gi 2024363113 1394 KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1221 |
6.44e-13 |
|
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: 72.49 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 999 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQI 1078
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1079 EELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDT 1158
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1159 LdttAAQQELRTKREQEVAELKKAIEEEtknhEAQIQEIRQRhATALEELSEQLEQAKRFKAN 1221
Cdd:COG4942 187 R---AALEALKAERQKLLARLEKELAEL----AAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1386-1929 |
9.37e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1386 TIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNI-- 1463
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLeg 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1464 SARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQV-- 1541
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIke 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1542 -EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKqralavaAKK 1620
Cdd:PRK03918 333 lEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-------AKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1621 KMEMDLKDLE---GQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASR--DEIFAQSKESEKKLKGLEAEILQLQEE 1695
Cdd:PRK03918 402 EIEEEISKITariGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1696 FAASERARRHAEQER--DELADEIANSASGKSALLDEKRRLEARiaqleeeleeeqsNMELLNERFRKTTLQVDTLNSEL 1773
Cdd:PRK03918 482 LRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAE-------------EYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1774 agerSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEqLEQEAKERAAANKLVRRTEKKLKE 1853
Cdd:PRK03918 549 ----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKK 623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1854 VFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEatRANASRRKLQRELDDATEANEGLSREVSTLKNRLR 1929
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
883-1475 |
2.91e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 883 QQLLEEKNIL--AEQLQaetELFAEAEEMRARLA-AKKQE--LEEILhDLESRVEEEEERNQILQNEKKKMQghiqdlee 957
Cdd:COG4913 215 EYMLEEPDTFeaADALV---EHFDDLERAHEALEdAREQIelLEPIR-ELAERYAAARERLAELEYLRAALR-------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 958 qldeEEGARQKLQLekvtAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEeeKAKNLAKLKNKqemmIT 1037
Cdd:COG4913 283 ----LWFAQRRLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLERE----IE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1038 DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeavqknnALKVIRELQ 1117
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE----------AEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1118 AQIAELQEDLESEKASRN----KAEKQKRDLSEELEALKTEL-----------EDTLDTTAAQQELRTKR------EQEV 1176
Cdd:COG4913 419 RELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAELpfvgelievrpEEERWRGAIERVLGGFAltllvpPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1177 AELKKAIEE---------------------------------ETKNHEAQ---IQEIRQRHATALEELSEQLEQAKRF-- 1218
Cdd:COG4913 499 AAALRWVNRlhlrgrlvyervrtglpdperprldpdslagklDFKPHPFRawlEAELGRRFDYVCVDSPEELRRHPRAit 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1219 KANLEKNKQGL-ESDNKELACEVKVLQQvkaESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLE 1297
Cdd:COG4913 579 RAGQVKGNGTRhEKDDRRRIRSRYVLGF---DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1298 EAEKKgikfaKDAASLESQLQDTQELLQ--EETRQKL-NLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLA 1374
Cdd:COG4913 656 YSWDE-----IDVASAEREIAELEAELErlDASSDDLaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1375 EAKKKVDD-----DLGTIEGLEENKKKLLKD--MESLSQRLEEKamaYDKLEKTKNRLQQELDDLM-----------VDL 1436
Cdd:COG4913 731 ELQDRLEAaedlaRLELRALLEERFAAALGDavERELRENLEER---IDALRARLNRAEEELERAMrafnrewpaetADL 807
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1437 D------------HQRQIVSNLEKKQKKFDQMLAEE-----KNISARYAEERDRAE 1475
Cdd:COG4913 808 DadleslpeylalLDRLEEDGLPEYEERFKELLNENsiefvADLLSKLRRAIREIK 863
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
848-1462 |
4.89e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.20 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 848 TRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 927
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 928 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQ-----------------LEKVTAEAKIKKMEEEILLL 990
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQknidkiknkllklelllSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 991 EDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNlakLKNKQEMMITDLEERlkkeektRQELEKAKRKLDgettDLQDQ 1070
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ---LKDEQNKIKKQLSEK-------QKELEQNNKKIK----ELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELKIQlakKEEELqaalargdeeavqknnalkvIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1150
Cdd:TIGR04523 290 LNQLKSEISDLNNQ---KEQDW--------------------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1151 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIE---EETKNHEAQIQEIRQrhataleelseQLEQAKRFKANLEKNKQ 1227
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQIK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1228 GLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFA 1307
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1308 KDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQeeeeearKNLEKQMLALQAQL--AEAKKKVDDDLG 1385
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNKDDFELkkENLEKEIDEKNK 568
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1386 TIEGLEENKKKLLKDMESLSQRLeekamayDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKN 1462
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELI-------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1038-1212 |
5.72e-12 |
|
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: 67.64 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1038 DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKViRELQ 1117
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1118 AqiaeLQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKAIEEETKNHEAQIQEI 1197
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 2024363113 1198 RQRHATALEELSEQL 1212
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
860-1432 |
7.29e-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: 71.02 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 860 ELMKVKEKQTKVEAELEEMERKHQQLLEEKnilAEQLQAETELF----AEAEEMRARLAA---KKQELEEILHDLESRVE 932
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLpswqSELENLEERLKAltgKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 933 EEEERNQILQNEKKKMQghiqdleeqldeeegaRQKLQLEKVTAEAKIKKMEEEI-LLLEDQNSKFLKEKKLMEDRIAEC 1011
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKI----------------REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1012 TSQLAE---EEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQIEELKIQL 1085
Cdd:pfam12128 450 KLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSALDELELQL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1086 AKKEEELQAALA------------------------------------------RGDEEAVQKNNALKVIRELQAQIAEL 1123
Cdd:pfam12128 530 FPQAGTLLHFLRkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELRERLDKA 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1124 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT-----------TAAQQELRTKREQEVAELKKAIEEETKNHEA 1192
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSANERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1193 QIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGlESDNKelacevkvLQQVKAESEHKRKKLDAQVQEL-TAKVTEG 1271
Cdd:pfam12128 690 QLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG-ALDAQ--------LALLKAAIAARRSGAKAELKALeTWYKRDL 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1272 ERLRVElAEKANKLQNELDNVSSLLEEAEKKGikfaKDAASLESQLQDTqeLLQEETRQKLNLSSRIRQLEEEKNNLQEQ 1351
Cdd:pfam12128 761 ASLGVD-PDVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLATQLSNIERAISELQQQLARL 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1352 QEEEEEARKNLEKQMLALQAQLAEAK---KKVDDDLGTIEGLEENKKKLLKDMeSLSQRLEEKAMAYDKLEKTKNRLQQE 1428
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSenlRGLRCEMSKLATLKEDANSEQAQG-SIGERLAQLEDLKLKRDYLSESVKKY 912
|
....
gi 2024363113 1429 LDDL 1432
Cdd:pfam12128 913 VEHF 916
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1009-1740 |
7.98e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.14 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1009 AECTSQLAEEEEK----AKNLAKLKNKQEMMITDLE---ERL----------KKEEKTRQELEKAKRKLD---GETTDLQ 1068
Cdd:COG3096 295 FGARRQLAEEQYRlvemARELEELSARESDLEQDYQaasDHLnlvqtalrqqEKIERYQEDLEELTERLEeqeEVVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1069 DQIAELQAQ-------IEELKIQLAkkeeELQAALARGDEEAVQKNNALKVIRELQAQ--------------IAELQEDL 1127
Cdd:COG3096 375 EQLAEAEARleaaeeeVDSLKSQLA----DYQQALDVQQTRAIQYQQAVQALEKARALcglpdltpenaedyLAAFRAKE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1128 ESEKASRNKAEkQKRDLSEE-----------LEALKTELEDTLDTTAAQQELRTKREQEvAELKKAIEEETKNHEAQIQE 1196
Cdd:COG3096 451 QQATEEVLELE-QKLSVADAarrqfekayelVCKIAGEVERSQAWQTARELLRRYRSQQ-ALAQRLQQLRAQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1197 IRQRHATAL-EELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKvtegERLR 1275
Cdd:COG3096 529 RQQQNAERLlEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR----APAW 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1276 VELAEKANKLQNELdnvsslleeaekkGIKFAkDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEqqeee 1355
Cdd:COG3096 605 LAAQDALERLREQS-------------GEALA-DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ----- 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1356 eeARKNLEKQMLALQAQ------------------------------------LAEAKKKVD------DDLGTIEGLEEN 1393
Cdd:COG3096 666 --PGGAEDPRLLALAERlggvllseiyddvtledapyfsalygparhaivvpdLSAVKEQLAgledcpEDLYLIEGDPDS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1394 KKKLLKDMESLSQ----RLEEKAMAYDKL-----------EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1458
Cdd:COG3096 744 FDDSVFDAEELEDavvvKLSDRQWRYSRFpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1459 EEKNIsaryAEERDrAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEK-SKRTL 1537
Cdd:COG3096 824 GHLAV----AFAPD-PEAELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLlADETL 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1538 EQQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMK---AQFERdLQARDEQNEEKKRMLVKQVRELEaeledERKQ 1611
Cdd:COG3096 892 ADRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVVQ 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1612 RALAVAAKKKMEM-----DLKD-LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGL 1685
Cdd:COG3096 966 RRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1686 EAEILQLQEEFAASERARRHAeqerdeladEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:COG3096 1046 GVQADAEAEERARIRRDELHE---------ELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
764-1151 |
9.10e-12 |
|
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: 70.86 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 764 GQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRgylARKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVKP 843
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 844 LLQ-VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETElfaeaeemrarlaaKKQELEE 922
Cdd:TIGR02168 745 LEErIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--------------ALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 923 ILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEeqldeeegarqklqlekvtaeAKIKKMEEEILLLEDQnskflkekk 1002
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLE---------------------EQIEELSEDIESLAAE--------- 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1003 lmedrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELK 1082
Cdd:TIGR02168 861 -----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1083 IQLAKKEEELQAALARGDEEAVQKNNALKV--------IRELQAQIAEL-------QEDLESEKASRNKAEKQKRDLSEE 1147
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALENKIEDdeeearrrLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEA 1015
|
....
gi 2024363113 1148 LEAL 1151
Cdd:TIGR02168 1016 KETL 1019
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1040-1870 |
9.28e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 70.75 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1040 EERLKKEEKT---RQELEKAKRKLDGEttdlQDQIAELQAQIEELKIQLAKKEEELQAA---LARGdEEAVQKNNAlkvI 1113
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAAsdhLNLV-QTALRQQEK---I 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1114 RELQAQIAELQEDLESEKASRNKAEKQKrdlsEELEALKTELEDTLDTTAAQqelrtkreqeVAELKKAIEEEtknheaQ 1193
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQL----AEAEARLEAAEEEVDSLKSQ----------LADYQQALDVQ------Q 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1194 IQEIRQRHA-TALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGE 1272
Cdd:COG3096 410 TRAIQYQQAvQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1273 RLR-----VELAEKANKLQNELDNVSSL---LEEAEKkgikfakdaasLESQLQDTQELLQE-ETRQKLNLSSRIR---- 1339
Cdd:COG3096 490 RSQawqtaRELLRRYRSQQALAQRLQQLraqLAELEQ-----------RLRQQQNAERLLEEfCQRIGQQLDAAEEleel 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1340 --QLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLE----------ENKKKLLKDMESLSQR 1407
Cdd:COG3096 559 laELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1408 LEEKAMAYDKLEKTKNRLQQElddlmvdldhqrqiVSNLEKKQKKFD---QMLAEEKN------------------ISAR 1466
Cdd:COG3096 639 EREATVERDELAARKQALESQ--------------IERLSQPGGAEDprlLALAERLGgvllseiyddvtledapyFSAL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1467 YAEER------DraeaeareketkaLSLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK-- 1532
Cdd:COG3096 705 YGPARhaivvpD-------------LSAVK-------------EQLAGLEDCPEDLYliegdpDSFDDSVFDAEELEDav 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1533 ----SKRTL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDL-----QARDEQ 1586
Cdd:COG3096 759 vvklSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPD 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1587 NEEKKRMLVKQVRELEAELED----ERKQRALAVAAKKKMEMdlkdLEGQIEAANKARDEAikqlrkLQAQMKDYQRELE 1662
Cdd:COG3096 834 PEAELAALRQRRSELERELAQhraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELD 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1663 EARASRDEIFAQSK---ESEKKLKGLEAEILQ---LQEEFAASERARRHAEQERDELADEIANSA----SGKSALLDEKR 1732
Cdd:COG3096 904 AAQEAQAFIQQHGKalaQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENS 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1733 RLEARIAQLEEELEEEQSNmelLNERFRKTTLQVDTLNSELAGERSAAQkseNARQQLerqnKELKAKLQELEGSV---- 1808
Cdd:COG3096 984 DLNEKLRARLEQAEEARRE---AREQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQAdaea 1053
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1809 -------KSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKevfmqveDERRHADQYKE 1870
Cdd:COG3096 1054 eerarirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKA 1115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1635-1853 |
1.03e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1635 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1714
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1715 DEIANSASGKSALLDE----KRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQL 1790
Cdd:COG4942 97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1791 ERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKE 1853
Cdd:COG4942 177 EALLAELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1431 |
1.93e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 69.43 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 847 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNilaEQLQAETELFAEAEEMRARLaakKQELEEILHD 926
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNRL---QQELDDLLVD 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 927 LESrveeeeeRNQILQNEKKKMQG-----------HIQDLEEQLDEEEGARQK----LQLEKVTAEAKIKKME------- 984
Cdd:pfam01576 589 LDH-------QRQLVSNLEKKQKKfdqmlaeekaiSARYAEERDRAEAEAREKetraLSLARALEEALEAKEElertnkq 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 985 -----EEILLLEDQNSKFLKE----KKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEK 1055
Cdd:pfam01576 662 lraemEDLVSSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1056 AKRKLdgettdLQDQIAELQAQIEELKIQLA-------KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLE 1128
Cdd:pfam01576 742 EKRRQ------LVKQVRELEAELEDERKQRAqavaakkKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1129 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQ---RHATAL 1205
Cdd:pfam01576 816 EARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRleaRIAQLE 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1206 EELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQvkaeSEHKRKKLDAQVQELTAKVTEgerlrvelaekankl 1285
Cdd:pfam01576 896 EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKLQE--------------- 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1286 qneldnvsslLEEAEKKgiKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknnlqeqqeeeeearknlekq 1365
Cdd:pfam01576 957 ----------MEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK---------------------- 1002
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1366 mlalqaQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDD 1431
Cdd:pfam01576 1003 ------KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
2.50e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 60.14 E-value: 2.50e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2024363113 31 TAKKLVWIPSERHGFEAASIKEERGDEVLVELaENGKKALVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
894-1267 |
2.87e-11 |
|
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: 68.61 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 894 EQLQAETELFAEAEEMRA-------RLAAKKQELEEILHDLESRVEEEEERNQILQNEK--KKMQGHIQDLEEQLDEEEG 964
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 965 ARQKLQLEKVTAEAKIKKmeEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAE--EEEKAKNLAKLKNKQEMMItdleER 1042
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERirQEEIAMEISRMRELERLQM----ER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1043 LKKEEKTRQELEKAkRKLDGETTDLQDQIAELQAQIEELK--------IQLAKKEEELQAALARGDEEAVQKNNALKVIR 1114
Cdd:pfam17380 388 QQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1115 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEElealktELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQI 1194
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1195 QEIRQRHATALEELSEQLEQAKRFKANLEKNKQglesdnkelacEVKVLQQVKaESEHKRKKLDAQVQELTAK 1267
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----------EREMMRQIV-ESEKARAEYEATTPITTIK 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1068-1312 |
3.26e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1068 QDQIAELQAQIEELKIQLAKKEEELQAALArgdeeavQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEE 1147
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1148 LEALKTELEdtldttaaqqelrtKREQEVAELKKAIEEETKNHEAQI---QEIRQRHATALEELSEQLEQAKRFKANLEK 1224
Cdd:COG4942 92 IAELRAELE--------------AQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1225 NKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGI 1304
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*...
gi 2024363113 1305 KFAKDAAS 1312
Cdd:COG4942 238 AAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
852-1270 |
3.43e-11 |
|
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: 68.51 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 852 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEK-----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 926
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 927 LESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1006
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1007 RIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLA 1086
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1087 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKA--EKQKRDLSEELEALKTELEDTLDTTAA 1164
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1165 QQELRTKREQEVAELKKAIEEETKnheaqiqeirqrhatALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ 1244
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEK---------------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
410 420
....*....|....*....|....*.
gi 2024363113 1245 QVKAESEHKRKKLDAQVQELTAKVTE 1270
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1253-1710 |
3.45e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1253 KRKKLDAQVQELTAKVTEGERLRVELAEkankLQNELDNVSSLLEEAEKKGIKFAKDAASLEsQLQDTQELLQEETRQKL 1332
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1333 NLSSRIRQLEEEKNNLQeqqeeeeeARKNLEKQMLALQAQLAEAKKKVDddlgtiEGLEENKKKLLKDMESLSQRLEEKA 1412
Cdd:COG4717 140 ELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1413 MAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM------------LAEEKNISARYAEERDRAEAEARE 1480
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1481 KETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ--AT 1558
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1559 EDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQVRELEAELEDERK--QRALAVAAKKKMEMDLKDLEGQIEAA 1636
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1637 NKARDEAIKQLRKLQAQMKDY--QRELEEARASRDEIFAQskesekkLKGLEAEILQLQEEFAASERARRHAEQER 1710
Cdd:COG4717 445 EEELEELREELAELEAELEQLeeDGELAELLQELEELKAE-------LRELAEEWAALKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1032-1284 |
3.57e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1032 QEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeavqknnalk 1111
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1112 vIRELQAQIAELQEDLesekasrnkaEKQKRDLSEELEAL-KTELEDTLDTTAAQQELrtKREQEVAELKKAIEEETKNH 1190
Cdd:COG4942 85 -LAELEKEIAELRAEL----------EAQKEELAELLRALyRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1191 EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVte 1270
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI-- 229
|
250
....*....|....
gi 2024363113 1271 gERLRVELAEKANK 1284
Cdd:COG4942 230 -ARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
846-1231 |
3.88e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 846 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 925
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 926 DLESRVEEEEERNQILQNEKKKMQGHIQDLE--EQLDEEEGARQKLQLEKvtAEAKIKKMEEEILLLEDQNSKFLKEKKL 1003
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKcpECGQPVEGSPHVETIEE--DRERVEELEAELEDLEEEVEEVEERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1004 MEDrIAECTSQLAEEEEKAKNLAKLknkqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKI 1083
Cdd:PRK02224 501 AED-LVEAEDRIERLEERREDLEEL-------IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1084 QLAKKEEELQAALARGDeeavqknnALKVIRELQAQIAELQEDLES---EKASRNKAEKQKRDLSEELEALKTELEDTLD 1160
Cdd:PRK02224 573 EVAELNSKLAELKERIE--------SLERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKRELEAEFD 644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 1161 tTAAQQELRTKREQEVAELKKaIEEETKNHEAQIQEIRQRHATALEELsEQLEQAKRFKANLEKNKQGLES 1231
Cdd:PRK02224 645 -EARIEEAREDKERAEEYLEQ-VEEKLDELREERDDLQAEIGAVENEL-EELEELRERREALENRVEALEA 712
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1204-1927 |
4.23e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 68.53 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1204 ALEELSEQLEQAKRFKANLEKNKQGLESDNKELA---CEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAE 1280
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQehqMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1281 KANKLQNELDNVSSLLEeaekkgikfakdaaslesqLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLQEQQEEEEEARK 1360
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMK-------------------LDNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNDLYH 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1361 NLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLS---QRLEEKAMAYDkLEKTKNRLQQELDDLMVDLD 1437
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlqaDRHQEHIRARD-SLIQSLATRLELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1438 HQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1517
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1518 SSKDDVGKNVHELEKSKRTLEQQveemrtqleeledELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKR----- 1592
Cdd:TIGR00606 468 GSSDRILELDQELRKAERELSKA-------------EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttr 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1593 ----MLVKQVRELEAELEDERKQRALAVAA---------------------KKKMEMDLKDLEGQIEAANKARDEAIKQL 1647
Cdd:TIGR00606 535 tqmeMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkqledwlhskskeINQTRDRLAKLNKELASLEQNKNHINNEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1648 RKLQAQMKDYQRELEEARASRDE------IFAQSKESEKKLKGLEAE-------ILQLQEEFAASERARRHAEQERDELA 1714
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCGSQDEesdlerLKEEIEKSSKQRAMLAGAtavysqfITQLTDENQSCCPVCQRVFQTEAELQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1715 DEIANSASGKSALLDEKRRLEARIAQLEEELEE-------EQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSEnar 1787
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE--- 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1788 QQLERQNKELK-AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAA--NKLVRRTEKKLKEVFMQVEDERRH 1864
Cdd:TIGR00606 772 TLLGTIMPEEEsAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKIELNRKL 851
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1865 ADQYKEQMEKANARMKQLKRQleeaEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1927
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSE----KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
852-1270 |
1.00e-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: 67.05 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 852 EELQAKDEELMKVKEKQTKVEAE-------LEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQEL 920
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 921 EEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLK- 999
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1000 ----EKKLMEDR--IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1073
Cdd:pfam05483 491 tahcDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1074 LQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKT 1153
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1154 ELEDTLDTTAAQQELRTKREQ--------------EVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFK 1219
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLY 730
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1220 ANLEKN----KQGLESDNKELACE-VKVLQQVKAESEHKrKKLDAQVQELTAKVTE 1270
Cdd:pfam05483 731 KNKEQEqssaKAALEIELSNIKAElLSLKKQLEIEKEEK-EKLKMEAKENTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1009-1738 |
1.82e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1009 AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERL-----------------KKEEKTRQELEKAKRKL----------D 1061
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYqaasdhlnlvqtalrqqEKIERYQADLEELEERLeeqnevveeaD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1062 GETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1141
Cdd:PRK04863 376 EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTR----AIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1142 RDLSEELEALKTELEDTLDT----TAAQQELRT-------KREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSE 1210
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAhsqfEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1211 Q------LEQA-KRFKANLEKNKQgLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerlrveLAEKAN 1283
Cdd:PRK04863 532 QqraerlLAEFcKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR-------LAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1284 KLQNELDNVSSLLEEAekkGIKFAkDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLE 1363
Cdd:PRK04863 604 AWLAAQDALARLREQS---GEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALA 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1364 KQM--------------------LALQAQLAEAkkKVDDDLGTIEGLEENKKKLLKDM---------------------E 1402
Cdd:PRK04863 680 ERFggvllseiyddvsledapyfSALYGPARHA--IVVPDLSDAAEQLAGLEDCPEDLyliegdpdsfddsvfsveeleK 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1403 SLSQRLEEKAMAYDKL-----------EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEER 1471
Cdd:PRK04863 758 AVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEA 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1472 DRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelekskRTLEQQVEEMRTQLEE 1550
Cdd:PRK04863 838 ELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ETLADRVEEIREQLDE 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1551 LEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELeaeleDERKQRALAVAAKKKMEM 1624
Cdd:PRK04863 906 AEEAkrfVQQHGNALAQLEpivSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TEVVQRRAHFSYEDAAEM 979
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1625 DLKD------LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLkgleaEILQLQEEFAA 1698
Cdd:PRK04863 980 LAKNsdlnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL-----QDLGVPADSGA 1054
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 2024363113 1699 SERARRHaeqeRDELADEIANSASGKSALLDEKRRLEARI 1738
Cdd:PRK04863 1055 EERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1508-1930 |
3.48e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1508 QLRADMEDLMSSKDDVGKnvheLEKSKRTLEQqVEEMRTQLEELEDELQATEDAKLRLEVnmqAMKAQFERDLQARDEQN 1587
Cdd:COG4913 229 ALVEHFDDLERAHEALED----AREQIELLEP-IRELAERYAAARERLAELEYLRAALRL---WFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1588 EEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMD-LKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQrelEEARA 1666
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALG---LPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1667 SRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELe 1746
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1747 eeQSNM----ELL-----NERFR----------KTTLQVDT------------------LNSELAGERSAAQKSENA--- 1786
Cdd:COG4913 457 --EAELpfvgELIevrpeEERWRgaiervlggfALTLLVPPehyaaalrwvnrlhlrgrLVYERVRTGLPDPERPRLdpd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1787 -----------------RQQLERQNKELK-AKLQEL---------EGSVKSKF---------------------KATIST 1818
Cdd:COG4913 535 slagkldfkphpfrawlEAELGRRFDYVCvDSPEELrrhpraitrAGQVKGNGtrhekddrrrirsryvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1819 LEAKIAQLEEQLEQEAKERAAANKLVRRTEK------KLKEVF------MQVEDERRHADQYKEQMEKANARMKQLKRQL 1886
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQErrealqRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAALEEQL 694
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2024363113 1887 EEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
967-1712 |
4.15e-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: 65.13 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 967 QKLQLEKVTAEAKIK----KMEEEILLLEDQNsKFLKEKKLMEDRIaecTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1042
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1043 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALaRGDEEAVQKnnalkVIRELQAQIAE 1122
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKL-KEDHEKIQH-----LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1123 LQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEetknheaqIQEIRQRHA 1202
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1203 TALEELSEQLEQAKRFKANLEKNKQG-LESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEK 1281
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1282 anklqneldnvSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLQEQQEEEEEARKN 1361
Cdd:pfam05483 390 -----------SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1362 LEKQMLALQAQLAEAKKKVDDDLGTIEGLE-ENKKKLLKDMESLSQRleekamayDKLEKTKNRLQQELDDLMVDLDHQR 1440
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1441 QIVSNLEKKQKKfdqMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSK 1520
Cdd:pfam05483 520 EDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1521 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRE 1600
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1601 LEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRdeifaqskesEK 1680
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EI 746
|
730 740 750
....*....|....*....|....*....|..
gi 2024363113 1681 KLKGLEAEILQLQEEFAASERARRHAEQERDE 1712
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1182-1412 |
7.13e-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: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1182 AIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQV 1261
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1262 QELTAKVtegERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1341
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 1342 EEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKA 1412
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1930 |
7.53e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1528 HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnmqamkAQFERDLQARDEQNEEKKRMLVKQVRELEAELED 1607
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1608 ERKQRALAVAAKKKMEMDLKDL----EGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLK 1683
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1684 GLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTT 1763
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1764 LQVDTLNSELAGE--RSAAQKSENARQQLERQNK-ELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAA 1840
Cdd:COG4717 325 LAALGLPPDLSPEelLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1841 NKLVRRTEKKLKEVFMQVEDERRhadqykeqmEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE--GLS 1918
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDE---------EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELL 475
|
410
....*....|..
gi 2024363113 1919 REVSTLKNRLRR 1930
Cdd:COG4717 476 QELEELKAELRE 487
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1039-1216 |
7.93e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.88 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1039 LEERLkkeEKTRQELEKAKRKL------------DGETTDLQDQIAELQAQIEELKIQLAKKE---EELQAALARGDEEA 1103
Cdd:COG3206 180 LEEQL---PELRKELEEAEAALeefrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEarlAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1104 VQKNNAlKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKR-EQEVAELKKA 1182
Cdd:COG3206 257 PELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAlQAREASLQAQ 335
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024363113 1183 IEEETK------NHEAQIQEIRQRHATA---LEELSEQLEQAK 1216
Cdd:COG3206 336 LAQLEArlaelpELEAELRRLEREVEVArelYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
966-1214 |
9.44e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 966 RQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRI--AECTSQLAEEEEKAKNLAKLKNKqemmITDLEERL 1043
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDD----LAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1044 KKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAEL 1123
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1124 QEDLESEKA-SRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQE-----VAELKKAIEEETKNH------- 1190
Cdd:COG4913 775 IDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFvadllsk 854
|
250 260
....*....|....*....|....*
gi 2024363113 1191 -EAQIQEIRQRhataLEELSEQLEQ 1214
Cdd:COG4913 855 lRRAIREIKER----IDPLNDSLKR 875
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1137-1886 |
1.18e-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: 63.83 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1137 AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKREQEVAELKKAIEEEtknheaqiQEIRQRHATALEELSEQLEQA 1215
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQlLTLCTPCMPDTYHERKQVLEKELKHLREAL--------QQTQQSHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1216 KRFKANleknkqglesdnKELACEVKVLQQVKAESEHKRKKLDAQVQelTAKVTEGERLRVELAEKANKLQNELDNVSSL 1295
Cdd:TIGR00618 257 KKQQLL------------KQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1296 LEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQklnlssrirqleEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAE 1375
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI------------RDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1376 AKKKVDDDLGTIEGLEENKKKLlkDMESLSQRLEEKAMAydKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQ 1455
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLA--HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1456 MLAEEKNisaryaEERDRAEAEAREKETKALSLARALEEALEAKEEFER-----QNKQLRADMEDLMSSKDDVGKNVHEL 1530
Cdd:TIGR00618 467 SLKEREQ------QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpnPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1531 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkrmlvkqvreLEAELEDERK 1610
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-----------TEKLSEAEDM 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1611 QRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES-EKKLKGLEAEI 1689
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQSEK 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1690 LQL---QEEFAASERARRHAEQ---ERDELADEIANSASGKSALLDekrrleariAQLEEELEEEQSNMELLNERFRKTT 1763
Cdd:TIGR00618 690 EQLtywKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLA---------AREDALNQSLKELMHQARTVLKART 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1764 LQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELegsvkskfkatistleakiAQLEEQLEQEAKEraaankl 1843
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL-------------------KTLEAEIGQEIPS------- 814
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2024363113 1844 vrrtekKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1886
Cdd:TIGR00618 815 ------DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1217 |
1.44e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 851 EEELQAKDEELMKVKEKQTKVEAELEEMER--KHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 928
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 929 SrveEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRI 1008
Cdd:COG4717 174 E---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1009 -------------------------------------------AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLK- 1044
Cdd:COG4717 251 llliaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1045 KEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEE--LQAALARGDEEAVQKNNALKVIRELQAQIAE 1122
Cdd:COG4717 331 PPDLSPEELLELLDRIE----ELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1123 LQEDLESEKASRNKAEKQkrdlsEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEaqIQEIRQRHA 1202
Cdd:COG4717 407 LEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELE 479
|
410
....*....|....*
gi 2024363113 1203 TALEELSEQLEQAKR 1217
Cdd:COG4717 480 ELKAELRELAEEWAA 494
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1115-1906 |
1.46e-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: 63.53 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1115 ELQAQIAELQEDLESEKASRNKAEKQKRDLSE---ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE 1191
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1192 AQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ-QVKAESEHKRKKlDAQVQELTAkvte 1270
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLAT---- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1271 geRLRVELAEKANKLQNELDNVSSLLEEAEKKGikfAKDAASLESQLQDTQELLQE---ETRQKLNLSSRIRQLEEEKnn 1347
Cdd:TIGR00606 376 --RLELDGFERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTIELKKEI-- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1348 lqeqqeeeeearknLEKQmlalQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSqRLEEKAMAYDKLEKTKNRLQQ 1427
Cdd:TIGR00606 449 --------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1428 ELDdlmvdldhqrqivsnLEKKQKKFDQMLAEEKnisaRYAEERDRAEAEAREKETKalslaraleealeakeefERQNK 1507
Cdd:TIGR00606 510 KAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------------------DEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1508 QLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFERDLQARDEQn 1587
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ- 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1588 eekkrmlvkqvrelEAELEDerkqRALAVAAKKKMEMDLKDLEGQIEAANKardeaikQLRKLQAQMKDYQRELEEARAS 1667
Cdd:TIGR00606 621 --------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1668 R-------DEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:TIGR00606 676 NqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1741 LEEELEEEQSNMELlNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVK----SKFKATI 1816
Cdd:TIGR00606 756 VNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEK 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1817 STLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRA 1896
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPL 914
|
810
....*....|
gi 2024363113 1897 NASRRKLQRE 1906
Cdd:TIGR00606 915 ETFLEKDQQE 924
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1628-1930 |
2.00e-09 |
|
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: 63.16 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1628 DLEGQIEAANKARDEAIKQLrklqAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAE 1707
Cdd:TIGR02169 143 DVTDFISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1708 QERDELADEIANSasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERfrkttlqvdtlnselagersaaqkSENAR 1787
Cdd:TIGR02169 219 EKREYEGYELLKE---KEALERQKEAIERQLASLEEELEKLTEEISELEKR------------------------LEEIE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1788 QQLERQNKELKAKLQELEGSVKSK---FKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRH 1864
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1865 ADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
978-1348 |
2.32e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 978 AKIKKMEEEILLLEDQNSKF---LKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMM---------ITDLEERLKK 1045
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1046 EEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQL-AKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQ 1124
Cdd:COG4717 151 LEERLEELRELEEELE----ELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1125 EDLESEKASRNKAEKQKRDLSEE----LEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQR 1200
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1201 HATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELT-------AKVTEGER 1273
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeAGVEDEEE 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1274 LR--VELAEKANKLQNELDNVSSLLEEAEKKGIKFAK--DAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1348
Cdd:COG4717 387 LRaaLEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1474-1699 |
2.56e-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: 61.32 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1474 AEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1553
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1554 ELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLV----------KQVRELEAELEDERKQRALAVAAKKKME 1623
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1624 MDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKGLEAEILQLQEEFAAS 1699
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPAA 246
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1508-1840 |
3.00e-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: 61.24 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1508 QLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQARDEQN 1587
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1588 EEKK---RMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1664
Cdd:pfam19220 107 EELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1665 RASRDEIFAQSKESEKKLKGLEAEILQLQ----EEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1741 LEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQ-----------NKELKAKLQELEGSVK 1809
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraeleeraemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2024363113 1810 S-------------KFKATISTLEAKIAQLEEQLEQEAKERAAA 1840
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1685-1927 |
3.56e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1685 LEAEILQLQEEFAASERARRHAEQERDELAdeiansasgksaLLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTtl 1764
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1765 QVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLV 1844
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1845 RRTEkklkevfMQVEDErrhADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateanegLSREVSTL 1924
Cdd:COG4913 369 AALG-------LPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIASL 431
|
...
gi 2024363113 1925 KNR 1927
Cdd:COG4913 432 ERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1504-1725 |
5.01e-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: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1504 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQAR 1583
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1584 DEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEE 1663
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 1664 ARASRDEIFAQskeSEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKS 1725
Cdd:COG4942 193 LKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
846-1377 |
5.08e-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: 61.66 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 846 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELE 921
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 922 EILHDLESRVEEEEernQILQNEKKKMQGHIQDLEEQLDEEEgaRQKLQLEKVTAEAKIKKME-EEILLLEDQNSKFLKE 1000
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQ--KKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1001 KKLMEdRIAEctsqlaEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEE 1080
Cdd:pfam05483 424 KKQFE-KIAE------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1081 LKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQedlESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1160
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1161 TTAAQQELRTKREQEVAELKKA---IEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1237
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1238 CEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKlqneldNVSSLLEEAEKKGIKFAKDAASLESQL 1317
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH------KIAEMVALMEKHKHQYDKIIEERDSEL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1318 QDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAK 1377
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
941-1165 |
5.87e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 941 LQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEE 1020
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1021 KaknLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGD 1100
Cdd:COG4942 105 E---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1101 EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1165
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
840-1482 |
6.19e-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: 61.60 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 840 KVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERK---HQQLLEEKNILAEQLQAETELFAEAEEMRAR---- 912
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhht 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 913 --------LAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKME 984
Cdd:TIGR00606 532 ttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 985 EEILLLEDQNSKFlkekklmEDRIAECTSQLAEE----------EEKAKNLAKLKNKQEMMITDLEERLKKEEK---TRQ 1051
Cdd:TIGR00606 612 NELESKEEQLSSY-------EDKLFDVCGSQDEEsdlerlkeeiEKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQ 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1052 ELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEK 1131
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1132 ASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR---TKREQEVAELKKAIEEETKNheaQIQEIRQRHATALEEL 1208
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKdveRKIAQQAAKLQGSDLDRTVQ---QVNQEKQEKQHELDTV 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1209 SEQLEQAKRFKANLEKNKQGLESDNKELACE---VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKL 1285
Cdd:TIGR00606 842 VSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1286 QNELDNVSSLLEEAEKKGikfakdaaslESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlqeqqeeeeeaRKNLEKQ 1365
Cdd:TIGR00606 922 QQEKEELISSKETSNKKA----------QDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY-------------LKQKETE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1366 MLALQAQLAEA---KKKVDDDLGTIEG---LEENKKKLLKDMESLSQRLEEkamaYDKLEKTKNRLQQELDDLMVdldhq 1439
Cdd:TIGR00606 979 LNTVNAQLEECekhQEKINEDMRLMRQdidTQKIQERWLQDNLTLRKRENE----LKEVEEELKQHLKEMGQMQV----- 1049
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2024363113 1440 RQIVSNLEKKQKKFDQMLAEEKNISAR---YAEERDRAEAEAREKE 1482
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVLALGRqkgYEKEIKHFKKELREPQ 1095
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1025-1468 |
6.98e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1025 LAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTD---LQDQIAELQAQIEELKIQLAKKEEELQAAlargdE 1101
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKL-----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1102 EAVQKNNALKVIRELQAQIAELQEDLESEKAsrnkAEKQKRDLSEELEALKTELEdtldttaaqqELRTKREQEVAELKK 1181
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELA----------ELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1182 AIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKE--------------LACEVKVLQQVK 1247
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1248 AESEHKRKKLDAQVQELTA----------KVTEGERLRVELAEKANKLQNEldNVSSLLEEAEKKGIKFAKDAASLESQL 1317
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLAllflllarekASLGKEAEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1318 QDTQELLQEetRQKLNLSSRIRQLEEEKNNLQEQ-----------QEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGT 1386
Cdd:COG4717 347 EELQELLRE--AEELEEELQLEELEQEIAALLAEagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1387 iegleENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDldhqrqivSNLEKKQKKFDQMLAEEKNISAR 1466
Cdd:COG4717 425 -----LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--------GELAELLQELEELKAELRELAEE 491
|
..
gi 2024363113 1467 YA 1468
Cdd:COG4717 492 WA 493
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1040-1312 |
7.09e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1040 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeavqknnalkvIRELQAQ 1119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE--------------IAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1120 IAELQEDLesekASRNKAEKQKRDLSEELEALK--TELEDTLDTTAAqqelrtkreqevaelkkaieeetknheaqIQEI 1197
Cdd:COG3883 81 IEERREEL----GERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-----------------------------LSKI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1198 RQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVE 1277
Cdd:COG3883 128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250 260 270
....*....|....*....|....*....|....*
gi 2024363113 1278 LAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAAS 1312
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1109-1368 |
8.72e-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: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1109 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRtKREQEVAELKKAIEEetk 1188
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------ALARRIR-ALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1189 nHEAQIQEIRQRHATALEELSEQLEQAKRFkANLEKNKQGLESDNKELAceVKVLQQVKAESEHKRKKLDAQVQELTakv 1268
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDA--VRRLQYLKYLAPARREQAEELRADLA--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1269 tegerlrvELAEKANKLQNELDNVSSLLEEAEKKgikfakdAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1348
Cdd:COG4942 161 --------ELAALRAELEAERAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260
....*....|....*....|
gi 2024363113 1349 QEQQEEEEEARKNLEKQMLA 1368
Cdd:COG4942 226 EALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1630-1853 |
1.03e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1630 EGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFaaserarrhaEQE 1709
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1710 RDELADEIA------NSASGKSALLDekrrleariAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAqks 1783
Cdd:COG3883 85 REELGERARalyrsgGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1784 ENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKE 1853
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1366-1853 |
3.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1366 MLALQAQLAEAKKKVDDDLGTIEG-LEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1444
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1445 NLEKKQKKFDQMLAEEK------NISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1518
Cdd:COG4717 120 KLEKLLQLLPLYQELEAleaelaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1519 SKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRM----- 1593
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1594 ------LVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARAS 1667
Cdd:COG4717 280 flvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1668 RDEIfaqskesekKLKGLEAEILQLQEEFAASERARRHAEQERDELADEiansasgksaLLDEKRRLEARIAQLEEELEE 1747
Cdd:COG4717 360 EEEL---------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE----------LKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1748 EQSnmellnerfrktTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvkskfkATISTLEAKIAQLE 1827
Cdd:COG4717 421 LLE------------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED------GELAELLQELEELK 482
|
490 500
....*....|....*....|....*....
gi 2024363113 1828 EQLEQEAKERAAAN---KLVRRTEKKLKE 1853
Cdd:COG4717 483 AELRELAEEWAALKlalELLEEAREEYRE 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
965-1344 |
3.52e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 965 ARQKLQLEKVTAEAKIKKMEEEILLLED--QNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1042
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1043 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGD--EEAVQKNNALKVIRELQ--A 1118
Cdd:COG4717 176 QEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARllL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1119 QIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR 1198
Cdd:COG4717 253 LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1199 QRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEvKVLQQVKAESEHKRKKLDAQVQELtakvtegERLRVEL 1278
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEY-------QELKEEL 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1279 AEKANKLQNELDNVSSLLEEAEKKGIKfaKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEE 1344
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1092-1330 |
3.78e-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: 57.85 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1092 LQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqqelrtk 1171
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1172 rEQEVAELKKAIEEETKNHEAQIQEIRQRhATALEELSEQLEQAKRFKAN----LEKNKQGLESDNKELACEVKVLQQVK 1247
Cdd:COG4942 82 -EAELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1248 AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1327
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
...
gi 2024363113 1328 TRQ 1330
Cdd:COG4942 240 AER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1107 |
4.13e-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: 57.47 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 887 EEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-- 964
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 965 ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM---------EDRIAECTSQLAEEEEKAKNLAKLKNKQEMM 1035
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 1036 ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKN 1107
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1080 |
6.19e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 850 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELEEILH 925
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 926 DLESRVEEEEERNQILQneKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAE--AKIKKMEEEILLLEDQNSKFLKEKKL 1003
Cdd:COG4942 98 ELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1004 MEdriaectSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRkldgettDLQDQIAELQAQIEE 1080
Cdd:COG4942 176 LE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE-------ELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1485-1726 |
6.35e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1485 ALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1564
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1565 LEVNMQAMKAQferdLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAI 1644
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1645 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGK 1724
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 2024363113 1725 SA 1726
Cdd:COG4942 244 PA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1067-1853 |
6.53e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1067 LQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNAL----KVIRELQAQIAELQEDLESEKASRNKAEKQKR 1142
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLqenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1143 DLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIqeirqrhaTALEELSEQLEQAK-RFKAN 1221
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlEMHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1222 LEKNKQGLESDNKELACEVKvlqqvkaESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1301
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEIN-------DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1302 KGIKFAKDAASLESQLQ---DTQELLQEETRQKlnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1378
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQrsmSTQKALEEDLQIA---TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1379 KVDddlgtiEGLEENKKKLlkdmESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1458
Cdd:pfam05483 367 TEQ------QRLEKNEDQL----KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1459 EEKNISARYaeerdraeaEAREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLE 1538
Cdd:pfam05483 437 KEQELIFLL---------QAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1539 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfERDLQARDEQnEEKKRMLVKQVRELEAELEderkqralavaa 1618
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDEL-ESVREEFIQKGDEVKCKLD------------ 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1619 kkKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAA 1698
Cdd:pfam05483 570 --KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1699 serARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLeeeleeeqsnMELLNERFRKTTLQVDTLNSELAGERS 1778
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----------VKLQKEIDKRCQHKIAEMVALMEKHKH 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1779 AAQKSenarqqLERQNKEL---KAKLQElEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKE 1853
Cdd:pfam05483 715 QYDKI------IEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1385-1930 |
7.23e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1385 GTIEGLEENKKKLlkdmESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLdhqRQIVSNLEKKQKKFDQMLAEEKNiS 1464
Cdd:pfam12128 241 PEFTKLQQEFNTL----ESAELRLSHLHFGYKSDETLIASRQEERQETSAEL---NQLLRTLDDQWKEKRDELNGELS-A 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1465 ARYAEERDRAEAEAREKETKALSLARALEEALEAKeeferQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQV-EE 1543
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQE-----QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1544 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQardEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAkkkmE 1623
Cdd:pfam12128 388 NNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT----P 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1624 MDLKDLEGQIEAANKARDEaikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEE-FAAS--- 1699
Cdd:pfam12128 461 ELLLQLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAgtl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1700 -ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR-----------RLEARIAQLEEELEEE 1748
Cdd:pfam12128 537 lHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpewaaseeELRERLDKAEEALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1749 QSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEE 1828
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1829 QLeQEAKERAAANKLVRRTEK--KLKEVfmqVEDERRHADQYKEQMEkanARMKQLKRQLEEAEEEATRANASRrklqre 1906
Cdd:pfam12128 697 KH-QAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIA---ARRSGAKAELKALETWYKRDLASL------ 763
|
570 580
....*....|....*....|....
gi 2024363113 1907 lDDATEANEGLSREVSTLKNRLRR 1930
Cdd:pfam12128 764 -GVDPDVIAKLKREIRTLERKIER 786
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1067-1849 |
8.28e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.52 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1067 LQDQIAELQAQIEELKIQLAKKEEELQAALargdeeavqknNALKVIrelqaqiaeLQEDLESEKASRNKAEKQKRDLSE 1146
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTF---------WSPELKKERALRKEEAARISVLKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1147 ELEALKTELED-TLDTTAAQQELRTKRE------------QEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLE 1213
Cdd:pfam10174 61 QYRVTQEENQHlQLTIQALQDELRAQRDlnqllqqdfttsPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1214 QakrFKANLEKNKQGLESDNKELACEVKVLQ-----QVKAESEHKRKK----LDAQVQELTA----KVTEGERLRVELAE 1280
Cdd:pfam10174 141 E---MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHLEVlldqKEKENIHLREELHR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1281 KaNKLQNELDNVSSLLEEAEKKGIKFakdaASLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKNNLQEQQEEEE 1356
Cdd:pfam10174 218 R-NQLQPDPAKTKALQTVIEMKDTKI----SSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKID 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1357 EARKNLEK---QMLALQAQLAEAKKKVDDDLGTIEGLEEN-------KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQ 1426
Cdd:pfam10174 293 QLKQELSKkesELLALQTKLETLTNQNSDCKQHIEVLKESltakeqrAAILQTEVDALRLRLEEKESFLNKKTKQLQDLT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1427 QELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLaraleealeakeef 1502
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL-------------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1503 erqnkqlrADMEDLMSSKDDVGKNV-HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQ 1581
Cdd:pfam10174 439 --------TTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----A 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1582 ARDEQNEEKKRMLVKQvreLEAELEDERKQRALAVAAKKKMEmdlkdlegQIEAANKARDEAIKQLRKLQAQMKDYQREL 1661
Cdd:pfam10174 506 SSLASSGLKKDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1662 EEARASRDEIFAQSKESE-------KKLKGLEAEILQLQEEFAASERARRHAEQERDEladeiansasgKSALLDEkrrl 1734
Cdd:pfam10174 575 GKAQAEVERLLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE---- 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1735 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAgerSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKA 1814
Cdd:pfam10174 640 EARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLS---STQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLA 716
|
810 820 830
....*....|....*....|....*....|....*
gi 2024363113 1815 TISTLEAKIAQLEeqLEQEAKERAAANKLVRRTEK 1849
Cdd:pfam10174 717 AISEKDANIALLE--LSSSKKKKTQEEVMALKREK 749
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1017-1216 |
9.77e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1017 EEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1096
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1097 ------------------ARGDEEAVQKNNAL--------KVIRELQAQIAEL---QEDLESEKASRNKAEKQKRDLSEE 1147
Cdd:COG3883 93 ralyrsggsvsyldvllgSESFSDFLDRLSALskiadadaDLLEELKADKAELeakKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1148 LEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAK 1216
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1571-1738 |
1.02e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1571 AMKAQFER--DLQARD---EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIK 1645
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1646 QLRKLQA--QMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAsg 1723
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-- 158
|
170
....*....|....*
gi 2024363113 1724 kSALLDEKRRLEARI 1738
Cdd:COG1579 159 -EELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1693-1931 |
1.04e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1693 QEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSE 1772
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1773 LAGERSAAQKSENARQQLERQNKeLKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLK 1852
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1853 EVFMQVEDERRhadQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRG 1931
Cdd:COG4942 178 ALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
852-1842 |
1.23e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.37 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 852 EELQAK-DEELMKVKEKQTK-VEAELEEMERKHQQLLEekNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 929
Cdd:TIGR01612 699 DDLKSKiDKEYDKIQNMETAtVELHLSNIENKKNELLD--IIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 930 RveeeeernqilQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIA 1009
Cdd:TIGR01612 777 E-----------KDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1010 ECTSQLAEEEEKAKNLAklkNKQEMMITDLEERLKKEEKTRQeLEKAKRKLDgettDLQDQIAELQAQIEE--LKIQLAK 1087
Cdd:TIGR01612 846 NKVDKFINFENNCKEKI---DSEHEQFAELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1088 KEEELqAALARGDEEAVQK--NNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELedTLDTTAA- 1164
Cdd:TIGR01612 918 KVDEY-IKICENTKESIEKfhNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAk 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1165 -----------QQELRTKRE----QEVAELKKA---IEEETKNHEAQIQEIRQRHATALEELSEQLEqaKRFKANLEK-N 1225
Cdd:TIGR01612 995 nnelikyfndlKANLGKNKEnmlyHQFDEKEKAtndIEQKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlN 1072
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1226 KQGLESDNKELACEVKVLQQVK------------AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVS 1293
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI 1152
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1294 SLLEEAEKKGIkFAKDAASLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLQEQQEEEEEARKNLEKQML 1367
Cdd:TIGR01612 1153 NDLEDVADKAI-SNDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGKLFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1368 AlqaQLAEAKKKVDDDLGTIEGLEENkkklLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDD----LMVDLDHQRQIv 1443
Cdd:TIGR01612 1229 E---KIDEEKKKSEHMIKAMEAYIED----LDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI- 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1444 SNLEKKQKKFDQMLAEEKNIS------ARYAEERDRAEAEAREKETKALSLARALEEALEakeeferqnKQLRADMEDLM 1517
Cdd:TIGR01612 1301 SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDINLYLNEIANIYNILKLNKI---------KKIIDEVKEYT 1371
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1518 SSKDDVGKNVH-ELEKSKrTLEQQVEEmRTQLEELEDELQATEDAK---------LRLEVNMQAMKAQFERDLQARDEQN 1587
Cdd:TIGR01612 1372 KEIEENNKNIKdELDKSE-KLIKKIKD-DINLEECKSKIESTLDDKdidecikkiKELKNHILSEESNIDTYFKNADENN 1449
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1588 EEKKrMLVKQVreleaELEDERKQRALAVA---AKKKMEMDLKDLEGQIEAANKARDEA---IKQLRKLQAQMKDYQRE- 1660
Cdd:TIGR01612 1450 ENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDv 1523
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1661 --------------------------LEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1714
Cdd:TIGR01612 1524 tellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE 1603
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1715 D------EIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnerfrkTTLQVDTLNSELAGERSAAQKSENARQ 1788
Cdd:TIGR01612 1604 NfenkflKISDIKKKINDCLKETESIEKKI-----------------------SSFSIDSQDTELKENGDNLNSLQEFLE 1660
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1789 QLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANK 1842
Cdd:TIGR01612 1661 SLKDQKKNIEDKKKELD-ELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1460-1912 |
1.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1460 EKNISARYAEERDRAEAEAREKETKALslARALEEALEAKEEFERQNKQLRADMEDLmsskdDVGKNVHELEKSKRTLEQ 1539
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1540 QVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAV 1616
Cdd:COG4717 140 ELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1617 AAKKKMEMDLKDLEGQIEAANKArdEAIKQLRKLQAQM-------------KDYQRELEEARASRDEIFAQSKESEKKLK 1683
Cdd:COG4717 220 EELEELEEELEQLENELEAAALE--ERLKEARLLLLIAaallallglggslLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1684 gleAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTT 1763
Cdd:COG4717 298 ---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1764 LQVDTLNSELAGERSAAQKSEnARQQLERQNKELKAKLQELEGSVKSKFKA-TISTLEAKIAQLEEQLEQEAKERAAANK 1842
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1843 LVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1912
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1548-1930 |
1.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1548 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQVRELEAELEDERKQRALAVAAKKKMEM--D 1625
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKllQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1626 LKDLEGQIEAANKARDEAIKQLRKLQAQMKDY---QRELEEARASRDEIFAQ--------SKESEKKLKGLEAEILQLQE 1694
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1695 EFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARI------------AQLEEELEEEQSNMELLNERFRKT 1762
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1763 TLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERAAANK 1842
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1843 LVRRTEKK--LKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEANEGLS 1918
Cdd:COG4717 366 EELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELE 445
|
410
....*....|..
gi 2024363113 1919 REVSTLKNRLRR 1930
Cdd:COG4717 446 EELEELREELAE 457
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1072-1372 |
1.32e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.84 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1072 AELQAQIEELKiqlakKEEELQAalargDEEAVQKN--NALKVIrelqAQIAELQEDLESEKASRNKAEKQKRDLSEELE 1149
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQDleQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1150 ALKTELEDTLDTTAAQQELRTkREQEVAELKKAIEEETKN-HEAQIQEIRQRHA-----TALEELSEQLEQAKRFKANLE 1223
Cdd:PRK11281 105 ALKDDNDEETRETLSTLSLRQ-LESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQperaqAALYANSQRLQQIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1224 KNKQGLESDNK-ELACEvkvLQQVKAESEHKRKKLDA--QVQELtakvteGERLRVELAEKANKLQNELdnvsSLLEEA- 1299
Cdd:PRK11281 184 VGGKALRPSQRvLLQAE---QALLNAQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL----QLLQEAi 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1300 -EKKGIKFAKDAASLESQlQDTQE-----LLQEETRQKLNLSSRIRQLEEEKNNLQeqqeeeeeaRKNLE-KQML--ALQ 1370
Cdd:PRK11281 251 nSKRLTLSEKTVQEAQSQ-DEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLT---------QQNLRvKNWLdrLTQ 320
|
..
gi 2024363113 1371 AQ 1372
Cdd:PRK11281 321 SE 322
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1590-1881 |
1.37e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1590 KKRMLVKQVRE---LEAELEDERKQRALAVA---AKKKMEMDLKDlegQIEAANKARDEAIKQLRKLQAQMKDYQRELEE 1663
Cdd:COG3206 124 RKNLTVEPVKGsnvIEISYTSPDPELAAAVAnalAEAYLEQNLEL---RREEARKALEFLEEQLPELRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1664 ARASRDEIF--AQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN--SASGKSALLDEKRRLEARIA 1739
Cdd:COG3206 201 FRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1740 QleeeleeeqsnmelLNERFRKTTLQVdtlnselagersaaqksenarQQLERQNKELKAKLQELEGSVKSKFKATISTL 1819
Cdd:COG3206 281 E--------------LSARYTPNHPDV---------------------IALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 1820 EAKIAQLEEQLEQEAKERAAANKLvrrtEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQ 1881
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1277-1886 |
1.54e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1277 ELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEE 1356
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1357 EARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDL 1436
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1437 DHQRQIVSNLEKKQKKFDQMLAEeknisaryaeerdraeaeareketkalslaraleealeakeeferqnkqlradmedl 1516
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQ--------------------------------------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1517 msskddvgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVK 1596
Cdd:TIGR04523 220 ----------ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS-EKQKELEQNNKKIKELEK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1597 QVRELEAELEDERKQRALAVAakKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1676
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1677 ESEKKLKGLEAEilqlqeefaaserarrhaeqerdeladeiansasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1756
Cdd:TIGR04523 367 EKQNEIEKLKKE-----------------------------------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1757 ERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKE 1836
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-NTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1837 RAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1886
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1195-1432 |
1.57e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1195 QEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVtegERL 1274
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1275 RVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEetrqklnLSSRIRQLEEEKNNLQEQQEE 1354
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA-------RREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1355 EEEARKNLEKQMLALQAQLAEakkkvdddlgtiegLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1432
Cdd:COG4942 169 LEAERAELEALLAELEEERAA--------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1277-1924 |
1.78e-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: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1277 ELAEKANKLQNELDNVSSLleEAEKKGIKFA-KDAASLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNNLQEQQEEE 1355
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESA--ELRLSHLHFGyKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1356 EEARKNLEKQMLALQAQlaeAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQelddlMVD 1435
Cdd:pfam12128 314 DAAVAKDRSELEALEDQ---HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRS-----KIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1436 LDHQRQIVSNLEKKQKKFD----QMLAEEKNISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQ 1508
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREardrQLAVAEDDLQALESELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1509 LRADMEDLMSSKDDVGKNVHELEKSKRTL-----------------EQQVEEMRTQLEELEDELQA---TEDAKLRLEVN 1568
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasealrqaSRRLEERQSALDELELQLFPqagTLLHFLRKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1569 M--QAMKAQFERDLQARDEQNEEKKRMLVKQVRELEA-ELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIK 1645
Cdd:pfam12128 546 DweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1646 QLRKLQAQMKDYQRELEEARASrdeiFAQSKESEKKLKG-LEAEILQLQEefaASERARRHAEQERDELADEIANSASGK 1724
Cdd:pfam12128 626 QLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKH 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1725 SALLDEKRR--LEARIAQLeeeleeeqsnmELLNERFRKTTLQVDTLNSELAGERSAAQKSENArqqLERQNK-ELKAKL 1801
Cdd:pfam12128 699 QAWLEEQKEqkREARTEKQ-----------AYWQVVEGALDAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASLG 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1802 QELEgsvkskfkaTISTLEAKIAQLEEQLEQEAKERAAanklVRRTEKKLKEVFMQvederrHADQYKEQMEKANARMK- 1880
Cdd:pfam12128 765 VDPD---------VIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLATQLSNIERAISe 825
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2024363113 1881 ---QLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTL 1924
Cdd:pfam12128 826 lqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1358-1740 |
2.05e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1358 ARKNLEKQMLALQAQLAEAKKKvdddlgtiegleenkkkllkdMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL----- 1432
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQ---------------------LAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhln 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1433 --MVDLDHQRQI---VSNLEKKQKKfdqmLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNK 1507
Cdd:PRK04863 339 lvQTALRQQEKIeryQADLEELEER----LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1508 QLRADMEDLMSSKDDVGKNVHELEKskrtLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQARDEQN 1587
Cdd:PRK04863 415 QYQQAVQALERAKQLCGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1588 EEKKRMLVKQV-RELeaeLEDERKQRALAVAAkKKMEMDLKDLEGQIE---AANKARDEAIKQLRK---LQAQMKDYQRE 1660
Cdd:PRK04863 487 GEVSRSEAWDVaREL---LRRLREQRHLAEQL-QQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKnldDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1661 LEEARASRDEIFAQSKES----EKKLKGLEAEILQL----QEEFAASERARRHAEQERDELADE------IANSASGKSA 1726
Cdd:PRK04863 563 LEARLESLSESVSEARERrmalRQQLEQLQARIQRLaaraPAWLAAQDALARLREQSGEEFEDSqdvteyMQQLLERERE 642
|
410
....*....|....
gi 2024363113 1727 LLDEKRRLEARIAQ 1740
Cdd:PRK04863 643 LTVERDELAARKQA 656
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1597-1928 |
2.51e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1597 QVRELEAELEDerKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYqrelEEARASRDEIFAQSK 1676
Cdd:PRK02224 188 SLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEH----EERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1677 ESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1756
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1757 ERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkFKATISTLEAKIAQLEEQLEQEAKE 1836
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE-LRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1837 RAAANKLVRRTEKKLKEVFMQVEDERR------------------HAD---QYKEQMEKANARMKQLKRQLEEAEEEATR 1895
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegspHVEtieEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350
....*....|....*....|....*....|...
gi 2024363113 1896 ANASrRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:PRK02224 501 AEDL-VEAEDRIERLEERREDLEELIAERRETI 532
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1205-1719 |
3.54e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1205 LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1284
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1285 LQNELDNVSSlLEEAEKKGIKFAKDAASLEsqlqdtqellQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEk 1364
Cdd:PRK01156 265 LSMELEKNNY-YKELEERHMKIINDPVYKN----------RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1365 QMLALQAQLAEAKKKVDD---DLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKL-----------EKTKNRLQQELD 1430
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiseilkiqEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1431 DLMVDLDHQRQIVSNLEKKQKKFDQMLAE-------------------------EKNISARYAEERDRAEAEAREKETKA 1485
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDElsrnmemlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1486 LSLaraleeALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQAT--EDAKL 1563
Cdd:PRK01156 493 KDI------DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLklEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1564 RLEVNMQAMKAQFERDLQARDEQNEEKKRML---VKQVRELEAELEDERKQRALAVaakKKMEMDLKDLEGQIEAAnKAR 1640
Cdd:PRK01156 566 KRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKSYIDKSI---REIENEANNLNNKYNEI-QEN 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1641 DEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN 1719
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1020-1155 |
3.88e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.22 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1020 EKAK-NLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLakkEEELQAALAR 1098
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1099 GDEEAVQknnalkVIRELQAQIAELQEDLESEKASrnkaEKQKRdLSEELEALKTEL 1155
Cdd:PRK00409 582 AKKEADE------IIKELRQLQKGGYASVKAHELI----EARKR-LNKANEKKEKKK 627
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
979-1341 |
4.00e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.86 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 979 KIKKMEEEILLLEDQNSK--FLKEKKLMEdriaECTSQLAEEEEKAKNlaklknkqemMITDLEERLKKEEKTRQELEKA 1056
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrFKKAKKALD----EIEELLDDIEEDIKQ----------ILEELDELLESEEKNREEVEEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1057 KRKLDGETTDLQDQ-------IAELQAQIEELKIQLAKKEEELQAalarGDEEAvqknnALKVIRELQAQIAELQEDLES 1129
Cdd:pfam06160 127 KDKYRELRKTLLANrfsygpaIDELEKQLAEIEEEFSQFEELTES----GDYLE-----AREVLEKLEEETDALEELMED 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1130 EKASRNKAEKQKRDLSEELEALKTELED---TLDTTAAQQELRTKREQeVAELKKAIEE-ETKNHEAQIQEIRQRhataL 1205
Cdd:pfam06160 198 IPPLYEELKTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEIEER----I 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1206 EELSEQLEQAKRFKANLEKNKQGLESD-------NKELACEVKVLQQ---VKAESEHKRKKLDAQVQELTAKVtegERLR 1275
Cdd:pfam06160 273 DQLYDLLEKEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKRY---DEIV 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1276 VELAEKA---NKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1341
Cdd:pfam06160 350 ERLEEKEvaySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1117-1336 |
4.72e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1117 QAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQE 1196
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1197 IRQ--RHATALEEL--SEQLEQakrFKANLEKNKQGLESDNKELacevKVLQQVKAESEHKRKKLDAQVQELTAKVTEGE 1272
Cdd:COG3883 95 LYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1273 RLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSS 1336
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1359-1621 |
5.38e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1359 RKNLEKQMLALQAQLAEAKKKvdddlgtiegleenKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDH 1438
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1439 QRQivsNLEKKQKKFDQMLAEeknisaryaeerdrAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1518
Cdd:COG4942 95 LRA---ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1519 SKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQV 1598
Cdd:COG4942 158 DLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALI 229
|
250 260
....*....|....*....|...
gi 2024363113 1599 RELEAELEDERKQRALAVAAKKK 1621
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1060-1237 |
5.95e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1060 LDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAV--QKNNALKVIRELQAQIAELQEDLESEKASRNKA 1137
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1138 EKQKRDL---------SEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEetknheaQIQEIRQRHATALEEL 1208
Cdd:COG3206 246 RAQLGSGpdalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA-------LRAQLQQEAQRILASL 318
|
170 180
....*....|....*....|....*....
gi 2024363113 1209 SEQLEQAKRFKANLEKNKQGLESDNKELA 1237
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELP 347
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
991-1233 |
6.27e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.55 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 991 EDQNSKFLKEKKLMEdRIAECTSQLAEEEEKAKNLAKLKNKQEmmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1070
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELKIqLAKKEEELQaaLARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNK-------AEKQKRD 1143
Cdd:PRK05771 116 IKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1144 LSEELEALKTELEDTLDTTAAQQELRTKrEQEVAELKKAIEEEtknhEAQIQEIRQRHATALEELSEQLEQAkRFKANLE 1223
Cdd:PRK05771 193 VEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIE-LERAEAL 266
|
250
....*....|
gi 2024363113 1224 KNkqGLESDN 1233
Cdd:PRK05771 267 SK--FLKTDK 274
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1292-1865 |
6.66e-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: 54.36 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1292 VSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQA 1371
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1372 QLAEAKKKVDDdlgtiegLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1451
Cdd:pfam05557 91 KLNEKESQLAD-------AREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1452 KFDQMLAEEKNISARYAEERDRAEaEAREKETKALSLARaleealeakeeFERQNKQLRADMEDLMSSKDDVGKNVHELE 1531
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSE-IVKNSKSELARIPE-----------LEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1532 KSKRTLEQQvEEMRTQLEELEDELQATEdAKLRLEVNMQAMKAQFER---DLQARDEQNEEKKRMLVKQVRELEAELEDE 1608
Cdd:pfam05557 232 DLKRKLERE-EKYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1609 RKQRalavaakKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQSKESEKKLKGL 1685
Cdd:pfam05557 310 EKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1686 E--AEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFR--- 1760
Cdd:pfam05557 383 EeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRlre 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1761 -KTTLQVDTLNSELAGERSAA-----QKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEA 1834
Cdd:pfam05557 463 qKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNF 542
|
570 580 590
....*....|....*....|....*....|....
gi 2024363113 1835 KERAAANKLVRRTEKK---LKEVFMQVEDERRHA 1865
Cdd:pfam05557 543 KEVLDLRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1750 |
7.62e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1538 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVA 1617
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1618 AKKKMEMDLKDLEGQIEAANKArdEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFA 1697
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1698 ASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1750
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1520-1740 |
8.58e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1520 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQfERDLQARDEQNEEKKRMLVKQVR 1599
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1600 ELEAELEDERKQRALAVAAKKKMEMD--LKDLEGQIEAANKARDEAIK-------QLRKLQAQMKDYQREL-EEARASRD 1669
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1670 EIFAQSKESEKKLKGLEAEILQLQEEFAA-SERARRHAEQERD-ELADEIANSasgksaLLdeKRRLEARIAQ 1740
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1465-1837 |
9.31e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.75 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1465 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1544
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1545 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMlvkQVRELEAELEDERKQRALAVAAKKKMEM 1624
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNSLAQR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1625 DLKDLEGQIEAANkardeaiKQLRKLQAQMKDYQRE--LEEARASRDEIFAqskeSEKKLKGLEAEIlqlqeEFAASERA 1702
Cdd:pfam07888 205 DTQVLQLQDTITT-------LTQKLTTAHRKEAENEalLEELRSLQERLNA----SERKVEGLGEEL-----SSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1703 RRHAEQERDEL-ADEIANSASGKSALLDEKRrleariAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQ 1781
Cdd:pfam07888 269 RTQAELHQARLqAAQLTLQLADASLALREGR------ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1782 KSE---------NARQQLE--RQNKELKAKLQELEGSvKSKFKATISTLEAKIAQLEEQLEQEAKER 1837
Cdd:pfam07888 343 KLEvelgrekdcNRVQLSEsrRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1529-1689 |
9.65e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1529 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlqardeqneEKKRMLVKQVRELEA---EL 1605
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---------EEQLGNVRNNKEYEAlqkEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1606 EDERKQRAlavaakkkmemdlkDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGL 1685
Cdd:COG1579 99 ESLKRRIS--------------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....
gi 2024363113 1686 EAEI 1689
Cdd:COG1579 165 REEL 168
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1365-1930 |
1.11e-06 |
|
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: 53.90 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1365 QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLlKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMV---------- 1434
Cdd:TIGR00606 225 QITSKEAQLESSREIVKSYENELDPLKNRLKEI-EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEkvfqgtdeql 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1435 -DLDHQRQiVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKEtkaLSLARALEEALEAKEEFERQNKQLRADM 1513
Cdd:TIGR00606 304 nDLYHNHQ-RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR---LQLQADRHQEHIRARDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1514 EDLMSSKDDVG--KNVHELEKskRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlQARDEQNEEKK 1591
Cdd:TIGR00606 380 DGFERGPFSERqiKNFHTLVI--ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK-KEILEKKQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1592 RMLVKQVRELEAELEDERKQRAlavaAKKKMEMDLKDLEgqieaankaRDEAIKQLRKLQAQMKDYQRELEEARASRDEI 1671
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQ----ELRKAERELSKAE---------KNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1672 FAQSKESEKKLKGLEaeiLQLQEEFAASERARRHAEQERDELADEIANSASGKS------ALLDEKRRLEARIAQLEEEL 1745
Cdd:TIGR00606 524 MEQLNHHTTTRTQME---MLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKEL 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1746 EEEQSNMELLNERFRKTTLQVDTLNSELAgersAAQKSENARQQLERQNKELKAKlqelegsvkSKFKATISTLEAKIAQ 1825
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKLF----DVCGSQDEESDLERLKEEIEKS---------SKQRAMLAGATAVYSQ 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1826 LEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKqlKRQLEEAEEEATRANASRRKlQR 1905
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLAPGRQSIIDLK-EK 744
|
570 580
....*....|....*....|....*
gi 2024363113 1906 ELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1135 |
1.12e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 851 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETElfaEAEEMRARLAAKKQELEEilhdlesr 930
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEE-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 931 veeeeeRNQILQNEKKKMQghiqdleeqldeeegaRQKLQLEKVtaeakikkmeeEILLLEDQNSKFLKEKKLMeDRIAE 1010
Cdd:COG3883 84 ------RREELGERARALY----------------RSGGSVSYL-----------DVLLGSESFSDFLDRLSAL-SKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1011 CTSQLAEEEEKAKnlAKLKNKQEmmitDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEE 1090
Cdd:COG3883 130 ADADLLEELKADK--AELEAKKA----ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2024363113 1091 ELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1135
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1528-1924 |
1.13e-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: 54.19 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1528 HELEKSKRTL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQ--FERDLQARDEQNE--EKKRM 1593
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQekIERYQEDLEELTErlEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1594 LVKQVRELEAELEdERKQRAlavaakkkmEMDLKDLEGQIEAANKARDEaiKQLRKLQAQMKdyQRELEEARA------- 1666
Cdd:COG3096 369 VVEEAAEQLAEAE-ARLEAA---------EEEVDSLKSQLADYQQALDV--QQTRAIQYQQA--VQALEKARAlcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1667 SRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARR---HAEQERDELADEIANSASGKSA--LLDEKRRLEARIAQl 1741
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTAreLLRRYRSQQALAQR- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1742 eeeleeeqsnmellnerfrkttlqVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgsvkskfkatisTLEA 1821
Cdd:COG3096 514 ------------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1822 KIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKeqmeKANARMKQLKRQLEEAEEEATRANASR- 1900
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMq 633
|
410 420 430
....*....|....*....|....*....|
gi 2024363113 1901 ------RKLQRELDDATEANEGLSREVSTL 1924
Cdd:COG3096 634 qllereREATVERDELAARKQALESQIERL 663
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
849-1188 |
1.25e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 849 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLleEKNILAEQlqaetelfaeaeemRARLAAKkQELEEILHdle 928
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLN--------------QARLQAL-EDLEKILT--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 929 srveeeeernqilqnEKKKMQGHIQDLEEQLDEEeGARQKLqlekvTAEAKIKkmeeeILLLEDQNSKFLKEKKLMEDRI 1008
Cdd:PLN02939 164 ---------------EKEALQGKINILEMRLSET-DARIKL-----AAQEKIH-----VEILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1009 AECTSQLAEEEE--KAKNLAkLKNKQEMM------ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAqiee 1080
Cdd:PLN02939 218 GLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1081 LKIQ-LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRdLSEELEALKTELEDTL 1159
Cdd:PLN02939 293 LQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASD 371
|
330 340
....*....|....*....|....*....
gi 2024363113 1160 DTTAAQQELRTKREQEVAELKKAIEEETK 1188
Cdd:PLN02939 372 HEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1529-1807 |
1.29e-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: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1529 ELEKSKRTLEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARdeQNEEKKR-----------MLV 1595
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRelerirqeeiaMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1596 KQVRELE--------------AELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQREL 1661
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1662 EEARASRDEIFAQsKESEKKLKGLEAEILQLQEEFAASERaRRHAEQERDEladeiansasGKSALLDEKRR---LEARI 1738
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEE----------RKQAMIEEERKrklLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1739 AQLEEELEEEQSNMELLNERFRKTTL----QVDTLNSELAGERSAAQKSENARQQLeRQNKELKAKLQELEGS 1807
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
804-1237 |
1.30e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.82 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 804 KAFAKKQQQLSALKILQRNCAAY-----LKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEM 878
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 879 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQ 958
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 959 LDEEEGARQKLQ-LEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQE---M 1034
Cdd:TIGR00618 586 IPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRehaL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1035 MITDLEER-LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVI 1113
Cdd:TIGR00618 666 SIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1114 RELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldttaaQQELRTKREQEVAELKKAIEEETKNHEA- 1192
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF-------FNRLREEDTHLLKTLEAEIGQEIPSDEDi 818
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 1193 ------QIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1237
Cdd:TIGR00618 819 lnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1322-1708 |
1.34e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1322 ELLQEETRQKLNLSSRIRQLEEEK---NNLQEQQEEEEEARKNLEKQMLALQAQLAEAKkkvdddlgTIEGLEENKKKLL 1398
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQyrlVEMARELAELNEAESDLEQDYQAASDHLNLVQ--------TALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1399 KDMESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMVDL-DHQ-------------RQIVSNLEKKQKKFDQML 1457
Cdd:PRK04863 355 ADLEELEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLaDYQqaldvqqtraiqyQQAVQALERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1458 AEEKNISARYAEERDRAEA---EAREKETKaLSLARALEEALEAKEEFERqnkQLRADMEdlMSSKDDVGKNVHELEKSK 1534
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEateELLSLEQK-LSVAQAAHSQFEQAYQLVR---KIAGEVS--RSEAWDVARELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1535 RTLEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQARDEQNEEKKRMLvkqvRELEAELEDERKQRAL 1614
Cdd:PRK04863 509 RHLAEQLQQLRMRLSELEQRLRQQQRA--------ERLLAEFCKRLGKNLDDEDELEQLQ----EELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1615 AVAAKKKMEMDLKDLEGQIEAANK------ARDEAIKQLRK-----------LQAQMKDYQRELEEARASRDEIFAQSKE 1677
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREqsgeefedsqdVTEYMQQLLERERELTVERDELAARKQA 656
|
410 420 430
....*....|....*....|....*....|..
gi 2024363113 1678 sekklkgLEAEILQL-QEEFAASERARRHAEQ 1708
Cdd:PRK04863 657 -------LDEEIERLsQPGGSEDPRLNALAER 681
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1016-1280 |
1.47e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1016 AEEEEKAKNLAKLKNKQEMMITDLEErlkKEEKTRQELEKAKRKLDG-----------ETTDLQDQIAELQAQIEELkiq 1084
Cdd:PRK04863 833 ADPEAELRQLNRRRVELERALADHES---QEQQQRSQLEQAKEGLSAlnrllprlnllADETLADRVEEIREQLDEA--- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1085 lakkeEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELE-----ALKTELEDTL 1159
Cdd:PRK04863 907 -----EEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfSYEDAAEMLA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1160 DTTAAQQELRTKREQEVAELKKAiEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEK----NKQGLE----S 1231
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRA-REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpADSGAEerarA 1060
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2024363113 1232 DNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAE 1280
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1574-1912 |
1.56e-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: 53.42 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1574 AQFERDLQ-ARDEQNEEKKRmLVKQVRELEaelEDERKQRAL----------------AVAAKKKMEM---DLKDLEGQI 1633
Cdd:COG3096 288 LELRRELFgARRQLAEEQYR-LVEMARELE---ELSARESDLeqdyqaasdhlnlvqtALRQQEKIERyqeDLEELTERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1634 EAANKARDEAIKQLRKLQAQmkdyqreLEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARR---HAEQER 1710
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcgLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1711 DELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLnerfrkttlqvdtlnSELAGERSAAQKSENARQQL 1790
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV---------------CKIAGEVERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1791 eRQNKELKAKLQELEgsvkskfkatisTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKevfmqvederrHADQYKE 1870
Cdd:COG3096 502 -RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----------AAEELEE 557
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2024363113 1871 QMEKANARMKQLKRQLEeaeeeatRANASRRKLQRELDDATE 1912
Cdd:COG3096 558 LLAELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRA 592
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1071-1348 |
1.77e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 53.32 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKnnaLKviRELQAQIAE------LQEDLESEKASRNKAEKQK--- 1141
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LK--KEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1142 -RDLSEELEALKTELEDTLDTTAAQQELRTKRE--QEVAELKKAIEEETKNHEAQiQEIRQRHATALEElSEQLEQAKRF 1218
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFKEVMDR-PEIKEKMEAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1219 KANLEKNKQGLESD-NKELACEV-KVLQQVKAESEHKRKKLDAQVQELTAK--VTEGERLRVELAEKANKLQNELD---- 1290
Cdd:PLN03229 584 KAEVASSGASSGDElDDDLKEKVeKMKKEIELELAGVLKSMGLEVIGVTKKnkDTAEQTPPPNLQEKIESLNEEINkkie 663
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 1291 ---NVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1348
Cdd:PLN03229 664 rviRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1365-1912 |
1.97e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1365 QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEkamaYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1444
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISN----IDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1445 NLEKK-----------QKKFDQMLAEEKNISARyAEERDRAEAEAREKETKalslaraleealeaKEEFERQNKQLRADM 1513
Cdd:PRK01156 215 ITLKEierlsieynnaMDDYNNLKSALNELSSL-EDMKNRYESEIKTAESD--------------LSMELEKNNYYKELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1514 EDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFERDLQARDEQN------ 1587
Cdd:PRK01156 280 ERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilel 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1588 ---EEKKRMLVKQVRELEAELEDERKQR----ALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRE 1660
Cdd:PRK01156 359 egyEMDYNSYLKSIESLKKKIEEYSKNIermsAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1661 LEEARASRDEIFAQS------------------KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAS 1722
Cdd:PRK01156 439 LDELSRNMEMLNGQSvcpvcgttlgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSI 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1723 GKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRktTLQVDTLNSELAGERSA-AQKSENARQQLERQNKELKAKL 1801
Cdd:PRK01156 519 NEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK--SLKLEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1802 QELEG---SVKSKFKATISTLEAKIAQLEEQLeqeakeraaanKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANAR 1878
Cdd:PRK01156 597 NDLESrlqEIEIGFPDDKSYIDKSIREIENEA-----------NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
|
570 580 590
....*....|....*....|....*....|....
gi 2024363113 1879 MKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1912
Cdd:PRK01156 666 IPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1082-1340 |
2.11e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.13 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1082 KIQLAKKEEELQAALARGDEEAVQknnalkvirELQAQIAELQEdlesEKASRNKAEKQKR------DLSEELEALKTEL 1155
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEIVE---------ALQSALNWLEE----RKGSLERAKQYQQvidnfpKLSAELRQQLNNE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1156 ED---TLDTTAAQQELrtkrEQEVAELKKAIEEETknHEAQIQEIRQRH-ATALEELSEQLEQAKRFKANLEKNKQGLES 1231
Cdd:PRK10929 92 RDeprSVPPNMSTDAL----EQEILQVSSQLLEKS--RQAQQEQDRAREiSDSLSQLPQQQTEARRQLNEIERRLQTLGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1232 DNKELACEVKVLQQvkAESEHKRKKLD----AQV-----QELTakvtegeRLRVELAEK-ANKLQNELDNVSSLL----- 1296
Cdd:PRK10929 166 PNTPLAQAQLTALQ--AESAALKALVDelelAQLsannrQELA-------RLRSELAKKrSQQLDAYLQALRNQLnsqrq 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1297 ---EEAEKKGIKFAKDAASLE----SQLQDTQELLQE--ETRQKLNL-SSRIRQ 1340
Cdd:PRK10929 237 reaERALESTELLAEQSGDLPksivAQFKINRELSQAlnQQAQRMDLiASQQRQ 290
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1050-1913 |
2.38e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1050 RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQlakkEEELQAA---LARGDEEAVQKNNalkvIRELQAQIAELQED 1126
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAAsdhLNLVQTALRQQEK----IERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1127 LESEKASRNKA-------EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKA------IEEETKNHEAQ 1193
Cdd:PRK04863 364 LEEQNEVVEEAdeqqeenEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAkqlcglPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1194 IQEIR---QRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEH-KRKKLDAQVQELTAKVT 1269
Cdd:PRK04863 444 LEEFQakeQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1270 EGERlRVELAEKANKLQNELDNVSSLLEEAEKkgikfakDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlq 1349
Cdd:PRK04863 524 ELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQ----- 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1350 eqQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENkkkllkdMESLSQRLEEKAMAYDKLEKTKNRLQQEL 1429
Cdd:PRK04863 591 --LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEY-------MQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1430 DDLmvdldHQRQiVSNLEKKQKKFDQM-------------LAEEKNISARYAEER------DraeaeareketkaLSLAR 1490
Cdd:PRK04863 662 ERL-----SQPG-GSEDPRLNALAERFggvllseiyddvsLEDAPYFSALYGPARhaivvpD-------------LSDAA 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1491 aleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK------SKRTL----------------EQQVE 1542
Cdd:PRK04863 723 -------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKavvvkiADRQWrysrfpevplfgraarEKRIE 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1543 EMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQ-----ARDEQNEEKKRMLVKQVRELEAELED----ERKQR 1612
Cdd:PRK04863 790 QLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELRQLNRRRVELERALADhesqEQQQR 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1613 ALAVAAKKKMEMdLKDLEGQIEAAnkARDEAIKQLRKLQAQMKdyqrELEEARASRDE---IFAQSKESEKKLKGLEAEI 1689
Cdd:PRK04863 865 SQLEQAKEGLSA-LNRLLPRLNLL--ADETLADRVEEIREQLD----EAEEAKRFVQQhgnALAQLEPIVSVLQSDPEQF 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1690 LQLQEEFAASERARRHAEQERDELADEIANSASGKSAllDEKRRLEARIAqleeeleeeqsnmelLNERFRkttlqvdtl 1769
Cdd:PRK04863 938 EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD---------------LNEKLR--------- 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1770 nselagersaaQKSENARQQLERQNKELKAKLQELE--GSVKSKFKATISTLEAKIAQLEEQLE-------QEAKERAAA 1840
Cdd:PRK04863 992 -----------QRLEQAEQERTRAREQLRQAQAQLAqyNQVLASLKSSYDAKRQMLQELKQELQdlgvpadSGAEERARA 1060
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1841 NKlvrrtekklKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaeeeatranasrRKLQRELDDATEA 1913
Cdd:PRK04863 1061 RR---------DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL--------------RKLERDYHEMREQ 1110
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1071-1327 |
2.61e-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: 52.91 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELKIQLAKKEeelQAALARGDEEAVQKNNAlKVIRELQAQIAEL---QEDLES--EKASRNKAEKQKRDLS 1145
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDD---AAQNALADKERAEADRQ-RLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1146 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKAIEEE---TKNH-EAQIQEIRQRHATALEELSEQLE 1213
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1214 QAKRFKANLEKNKQGLESDNKelacevkvlqqvKAESEHKRKKLDAQVQELTAKVTEgerlrvelaEKANklqneldnvs 1293
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAE---------SDAN---------- 1741
|
250 260 270
....*....|....*....|....*....|....*
gi 2024363113 1294 SLLEEAEKKGIKFAKDAASLESQLQ-DTQELLQEE 1327
Cdd:NF012221 1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1277-1908 |
3.23e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1277 ELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLQEQQEE 1354
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1355 EEEA-----RKNLEKQMLALQAQLAEAKK-------KVDDDLGTIEGLEENKKKLLKDmeslsqrlEEKAMAYDKLEKTK 1422
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEIND--------KEKQVSLLLIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1423 NrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEF 1502
Cdd:pfam05483 252 K--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1503 ERQNKqlrADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAMKAQFERD 1579
Cdd:pfam05483 330 TEEKE---AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKFKNNKEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1580 LQARDEQNEEKKRMLV--KQVRELEAELEDERKQRALAVAAKKKmemDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDY 1657
Cdd:pfam05483 407 LEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1658 QRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAaserarrHAEQERDELADEIANSASGKSALLDEKRRLEAR 1737
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDII-------NCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1738 IAQLEEELE----EEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKlqeleGSVKSKfk 1813
Cdd:pfam05483 557 FIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-----GSAENK-- 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1814 aTISTLEAKIAQLEEQLEqeakerAAANKLVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANARMKQLKrqleeaeeea 1893
Cdd:pfam05483 630 -QLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV---------- 688
|
650
....*....|....*
gi 2024363113 1894 tranasrrKLQRELD 1908
Cdd:pfam05483 689 --------KLQKEID 695
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1691-1912 |
4.00e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1691 QLQEEFAASERARRHAEQERDELADEIansasgksalldekRRLEARIAQLEEeleeeQSNMELLNERFRKTTLQVDTLN 1770
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1771 SELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvkskfkATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKK 1850
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1851 LKEVFMQVEDE-RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRK---LQRELDDATE 1912
Cdd:COG3206 300 IAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
975-1213 |
4.01e-06 |
|
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: 52.07 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 975 TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTS----QLAEEEEKAKNLAKLKNKqemmITDLEErlKKEEKTR 1050
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1051 QELEK--------AKRKLDGETTDLQDQIAELQAQIEELKIQLA--KKEEELQAALARGDEEAVQKNNALKVIRELQAQI 1120
Cdd:pfam09731 261 QELVSifpdiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVR 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1121 A--ELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEvAELKKAIEEETKNHEAQIQEIr 1198
Cdd:pfam09731 341 AadEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNEL- 418
|
250
....*....|....*
gi 2024363113 1199 qrhATALEELSEQLE 1213
Cdd:pfam09731 419 ---LANLKGLEKATS 430
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
849-1157 |
4.59e-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: 52.15 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 849 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQL-QAETELFAEAEEMRARLAAKKQELeeilhDL 927
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQL-----DK 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 928 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEeillledQNSKFLKEKKLMEDR 1007
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALET-------WYKRDLASLGVDPDV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1008 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEektRQELEKAKRKLDGETTDLQDQiaeLQAQIEELKIQLAK 1087
Cdd:pfam12128 770 IAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQR---RPRLATQLSNIERAISELQQQ---LARLIADTKLRRAK 843
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1088 KEEELQAAlargDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQ------KRDLSEELEALKTELED 1157
Cdd:pfam12128 844 LEMERKAS----EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLaqledlKLKRDYLSESVKKYVEH 915
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
995-1153 |
4.73e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 995 SKFLK-EKKLMEDR---------IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGET 1064
Cdd:COG2433 350 NKFERvEKKVPPDVdrdevkarvIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1065 TDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEeavqknnalkvIRELQAQIAELQEDLESEkasrnkaEKQKRDL 1144
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEARSEERREIRKDRE-----------ISRLDREIERLERELEEE-------RERIEEL 491
|
....*....
gi 2024363113 1145 SEELEALKT 1153
Cdd:COG2433 492 KRKLERLKE 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
883-1737 |
5.07e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 883 QQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQIlqnekKKMQGHIQDLEEQLDEE 962
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-----ERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 963 EGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKF-----LKEKKLME--------DRIAECTSQLAEEEEKAKN-LAKL 1028
Cdd:PRK04863 368 NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyqqavqalERAKQLCGLPDLTADNAEDwLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1029 KNKQEMMIT---DLEERLKKEEKTRQELEKAK---RKLDGETT--DLQDQIAELQAQIEELKIQlAKKEEELQAALARGD 1100
Cdd:PRK04863 448 QAKEQEATEellSLEQKLSVAQAAHSQFEQAYqlvRKIAGEVSrsEAWDVARELLRRLREQRHL-AEQLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1101 EEAVQKNNALKVIRELQaQIAELQEDLESEkasrnkaekqkrdLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELK 1180
Cdd:PRK04863 527 QRLRQQQRAERLLAEFC-KRLGKNLDDEDE-------------LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1181 KAIEEetknHEAQIQEIRQRHAtALEELSEQleqakrFKANLEkNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQ 1260
Cdd:PRK04863 593 ARIQR----LAARAPAWLAAQD-ALARLREQ------SGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1261 VQELTAKVT-EGERLRVeLAEKANK-----------------------------LQNELDNVSSLLEEAEK--------K 1302
Cdd:PRK04863 661 IERLSQPGGsEDPRLNA-LAERFGGvllseiyddvsledapyfsalygparhaiVVPDLSDAAEQLAGLEDcpedlyliE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1303 GIKFAKDAASLESQLQDTQELLQEETRQkLNLS--------------SRIRQLEEEKNNLQEQQEEEEEARKNLE----- 1363
Cdd:PRK04863 740 GDPDSFDDSVFSVEELEKAVVVKIADRQ-WRYSrfpevplfgraareKRIEQLRAEREELAERYATLSFDVQKLQrlhqa 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1364 -KQMLALQAQLAEAkkkVDDDlgtiegleenkkkllKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqRQI 1442
Cdd:PRK04863 819 fSRFIGSHLAVAFE---ADPE---------------AELRQLNRRRVELERALADHESQEQQQRSQLEQA-------KEG 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1443 VSNLEKKQKKFDqMLAEEKNIsaryaeerDRAEaEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskDD 1522
Cdd:PRK04863 874 LSALNRLLPRLN-LLADETLA--------DRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF----EQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1523 VGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELE 1602
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQ 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1603 AELeDERKQRalavaakkkmemdLKDLEGQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARASRDEIFAQSKESEKK 1681
Cdd:PRK04863 1013 AQL-AQYNQV-------------LASLKSSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRDELHARLSANRSR 1075
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 1682 LKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALL------DEKRRLEAR 1737
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
874-1472 |
5.38e-06 |
|
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: 51.98 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 874 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeilhdLESRVEEEEERNQILQNEKKKmqghiq 953
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIIIKEIKD------ 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 954 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED--------------------RIAECts 1013
Cdd:TIGR01612 1556 -----------AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflkisdikkKINDC-- 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1014 qLAEEEEKAKNLAKLK-NKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQIEELKIQLAKKEEEL 1092
Cdd:TIGR01612 1623 -LKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1093 QAALA-RGDEEAVQKNNALKVIRELqaqiaeLQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK 1171
Cdd:TIGR01612 1698 EIGIIeKIKEIAIANKEEIESIKEL------IEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAG 1771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1172 REQEVAElkkaiEEETKNheaqiqEIRQRHATALEELSEQLEQAKRFKANLeknkqglesDNKElacevkvLQQVKAESE 1251
Cdd:TIGR01612 1772 CLETVSK-----EPITYD------EIKNTRINAQNEFLKIIEIEKKSKSYL---------DDIE-------AKEFDRIIN 1824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1252 HKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVS---------------------SLLEEAEKKGIKFAKDA 1310
Cdd:TIGR01612 1825 HFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLlfdilnktkdayagiigkkyySYKDEAEKIFINISKLA 1904
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1311 ASLESQLQDTQEL-------------LQEETRQKL-------NLSSRIRQLEEEKNNLQEQQEEEEEARKNlEKQMLAL- 1369
Cdd:TIGR01612 1905 NSINIQIQNNSGIdlfdniniailssLDSEKEDTLkfipspeKEPEIYTKIRDSYDTLLDIFKKSQDLHKK-EQDTLNIi 1983
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1370 --QAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEE---------------KAMAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR01612 1984 feNQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKF 2063
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2024363113 1433 MVDLDHQ--RQIVSNLEKKQKKFDQMLAEEKNISARYAEERD 1472
Cdd:TIGR01612 2064 GIDFDVKamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1559-1721 |
5.48e-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: 51.57 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1559 EDAKLRLEVNMQAMKAQFErDLQAR-DEQNEEKKRMLV--KQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEA 1635
Cdd:pfam05667 327 EELQQQREEELEELQEQLE-DLESSiQELEKEIKKLESsiKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIAK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1636 ANKARDEAIKQLRKLQAQMKDYQREL-EEARASRDEIFAQSKESEKKL---KGLEAEILQLQEEFAASERARRHAEQERD 1711
Cdd:pfam05667 406 LQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLeeiKELREKIKEVAEEAKQKEELYKQLVAEYE 485
|
170
....*....|
gi 2024363113 1712 ELADEIANSA 1721
Cdd:pfam05667 486 RLPKDVSRSA 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1335-1559 |
5.87e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1335 SSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvdddlgtIEGLEENKKKLLKDMESLSQRLEEKAMA 1414
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1415 YDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKNIsaRYAEERDRAEAEAREKETKAL-SLARAL 1492
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYL--KYLAPARREQAEELRADLAELaALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1493 EEALEAKEEFERQNKQLRADMEDLMSSKDDVgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1559
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1111-1286 |
7.17e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 50.35 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1111 KVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL---EALKTELEDTLDTTAAQqelRTKREQEVAELKKAIEEEt 1187
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQALLAELAGA---GAAAEGRAGELAQELDSE- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1188 knheaqiQEIRQRHATALEELSEQLEQAKRfkanleknkqglesdnkELAcevkVLQQVKAESEHKRKKLDAQVQELtak 1267
Cdd:PRK09039 129 -------KQVSARALAQVELLNQQIAALRR-----------------QLA----ALEAALDASEKRDRESQAKIADL--- 177
|
170
....*....|....*....
gi 2024363113 1268 vteGERLRVELAEKANKLQ 1286
Cdd:PRK09039 178 ---GRRLNVALAQRVQELN 193
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1091-1268 |
7.21e-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: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1091 ELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldtTAAQQELRT 1170
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1171 KREQEvaelkkAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVkvlqqvkAES 1250
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL-------AEL 154
|
170
....*....|....*...
gi 2024363113 1251 EHKRKKLDAQVQELTAKV 1268
Cdd:COG1579 155 EAELEELEAEREELAAKI 172
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1308-1737 |
7.41e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1308 KDAASLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQlaEAKKKVDDDLgti 1387
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMA---RELAELNEAESDLEQDYQAASDHLNLVQTALRQQ--EKIERYQADL--- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1388 egleenkkkllkdmESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMVDL-DHQ-------------RQIVSNL 1446
Cdd:PRK04863 358 --------------EELEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLaDYQqaldvqqtraiqyQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1447 EKKQKKFDQMLAEEKNISARYAEERDRAEA---EAREKETKaLSLARALEEALEAKEEFERQnkqLRADMEdlMSSKDDV 1523
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEateELLSLEQK-LSVAQAAHSQFEQAYQLVRK---IAGEVS--RSEAWDV 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1524 GKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQARDEQNEEKKRMLvkqvRELEA 1603
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA--------ERLLAEFCKRLGKNLDDEDELEQLQ----EELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1604 ELEDERKQRALAVAAKKKMEMDLKDLEGQIEaankardeaikQLRKLQAQMKDYQRELEEARASRDEIFAQSKesekklk 1683
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQ-----------RLAARAPAWLAAQDALARLREQSGEEFEDSQ------- 627
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1684 GLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEAR 1737
Cdd:PRK04863 628 DVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
970-1433 |
9.21e-06 |
|
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: 51.21 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 970 QLEKVTAEA-------KIKKMEEEILLLEDQNSKFLKEKKLMEDRIAEC-TSQLAEEEEKAKNLAKLKNKQEMMITDLEE 1041
Cdd:TIGR01612 1154 DLEDVADKAisnddpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1042 RLKKEEKTRQELEKAKRKLDG------ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVI-- 1113
Cdd:TIGR01612 1234 EKKKSEHMIKAMEAYIEDLDEikekspEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIed 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1114 -----------RELQAQIAELQED--------------------------LESEKASRNKAEKQKRDLSEE--------- 1147
Cdd:TIGR01612 1314 fseesdindikKELQKNLLDAQKHnsdinlylneianiynilklnkikkiIDEVKEYTKEIEENNKNIKDEldkseklik 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1148 -------LEALKTELEDTLD----------TTAAQQELRTKREQEVAELKKAIE------------EETKNHEAQIQEIR 1198
Cdd:TIGR01612 1394 kikddinLEECKSKIESTLDdkdidecikkIKELKNHILSEESNIDTYFKNADEnnenvlllfkniEMADNKSQHILKIK 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1199 QRHATA-----LEELSEQLEQAKRFKANLEKNKQGLESD---------------NKELACEVK-VLQQVKAESE------ 1251
Cdd:TIGR01612 1474 KDNATNdhdfnINELKEHIDKSKGCKDEADKNAKAIEKNkelfeqykkdvtellNKYSALAIKnKFAKTKKDSEiiikei 1553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1252 ---HKRKKLDAQVQELTAKVTEGERLRVE-LAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELlqEE 1327
Cdd:TIGR01612 1554 kdaHKKFILEAEKSEQKIKEIKKEKFRIEdDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESI--EK 1631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1328 TRQKLNLSSRIRQLEEEKNN---LQEQQEEEEEARKNLEKQmlalqaqlaeaKKKVDDDLGTIEGLEENKKKLLKDME-S 1403
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNlnsLQEFLESLKDQKKNIEDK-----------KKELDELDSEIEKIEIDVDQHKKNYEiG 1700
|
570 580 590
....*....|....*....|....*....|.
gi 2024363113 1404 LSQRLEEKAMA-YDKLEKTKNRLQQELDDLM 1433
Cdd:TIGR01612 1701 IIEKIKEIAIAnKEEIESIKELIEPTIENLI 1731
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1416-1681 |
1.05e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1416 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAR 1479
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1480 EKETKALSLaraleealeakeeferqnKQLRADMEDLMSSKDDVGKNVHELEKSKR--TLEQQVEEMRTQLEELEDelqa 1557
Cdd:PHA02562 249 DIEDPSAAL------------------NKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKD---- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1558 tedaklrlevNMQAMKAQFERDLQARDEQNE--EKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmdlkdlegqiea 1635
Cdd:PHA02562 307 ----------KLKELQHSLEKLDTAIDELEEimDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK------------ 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2024363113 1636 ankardeaiKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1681
Cdd:PHA02562 365 ---------AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1066-1699 |
1.09e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1066 DLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLS 1145
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1146 EELEA---LKTELEDTLDTTAAQQELRTKREQEVAELKKAIE---EETKNHEAQIQEIRQRH--ATALEELSEQLEQAKR 1217
Cdd:PRK01156 267 MELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEnkkQILSNIDAEINKYHAIIkkLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1218 FKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLdaqvqeltakvtegERLRVELAEKANKLQNELDNVSSLLE 1297
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI--------------ERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1298 EAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNlqeqqeeeeEARKNLEKQMLALQA 1371
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSN---------HIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1372 QLAEAKKKVDDdlgtiegLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1451
Cdd:PRK01156 484 KIREIEIEVKD-------IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1452 KFDQMLAEEKNISARYAEERdraeaeaREKETKALSLARAleealeakeeferqnkqlrADMEDLMSSKDDVGKNVHELE 1531
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSK-------RTSWLNALAVISL-------------------IDIETNRSRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1532 KSKRTLEQQVEEMRT----QLEELEDELQATEDAKLRLEVNMQAMkaqferdlqardeqneEKKRMLVKQVRELEAELED 1607
Cdd:PRK01156 601 SRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILI----------------EKLRGKIDNYKKQIAEIDS 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1608 ERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEaikqLRKLQAQMKDYQRELEEARASRDEIFaqskESEKKLKGLEA 1687
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR----LESTIEILRTRINELSDRINDINETL----ESMKKIKKAIG 736
|
650
....*....|..
gi 2024363113 1688 EILQLQEEFAAS 1699
Cdd:PRK01156 737 DLKRLREAFDKS 748
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1597-1919 |
1.16e-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: 50.07 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1597 QVRELEAELEDERkqralavAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1676
Cdd:pfam19220 49 RLLELEALLAQER-------AAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1677 ESEKKLKG-------LEAEILQLQEEFAASERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQ 1749
Cdd:pfam19220 122 ALERQLAAeteqnraLEEENKALREEAQAAEKALQRAEGELATARERLA-------LLEQENRRLQALSEEQAAELAELT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1750 SNMELLNERFRKTTLQVDTLNSELAGERSAAQKSEnarqqlerqnkelkaklqelegsvkskfkatistleakiAQLEEQ 1829
Cdd:pfam19220 195 RRLAELETQLDATRARLRALEGQLAAEQAERERAE---------------------------------------AQLEEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1830 LEQEAKERA-------AANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRK 1902
Cdd:pfam19220 236 VEAHRAERAslrmkleALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQE 315
|
330
....*....|....*..
gi 2024363113 1903 LQRELDDATEANEGLSR 1919
Cdd:pfam19220 316 MQRARAELEERAEMLTK 332
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1016-1380 |
1.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1016 AEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKakrkldgETTDLQDQIAELQAQIEELKIQLAKKEEELQAA 1095
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQE-------ELEQLREELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1096 LARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQE 1175
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1176 VAELKKAIEEETKNHEAQIQEIRQRhatALEELSEQLEQAKRFKANLEKNKQGLESDNKELAcEVKVLQQVKAESEHKRK 1255
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQ---ALDELLKEANRNAEKEEELAEAEKLIESLPRELA-EELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1256 KLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLS 1335
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024363113 1336 SRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKV 1380
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1548-1927 |
1.23e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1548 LEELEdELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLK 1627
Cdd:PTZ00121 1029 IEELT-EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQD--EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1628 DLEGQIEAANKARdEAIKQLRKLqaqmkdyqRELEEARasRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAE 1707
Cdd:PTZ00121 1106 TETGKAEEARKAE-EAKKKAEDA--------RKAEEAR--KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1708 QERDELA---DEIANSASGKSAllDEKRRLEAriAQLEEELEEEQSNMELLNERFRKTTLQVDtlnselagerSAAQKSE 1784
Cdd:PTZ00121 1175 AKKAEAArkaEEVRKAEELRKA--EDARKAEA--ARKAEEERKAEEARKAEDAKKAEAVKKAE----------EAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1785 NARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAqleEQLeQEAKERAAANKLVRRTEKKLKEVFMQVEDERRH 1864
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DEL-KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1865 ADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1927
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1030-1285 |
1.25e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1030 NKQEMMITDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQK 1106
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1107 NNALKVIRELQAQIAELQEdlesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK---REQEVAELKKAI 1183
Cdd:COG1340 81 DELNEKLNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKikeLEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1184 EEETKNHE--AQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKElacevkvLQQVKAESEHKRKKLDAQV 1261
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE-------ADELHKEIVEAQEKADELH 229
|
250 260
....*....|....*....|....
gi 2024363113 1262 QELTAKVTEGERLRVELAEKANKL 1285
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQ 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1212 |
1.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 846 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEekniLAEQLQAETELfAEAEEMRARLAAKKQELEEILH 925
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR----LAEYSWDEIDV-ASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 926 DLEsrveeeeernqilqnekkkmqghiqdleeqldeeegarqKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLME 1005
Cdd:COG4913 686 DLA---------------------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1006 DRIAECTSQLAEEEEKAKNLAklknkqemmITDLEERLKKEEKTRQElEKAKRKLDGETTDLQDQIAELQAQIEELKIQL 1085
Cdd:COG4913 727 EELDELQDRLEAAEDLARLEL---------RALLEERFAAALGDAVE-RELRENLEERIDALRARLNRAEEELERAMRAF 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1086 AKKEEELQAALARGDEEAVQKNNALKVIR-----ELQAQIAELQEDLESEKASR--NKAEKQKRDLSEELEALKTELEDT 1158
Cdd:COG4913 797 NREWPAETADLDADLESLPEYLALLDRLEedglpEYEERFKELLNENSIEFVADllSKLRRAIREIKERIDPLNDSLKRI 876
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1159 L--DTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQL 1212
Cdd:COG4913 877 PfgPGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
1.29e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.29e-05
10 20
....*....|....*....|....*
gi 2024363113 657 YKESLTKLMATLRNTNPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
975-1300 |
1.36e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.22 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 975 TAEAKIKKMEEEILLL---EDQNSKFLKE---------KKLMEDR------IAECTSQLAEEEEKAKNLAKLKN-----K 1031
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEEFSQFVELTEsgdyvE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1032 QEMMITDLEERLKKEEKTRQELEKAKRKLDgetTDLQDQIAELQAQIEELKIQ---------------LAKKEEELQAAL 1096
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeiqdLKEQIDENLALL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1097 ARGDEEAVQKNNAlkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEV 1176
Cdd:PRK04778 273 EELDLDEAEEKNE-----EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1177 aELKKAIEEETKNHEAQIQEIRQRHATA----------LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQV 1246
Cdd:PRK04778 348 -ESVRQLEKQLESLEKQYDEITERIAEQeiayselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1247 KAESEHKRKKL------DAQVQELTAKVTEGERLRVELaekaNKLQNELDNVSSLLEEAE 1300
Cdd:PRK04778 427 LHEIKRYLEKSnlpglpEDYLEMFFEVSDEIEALAEEL----EEKPINMEAVNRLLEEAT 482
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1047-1324 |
1.41e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.15 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1047 EKTRQeLEKAKRKLDGETTDLQDQ---------------IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALK 1111
Cdd:pfam00038 18 DKVRF-LEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1112 VIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEledtldttaaqqelrtkREQEVAELKKAIEEETKNHE 1191
Cdd:pfam00038 97 LRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1192 aqIQEIRQRH-ATALEELSEQLE-QAKRFKANLEKN-KQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKV 1268
Cdd:pfam00038 160 --MDAARKLDlTSALAEIRAQYEeIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1269 TEGERLRVELAEKANKLQNELDNVSSLLEEAEKkgiKFAKDAASLESQLQDTQELL 1324
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEA---ELQETRQEMARQLREYQELL 290
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
971-1139 |
1.63e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 971 LEKVTAEAKIKKMEEEIllledqnSKFLKE-KKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQ-EMMITDLEERLKKEEK 1048
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-------KRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRErRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1049 T----RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvqKNNAL-KVIRELQAQIAEL 1123
Cdd:PRK12704 97 NldrkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEA--KEILLeKVEEEARHEAAVL 174
|
170
....*....|....*.
gi 2024363113 1124 QEDLESEkaSRNKAEK 1139
Cdd:PRK12704 175 IKEIEEE--AKEEADK 188
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1040-1426 |
2.13e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1040 EERLKKEEKTRQELEKAKRKLDGETTDLQD-------QIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV 1112
Cdd:pfam10174 358 ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1113 IRELQAQIAELQEDLESEKASRNKAEKQKRdlsEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaieeETKNHEA 1192
Cdd:pfam10174 438 LTTLEEALSEKERIIERLKEQREREDRERL---EELESLKKENKDLKEKVSALQPELTEKESSLIDLK-----EHASSLA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1193 QIQEIRQRHATALE-ELSEQLEQAKRFKANLEKNKQGLESD--NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVT 1269
Cdd:pfam10174 510 SSGLKKDSKLKSLEiAVEQKKEECSKLENQLKKAHNAEEAVrtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILR 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1270 EGERLRVELAEKANKLQN-----------ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQ--------EETRQ 1330
Cdd:pfam10174 590 EVENEKNDKDKKIAELESltlrqmkeqnkKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQleelmgalEKTRQ 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1331 KLN-----LSSRIRQLEEEKNNLQEQQEEEeeaRKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLs 1405
Cdd:pfam10174 670 ELDatkarLSSTQQSLAEKDGHLTNLRAER---RKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMAL- 745
|
410 420
....*....|....*....|.
gi 2024363113 1406 qRLEEKAMAYDKLEKTKNRLQ 1426
Cdd:pfam10174 746 -KREKDRLVHQLKQQTQNRMK 765
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
901-1459 |
2.30e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 901 ELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEErnqiLQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKI 980
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 981 K-KMEEEILLLEDQN--SKFLKEKKLMEDRIAECTSQLAEEEEKAKNlaklknkqemmITDLEERLKKEEKTRQeleKAK 1057
Cdd:PRK01156 228 NnAMDDYNNLKSALNelSSLEDMKNRYESEIKTAESDLSMELEKNNY-----------YKELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1058 RKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQ--AALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1135
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1136 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRhataLEELSEQL--- 1212
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNMeml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1213 ---------------EQAKRFKANLEKNKQGLESDNKELACEVKVL-----QQVKAESEHKRKKL------DAQVQELTA 1266
Cdd:PRK01156 450 ngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIdekivDLKKRKEYLESEEInksineYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1267 KVTEGERLRVELAEKANKLQNELDNVSSL-LEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLN-LSSRIRQLEEE 1344
Cdd:PRK01156 530 DLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNdLESRLQEIEIG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1345 KNNLQEQQEEEEEARKNlEKQMLALQAQLAEAKKKVDDdlgTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNR 1424
Cdd:PRK01156 610 FPDDKSYIDKSIREIEN-EANNLNNKYNEIQENKILIE---KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKK 685
|
570 580 590
....*....|....*....|....*....|....*
gi 2024363113 1425 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1459
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1152 |
2.31e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 845 LQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERkhqqLLEEKNILAEQLQAETELFAEAEEmraRLAAKKQELEEil 924
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEK-- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 925 hdLESRVEEEEERNQILQNEKKKMQGhiqdleeqldeeegarqkLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKklm 1004
Cdd:PRK03918 530 --LKEKLIKLKGEIKSLKKELEKLEE------------------LKKKLAELEKKLDELEEELAELLKELEELGFES--- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1005 edrIAECTSQLAEEEEKAKNLAKLKNKQEmmitDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQIEELKIQ 1084
Cdd:PRK03918 587 ---VEELEERLKELEPFYNEYLELKDAEK----ELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKK 655
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1085 LAKKE-EELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1152
Cdd:PRK03918 656 YSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
842-1245 |
2.39e-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: 49.12 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 842 KPLLQVTRQEEELQAKD--EELMKVKEKQTKVEAELEEMERKhqqlleekniLAEQLQAETELFAEAEEMRARLAAKKQE 919
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQE----------RAELLQAQEAANRQREKEKERYKRDREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 920 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLK 999
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1000 EKKLMEDRIAECTSQLAEEEEKAKNLaklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIE 1079
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1080 ELKIQLAKKeEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESE-KASRNKAEKQKRDLSEELEALK------ 1152
Cdd:pfam07888 224 TAHRKEAEN-EALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAElHQARLQAAQLTLQLADASLALRegrarw 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1153 -TELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANL---EKNKQG 1228
Cdd:pfam07888 303 aQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQ 382
|
410
....*....|....*..
gi 2024363113 1229 LESDNKELACEVKVLQQ 1245
Cdd:pfam07888 383 LQAEKQELLEYIRQLEQ 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1507-1726 |
2.71e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1507 KQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL-------QATEDAKLRLEV------------ 1567
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralYRSGGSVSYLDVllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1568 NMQAMKAQFERDLQARDEQNEEKKrmlvkQVRELEAELEDERKQralAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1647
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1648 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSA 1726
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1311-1740 |
2.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1311 ASLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEkQMLALQAQLAEAKKKVDDDLGTIEG 1389
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1390 LEEN------KKKLLKDMESLSQRLEE---KAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkFDQMLAEE 1460
Cdd:COG4717 124 LLQLlplyqeLEALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1461 KNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKR----- 1535
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1536 ------TLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMlVKQVRELEAELEDER 1609
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR-IEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1610 KQRALAVAAKKKMEMdLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEkklkgLEAEI 1689
Cdd:COG4717 361 EELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1690 LQLQEEFAASERARRHAEQERDELADEIANSASGK--SALLDEKRRLEARIAQ 1740
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1053-1209 |
2.79e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.57 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1053 LEKAKRKLDGETTDLQDQIAELQAQIEelkiQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKA 1132
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1133 SRNKAEKQKRDLsEELEALKTELEDTLDTTAAQQE-LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1209
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1248-1425 |
2.79e-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: 47.61 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1248 AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgikfakdAASLESQLQD--TQELLQ 1325
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNvrNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1326 EETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDlgtIEGLEENKKKLLKDMESLS 1405
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELA 169
|
170 180
....*....|....*....|.
gi 2024363113 1406 QRLEEKAMA-YDKLEKTKNRL 1425
Cdd:COG1579 170 AKIPPELLAlYERIRKRKNGL 190
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1264-1618 |
2.82e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1264 LTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA---EKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1340
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELaglTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1341 LEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEK 1420
Cdd:pfam19220 116 KTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1421 TKNRLQQELDDlmvdldhQRQIVSNLEKKqkkFDQMLAEEKNISARYAEERDRAEAEAReketkalSLARALEEALEAKE 1500
Cdd:pfam19220 196 RLAELETQLDA-------TRARLRALEGQ---LAAEQAERERAEAQLEEAVEAHRAERA-------SLRMKLEALTARAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1501 EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE--VNM-----QAMK 1573
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerAEMltkalAAKD 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1574 AQFER------DLQARDEQ----NEEKKRMLVKQVRELEAELEDERKQRALAVAA 1618
Cdd:pfam19220 339 AALERaeeriaSLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1139-1377 |
2.88e-05 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 49.18 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1139 KQKRDLSEELEALKTELEDT----------LDTTAAQQEL-RTKREQEVAE----LKKAIEEETKNHEAQIQE----IRQ 1199
Cdd:pfam07902 78 KSLEEMLSQLKELNLELTDTknsnlwskikLNNNGMLREYhNDTIKTEIVEsaegIATRISEDTDKKLALINEtisgIRR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1200 RHATALEELSEqleqakRFKANLEKNKQGLESDNKELACEVKV-LQQVKAESEHKRKKLDAQVQELTAKVTEG------- 1271
Cdd:pfam07902 158 EYQDADRQLSS------SYQAGIEGLKATMASDKIGLQAEIQAsAQGLSQRYDNEIRKLSAKITTTSSGTTEAyeskldd 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1272 ---------ERLRVELAEKANKL----QNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQEL----------LQEET 1328
Cdd:pfam07902 232 lraeftrsnQGMRTELESKISGLqstqQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQDAEKNyssltqtvkgLQSTV 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1329 R-QKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAK 1377
Cdd:pfam07902 312 SdPNSKLESRITQLAGLIEQKVTRGDVESIIRQSGDSIMLAIKAKLPQSK 361
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1140 |
3.36e-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: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 967 QKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLE------ 1040
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1041 --------------------ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGD 1100
Cdd:COG3883 113 sfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024363113 1101 EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQ 1140
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1053-1214 |
3.70e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1053 LEKAKrkldgeTTDLQDQIAELQAQieelkiqLAKKEEE---LQAALARGDEEAvqknnalkviRELQAQIAELQEDLES 1129
Cdd:PRK09039 71 LERQG------NQDLQDSVANLRAS-------LSAAEAErsrLQALLAELAGAG----------AAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1130 EKASRNKAEKQKRDLSEELEALKTELedtldttaaqqelrtkreQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1209
Cdd:PRK09039 128 EKQVSARALAQVELLNQQIAALRRQL------------------AALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....*
gi 2024363113 1210 EQLEQ 1214
Cdd:PRK09039 190 QELNR 194
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1585-1737 |
4.03e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1585 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE--------AANKARD----EAIKQLRKLQA 1652
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1653 QMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEilqlQEEFAASERARRHAEQERDELADEIANSASGKSALLDEK- 1731
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 2024363113 1732 RRLEAR 1737
Cdd:COG1842 175 EEMEAR 180
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1243-1371 |
4.22e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1243 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAAslESQLQDTQE 1322
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2024363113 1323 LLQEETRqklnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQA 1371
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1054-1310 |
4.56e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1054 EKAKRKLDGETTDLQDQIAELqaqiEELKIQLAKKEEELQAALArgdeeavqknnalkvirelqaQIAELQEDLEsekas 1133
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASL----EELERELEQKAEEAEALLK---------------------EAEKLKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1134 rnkaeKQKRDLSEELEALKTELEDtldttaaqqelrtKREQEVAELKKAIEEETKN-HEAQIQEIRQRHATALEELSEQL 1212
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-------------EAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1213 EQAKRfKANLEKNKQGLESDNKELACEVKVLQ-QVKAESEHKRKKLDAQVQE----LTAKVTEGERLRVELAEKANKLQN 1287
Cdd:PRK00409 617 NKANE-KKEKKKKKQKEKQEELKVGDEVKYLSlGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKKPKT 695
|
250 260 270
....*....|....*....|....*....|...
gi 2024363113 1288 ELDNVSSL----------LEEAEKKGIKFAKDA 1310
Cdd:PRK00409 696 VKPKPRTVsleldlrgmrYEEALERLDKYLDDA 728
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1366-1588 |
4.88e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1366 MLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQivsN 1445
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1446 LEKKQKKFDQMLAE--EKNISARYAEE----RDRAEAEAReketkALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1519
Cdd:COG3883 81 IEERREELGERARAlyRSGGSVSYLDVllgsESFSDFLDR-----LSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1520 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNE 1588
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1392-1928 |
4.96e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1392 ENKKKLLKDMESLSQRLEEKAMAYD-------KLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS 1464
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAkkkslhgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1465 ARYAEERDRAEAEAReketkalslaraleealeakeeFERQNKQLRADMEDLMSSKddvgkNVHELEKSKRTLEQQVEEM 1544
Cdd:TIGR00618 243 AYLTQKREAQEEQLK----------------------KQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1545 RTQLEELEDELQATEDAKLRLEVNMQAM-KAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKK-- 1621
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqh 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1622 -MEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASE 1700
Cdd:TIGR00618 376 tLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1701 RARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAqleeELEEEQSNMELLNERFRKTTLQVdTLNSELAGERSAA 1780
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1781 QKSENARQQLERQNKELKAKLQELEGSVKSkFKATIsTLEAKIAQLEEQLEQEAKEraAANKLVRRTEKKLKEVFMQVED 1860
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRAS-LKEQM-QEIQQSFSILTQCDNRSKE--DIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1861 ERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
921-1137 |
5.10e-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: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 921 EEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKE 1000
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1001 KKlMEDRIAECTSQLAEEE------EKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1074
Cdd:COG3883 95 LY-RSGGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1075 QAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKA 1137
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
965-1106 |
5.58e-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: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 965 ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLK---------NKQEMM 1035
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1036 ITDLEERLK----KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQK 1106
Cdd:COG1579 105 ISDLEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1234-1884 |
5.65e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1234 KELACEVKVLQQVkaeSEHKRKKLDAQVQELTAkvtegerlrVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKdaasl 1313
Cdd:pfam07111 76 RRLEEEVRLLRET---SLQQKMRLEAQAMELDA---------LAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGS----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1314 ESQLQDTQELLQEEtrqklnLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEEN 1393
Cdd:pfam07111 139 QRELEEIQRLHQEQ------LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1394 KKKLLKDMESLSQRLEEKAMA---YDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEE 1470
Cdd:pfam07111 213 LEAQVTLVESLRKYVGEQVPPevhSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1471 RDRAEAEAREKETKALSLARALEEALEAkeeferqnkQLRADMEDLMSSKDDVGKNVHELEK--SKRTLEQQVEEMRTQL 1548
Cdd:pfam07111 293 SDSLEPEFPKKCRSLLNRWREKVFALMV---------QLKAQDLEHRDSVKQLRGQVAELQEqvTSQSQEQAILQRALQD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1549 EELEDELQATEDAKLRLEVNmQAMKAQfeRDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKD 1628
Cdd:pfam07111 364 KAAEVEVERMSAKGLQMELS-RAQEAR--RRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1629 LEGQIEAANK--ARDEAIKQLRKLQAQM--------KDYQRELEEARASRDEIFAQSKesekklkgLEAEILQLQeefaa 1698
Cdd:pfam07111 441 AVRKVHTIKGlmARKVALAQLRQESCPPpppappvdADLSLELEQLREERNRLDAELQ--------LSAHLIQQE----- 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1699 SERARRHAEQERdeladeiansasgksalldekRRLEARIAQLEEELEEEQSNMELLNERfrkttlqvdtLNSELAGERS 1778
Cdd:pfam07111 508 VGRAREQGEAER---------------------QQLSEVAQQLEQELQRAQESLASVGQQ----------LEVARQGQQE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1779 AAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKiaqLEEQLEQEAKERAAANKLVRRT--EKKLKEVFM 1856
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARREQAKAVVSLRQIQHRAtqEKERNQELR 633
|
650 660
....*....|....*....|....*...
gi 2024363113 1857 QVEDERRhadqyKEQMEKANARMKQLKR 1884
Cdd:pfam07111 634 RLQDEAR-----KEEGQRLARRVQELER 656
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1632-1912 |
5.68e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1632 QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKGLEAEILQLQEEfaasERARRHAE 1707
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1708 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnERFRKTTLQVDTLnSELAGERSAAQKSENAR 1787
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEM-EQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1788 QQLERQNKELKAKLQELEgsvKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRT-EKKLKEVFMQ-VEDERRHA 1865
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2024363113 1866 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1912
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1124-1478 |
5.83e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1124 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaiEEETKNheaQIQEIRQrhat 1203
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR---QEERKR---ELERIRQ---- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1204 alEELSEQLEQAKRfkanLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVElaekan 1283
Cdd:pfam17380 368 --EEIAMEISRMRE----LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR------ 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1284 klqneldNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNL--SSRIRQLEEEKNnlqeqqeeeeeaRKN 1361
Cdd:pfam17380 436 -------EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELekEKRDRKRAEEQR------------RKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1362 LEKQMLALQAQLAEakkkvdddlgtieglEENKKKLL-KDMESlsqrlEEKAMAydklEKTKNRLQQELDDLMVDLDHQR 1440
Cdd:pfam17380 497 LEKELEERKQAMIE---------------EERKRKLLeKEMEE-----RQKAIY----EEERRREAEEERRKQQEMEERR 552
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024363113 1441 QIVSNLEK---KQKKFDQMLAEEKNISARYAEERDRAEAEA 1478
Cdd:pfam17380 553 RIQEQMRKateERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
988-1382 |
6.30e-05 |
|
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: 48.43 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 988 LLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLaklKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDL 1067
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL---EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEEL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1068 QDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE-DLESEKASRNKAEKQKRDLSE 1146
Cdd:pfam02463 739 KLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLkAQEEELRALEEELKEEAELLE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1147 ELEALKTELEDTLDTTAAQQELRTKREQEvaELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNK 1226
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQK--LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1227 QGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKF 1306
Cdd:pfam02463 897 EEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1307 AKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1382
Cdd:pfam02463 977 LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLED 1052
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
845-1092 |
6.51e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 845 LQVTRQEEelqaKDEELMKVKEKQTKVEAE-LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 923
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISrMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 924 LHDLESrveEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLkEKKL 1003
Cdd:pfam17380 426 RAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKEL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1004 MEDRIAectsqLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKldgettDLQDQIaeLQAQIEELKI 1083
Cdd:pfam17380 502 EERKQA-----MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM--RKATEERSRL 568
|
....*....
gi 2024363113 1084 QLAKKEEEL 1092
Cdd:pfam17380 569 EAMEREREM 577
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
986-1136 |
6.94e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 986 EILLLEDQNSKFLkekklmEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLkkeektrQELEKAKRKLDGETT 1065
Cdd:PRK09039 67 DLLSLERQGNQDL------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 1066 DLQDQIAELQAQIEELKIQLAKKEEELQAALARGdeeavqknnalkviRELQAQIAELQEDLESEKASRNK 1136
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQLAALEAALDASEKRD--------------RESQAKIADLGRRLNVALAQRVQ 190
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1039-1213 |
7.19e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.33 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1039 LEERLKKEEKTRQELEKakrKLDGETTDLQDQIAElqaQIEELKIQLAKKEEELQAALARGDEEAVQKNNalKVIRELQA 1118
Cdd:pfam01442 2 LEDSLDELSTYAEELQE---QLGPVAQELVDRLEK---ETEALRERLQKDLEEVRAKLEPYLEELQAKLG--QNVEELRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1119 QIAELQEDLEseKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELKKAIEEETKNHEAQ 1193
Cdd:pfam01442 74 RLEPYTEELR--KRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQ 151
|
170 180
....*....|....*....|....
gi 2024363113 1194 ----IQEIRQRHATALEELSEQLE 1213
Cdd:pfam01442 152 lsqrLQELREKLEPQAEDLREKLD 175
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1550-1827 |
7.40e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1550 ELEDELQATEDAKLRLEvnmqAMKAQFERDLQARDEQNEEKKRmlvkqvrELEAELEDERKQRALAVAAKKKMEMDLKDL 1629
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAE-------ARAAKDKDAVAAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1630 EGQIEAANKARdEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEF-----AASERARR 1704
Cdd:PRK05035 509 KAGARPDNSAV-IAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEvdpkkAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1705 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMEllnerfrkTTLQVDTLNSELAGERSAAQKSE 1784
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAE--------PEEPVDPRKAAVAAAIARAKARK 659
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024363113 1785 NARQQLErqnkelkAKLQELEGSVKSKFKATISTLEAKIAQLE 1827
Cdd:PRK05035 660 AAQQQAN-------AEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
976-1122 |
7.52e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 47.75 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 976 AEAKIKKM--EEEILLLEDQNSKFLKEKKLMEDRIA---ECTSQLAEEEEKAKNL--AKLKNKQEMMITDLEERLKKEEK 1048
Cdd:pfam13166 344 LEAKRKDPfkSIELDSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYAGLEK 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1049 TRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDE-EAVQKNNALKVIRELQAQIAE 1122
Cdd:pfam13166 424 AINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKAFGFGELElSFNEEGKGYRIIRKGGSQAAE 498
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1026-1132 |
8.25e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1026 AKLKNKQEMM---ITDLEERLKKEEKTRQELEKAKRKLDGET-TDLQDQIAELQAQIEELKIQLaKKEEELQAALARGDE 1101
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARW-EAEKELIEEIQELKE 478
|
90 100 110
....*....|....*....|....*....|.
gi 2024363113 1102 EAVQKNNalkVIRELQAQIAELQEDLESEKA 1132
Cdd:COG0542 479 ELEQRYG---KIPELEKELAELEEELAELAP 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1203-1406 |
8.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1203 TALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVtegERLRVELAEKA 1282
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1283 NKLQNELDNVSSLLEEAEKKGI-KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKN 1361
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024363113 1362 LEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQ 1406
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
843-1216 |
8.74e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 843 PLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNI-LAEQLQAETElfaeaEEMRArLAAKKQELE 921
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPE-----AELRQ-LNRRRVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 922 EILHDLESrvEEEEERNQILQnekkkmqghiqdleeqldeeegARQKLQLekvtaeakIKKMEEEILLLEDQNskflkek 1001
Cdd:PRK04863 851 RALADHES--QEQQQRSQLEQ----------------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1002 klMEDRIAECTSQLAEEEEKA-------KNLAKLKNKQEMMITDLE--ERLKKE-EKTRQELEKAKRKLDGETTDLQ--- 1068
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDPEqfEQLKQDyQQAQQTQRDAKQQAFALTEVVQrra 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1069 ----DQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvqknnalkviRELQAQIAELQEDLESEKASRNKAEKQKRDL 1144
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQL----------RQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1145 SEELEALKTELEDTLDTTAA------QQELRTKREQEvAELKKAIEEETKNHEAQiqeirQRHATALEE----LSEQLEQ 1214
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARarrdelHARLSANRSRR-NQLEKQLTFCEAEMDNL-----TKKLRKLERdyheMREQVVN 1113
|
..
gi 2024363113 1215 AK 1216
Cdd:PRK04863 1114 AK 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1309-1519 |
9.69e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1309 DAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDL---- 1384
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1385 ---GTIEGLE-----ENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM 1456
Cdd:COG3883 97 rsgGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1457 LAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1519
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1000-1202 |
1.01e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.62 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1000 EKKLMEDRIaectsQLAEEEEKAKNLAklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQ------DQIAE 1073
Cdd:PLN03188 1046 EKKLEQERL-----RWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRCAEELKEAMQmameghARMLE 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1074 LQAQIEELKIQLAKKEEELQAAL---ARGDEEAVQKNNALKVIRELQAQIAELqedleseKASRnkaEKQKRDLSEELEA 1150
Cdd:PLN03188 1115 QYADLEEKHIQLLARHRRIQEGIddvKKAAARAGVRGAESKFINALAAEISAL-------KVER---EKERRYLRDENKS 1184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1151 LKTELEDTLDTTAAQQELRT-------------KR----EQEVAELKKAIEEETKNHEAQIQEIRQRHA 1202
Cdd:PLN03188 1185 LQAQLRDTAEAVQAAGELLVrlkeaeealtvaqKRamdaEQEAAEAYKQIDKLKRKHENEISTLNQLVA 1253
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
851-1348 |
1.07e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 851 EEELQAKDEELMKVKEKQTKVEA-------ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 923
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKshsitlkEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 924 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQ---LEKVTAEAKIKKMEEeillLEDQNSKFLKE 1000
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1001 KKLMEDRIAECT----------SQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1070
Cdd:PRK01156 345 KSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELKIQLAKKEEELQA----------------------------ALARGDEEAVQKNNALKVIRELQAQIAE 1122
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNMEMlngqsvcpvcgttlgeeksnhiinhyneKKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1123 LQEDLESEKASRNKAEKQKrdlseeLEALKTELEDTLDTTAAQQELRTKREQEVAELKKA-IEEETKNHEAQIQEIRQRH 1201
Cdd:PRK01156 505 RKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVIS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1202 ATALEELSEQLEQAKRFKANLEKNKQGLESDnkelacevkvLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEK 1281
Cdd:PRK01156 579 LIDIETNRSRSNEIKKQLNDLESRLQEIEIG----------FPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKL 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1282 ANKLQN------ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1348
Cdd:PRK01156 649 RGKIDNykkqiaEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1666 |
1.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1392 ENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfdqmlaeeknisaryAEER 1471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----------------ALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1472 DRAEAEAREKETKAlSLARALEEALEAKEEFERQNKQLRADMedLMSSKDdvgknVHELEKSKRTLEQQVEEMRTQLEEL 1551
Cdd:COG4942 84 ELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPED-----FLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1552 EDELQatedaklrlevnmqamkaqferDLQARDEQNEEKKrmlvKQVRELEAELEDERKQRALAVAAKKKMemdLKDLEG 1631
Cdd:COG4942 156 RADLA----------------------ELAALRAELEAER----AELEALLAELEEERAALEALKAERQKL---LARLEK 206
|
250 260 270
....*....|....*....|....*....|....*
gi 2024363113 1632 QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARA 1666
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1083-1423 |
1.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1083 IQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTT 1162
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1163 AAQQELRTKREQEVAELKK---AIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACE 1239
Cdd:COG4372 104 ESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1240 VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQD 1319
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1320 TQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLK 1399
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
330 340
....*....|....*....|....
gi 2024363113 1400 DMESLSQRLEEKAMAYDKLEKTKN 1423
Cdd:COG4372 344 QLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1167-1963 |
1.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1167 ELRTKREQEVAELKKAIEEEtknheaqiqeiRQRHatalEELSEQLEQAKRFKANLEknkQGLESDNKELACEVKVLQQV 1246
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAE-----------QYRL----VEMARELAELNEAESDLE---QDYQAASDHLNLVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1247 KAEsehkrKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELdnvssllEEAEKkgikfakDAASLESQLQDTQELLQE 1326
Cdd:PRK04863 348 EKI-----ERYQADLEELEERLEEQNEVVEEADEQQEENEARA-------EAAEE-------EVDELKSQLADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1327 -ETR-----QKLNLSSRIRQL-----------EEEKNNLQEQQEEEEEARKNLEKQMLALQA---QLAEAKKKVDDDLGT 1386
Cdd:PRK04863 409 qQTRaiqyqQAVQALERAKQLcglpdltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1387 IEGLE--ENKKKLLKDMES---LSQRLEEkamaydklektknrLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEk 1461
Cdd:PRK04863 489 VSRSEawDVARELLRRLREqrhLAEQLQQ--------------LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1462 nisaryaeerDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsSKDDVGKNVHEL-----EKSKRT 1536
Cdd:PRK04863 554 ----------DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA-ARAPAWLAAQDAlarlrEQSGEE 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1537 LE--QQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVR-ELEAELEDE----- 1608
Cdd:PRK04863 623 FEdsQDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLNALAERFGgVLLSEIYDDvsled 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1609 ---------RKQRALAV----AAKKKME------MDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARASRD 1669
Cdd:PRK04863 699 apyfsalygPARHAIVVpdlsDAAEQLAgledcpEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQWRYSRFPEV 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1670 EIFAQsKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAS---------GKSALLDEKRRLEARIAQ 1740
Cdd:PRK04863 777 PLFGR-AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALAD 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1741 LEEELEEEQSNMELLNERF--------RKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELkAKLQELEGSVKSKf 1812
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIVSVLQSD- 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1813 KATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTE------------------KKLKEVFMQVEDERrhaDQYKEQMEK 1874
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaaemlaknsdlnEKLRQRLEQAEQER---TRAREQLRQ 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1875 ANARMKQLKRQLEEAEEEATRANASRRKLQRELDDAT-----EANEGLSREVSTLKNRLRRggpitfssSRSGRRQLHIE 1949
Cdd:PRK04863 1011 AQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsGAEERARARRDELHARLSA--------NRSRRNQLEKQ 1082
|
890
....*....|....
gi 2024363113 1950 GASLELSDDDAESK 1963
Cdd:PRK04863 1083 LTFCEAEMDNLTKK 1096
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
802-1237 |
1.53e-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: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 802 ARKAFAKKQQQLSALKILQRNCAAYLKLR-----------HWQWWRVFTKVKpLLQ--VTRQEEELQAKDEELMKVKEKQ 868
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 869 TKV-----------------------------EAELEEMERKHQQLLEEKNILAEQLQAETELFAE----AEEMRARLAA 915
Cdd:COG4913 319 DALreeldeleaqirgnggdrleqlereierlERELEERERRRARLEALLAALGLPLPASAEEFAAlraeAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 916 KKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEeegARQKL--QLEKVTAEAKIK------KMEEEI 987
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA---LRDALaeALGLDEAELPFVgelievRPEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 988 ---------------LLLEDQN-SKFLK-------EKKLMEDRIAECTSQLAEEEEKAKNLA-KLKNK---------QEM 1034
Cdd:COG4913 476 wrgaiervlggfaltLLVPPEHyAAALRwvnrlhlRGRLVYERVRTGLPDPERPRLDPDSLAgKLDFKphpfrawleAEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1035 ------MITDLEERLKKEEK--TRQEL--------EKAKRKLDGET-----------TDLQDQIAELQAQIEELKIQLAK 1087
Cdd:COG4913 556 grrfdyVCVDSPEELRRHPRaiTRAGQvkgngtrhEKDDRRRIRSRyvlgfdnraklAALEAELAELEEELAEAEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1088 KEEELQAALARGD--EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKqkrdLSEELEALKTELEDTLDTTAAQ 1165
Cdd:COG4913 636 LEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDEL 711
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1166 QELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQL---EQAKRFKANLEKNKQGLESDNKELA 1237
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAE 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1237-1452 |
1.60e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1237 ACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQ 1316
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1317 LQDTQELLQEETRQKLNLSSRIRQLE--------EEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTie 1388
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1389 gLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1452
Cdd:COG3883 159 -LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1028-1459 |
1.61e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.39 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1028 LKNKQEMMITDLEERlKKEEKTR---QELEKAKR-KLDGETtdlQDQIAELQAQIEELK-IQLAKKEEELQAAlargdEE 1102
Cdd:pfam06160 4 LRKKIYKEIDELEER-KNELMNLpvqEELSKVKKlNLTGET---QEKFEEWRKKWDDIVtKSLPDIEELLFEA-----EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1103 AVQKNN---ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldttaAQQELRTKREQeVAEL 1179
Cdd:pfam06160 75 LNDKYRfkkAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRE------LRKTLLANRFS-YGPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1180 KKAIEEETKNHEAQIQEirqrhataLEELSEQ--LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVkaesehkrkkL 1257
Cdd:pfam06160 148 IDELEKQLAEIEEEFSQ--------FEELTESgdYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE----------L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1258 DAQVQELTAKVTEGER-----LRVELAEKANKLQNELDNVSSLLEEAEKKgiKFAKDAASLESQLQDTQELLQEETRQKL 1332
Cdd:pfam06160 210 PDQLEELKEGYREMEEegyalEHLNVDKEIQQLEEQLEENLALLENLELD--EAEEALEEIEERIDQLYDLLEKEVDAKK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1333 NLSSRIRQLEEEKNNLqeqqeeeeearknlEKQMLALQAQLAEAKKK---VDDDLGTIEGLEENKKKLLKDMESLSQRLE 1409
Cdd:pfam06160 288 YVEKNLPEIEDYLEHA--------------EEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDEIVERLE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1410 EKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1459
Cdd:pfam06160 354 EKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
965-1214 |
1.61e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 965 ARQKLQLEKVTAE-AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTS-QLAEEEEkaknlAKLKNKQEmmitdleeR 1042
Cdd:COG0497 151 AGLEELLEEYREAyRAWRALKKELEELRADEAERARELDLLRFQLEELEAaALQPGEE-----EELEEERR--------R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1043 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELkiqlAKKEEELQAALARGDEEAVQknnalkvIRELQAQIAE 1122
Cdd:COG0497 218 LSNAEKLREALQEALEALSGGEGGALDLLGQALRALERL----AEYDPSLAELAERLESALIE-------LEEAASELRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1123 LQEDLESEKASRNKAE---------KQK-RDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETknheA 1192
Cdd:COG0497 287 YLDSLEFDPERLEEVEerlallrrlARKyGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----E 362
|
250 260
....*....|....*....|...
gi 2024363113 1193 QIQEIRQRHATALEE-LSEQLEQ 1214
Cdd:COG0497 363 KLSAARKKAAKKLEKaVTAELAD 385
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
965-1132 |
1.72e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 965 ARQKLQlekvTAEAKIKKMEEE--ILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEEr 1042
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1043 LKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQIEELKIQLAKKEEELQAAL------ARGDEEAVQK-----NN 1108
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASLeaeleaLQAREASLQAqlaqlEA 341
|
170 180
....*....|....*....|....
gi 2024363113 1109 ALKVIRELQAQIAELQEDLESEKA 1132
Cdd:COG3206 342 RLAELPELEAELRRLEREVEVARE 365
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
852-1267 |
1.78e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.86 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 852 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFaeaeemRARLAAKKQELEEilhdlesrv 931
Cdd:pfam15818 14 EELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVF------KKQLQMKMCALEE--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 932 eeeeernqilqnEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEI---LLLEDQNSKFLKEkklMEDRI 1008
Cdd:pfam15818 79 ------------EKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLqlhLLAKEDHHKQLNE---IEKYY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1009 AECTSQLA---EEEEKA-----------KNLAKLKNKQEMMITDLEERLKK-----------------EEKT-----RQE 1052
Cdd:pfam15818 144 ATITGQFGlvkENHGKLeqnvqeaiqlnKRLSALNKKQESEICSLKKELKKvtsdlikskvtcqykmgEENInltikEQK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1053 LEKAKRKLDGEtTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRElQAQIAELQEDLESEKA 1132
Cdd:pfam15818 224 FQELQERLNME-LELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKE-NNQTLERDNELQREKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1133 SRNKA---------EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHAt 1203
Cdd:pfam15818 302 KENEEkflnlqnehEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENS- 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1204 alEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAK 1267
Cdd:pfam15818 381 --EMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQVLEKSFK 442
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1529-1740 |
1.82e-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: 45.99 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1529 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamKAQferdlQARDEQNEEKKrmlvkQVRELEAELEDE 1608
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK----------QAE-----QAAKQAEEKQK-----QAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1609 RKQRALAVAAKKKMEmdlkdlegqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKGLEAE 1688
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024363113 1689 ILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
846-1200 |
2.11e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.27 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 846 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLAAKKQELEE 922
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 923 IlHDLESRVEEEEERNqilqnekKKMQGHIQDLEEQLDEEEGARQKL-QLEKVTAEAKIKKMEEEILLLEDQNSKFLKEK 1001
Cdd:pfam05557 199 I-PELEKELERLREHN-------KHLNENIENKLLLKEEVEDLKRKLeREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1002 KLMEDRIAECTSQLAEEEEKAKNLAKLKNkqemmiTDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEEL 1081
Cdd:pfam05557 271 TGLNLRSPEDLSRRIEQLQQREIVLKEEN------SSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1082 --KIQLAKKEEE-LQAALARGDEEAVQKN---NALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL 1155
Cdd:pfam05557 345 qrRVLLLTKERDgYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024363113 1156 eDTLDTTAAQQELRTKREqEVAELKKAIEEetknHEAQIQEIRQR 1200
Cdd:pfam05557 425 -QALRQQESLADPSYSKE-EVDSLRRKLET----LELERQRLREQ 463
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1625-1856 |
2.18e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1625 DLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIfaqskeSEKKLK-GLEAEILQLQEEFAASERAR 1703
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL------EAAALQpGEEEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1704 RHAEQERDELADEIANSASgksaLLDE-KRRLEaRIAQleeeleeEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQK 1782
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEF 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1783 SENARQQLE-RQN--------------------KELKAKLQELEGSvkskfKATISTLEAKIAQLEEQLEQEAKE----- 1836
Cdd:COG0497 294 DPERLEEVEeRLAllrrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaar 368
|
250 260
....*....|....*....|
gi 2024363113 1837 RAAANKLVRRTEKKLKEVFM 1856
Cdd:COG0497 369 KKAAKKLEKAVTAELADLGM 388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1114-1302 |
2.29e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1114 RELQAQIAELQEdLESEKAsrnKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQevaelKKAIEEETKNHEAQ 1193
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELA------ALEARLEAAKTE-----LEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1194 IQEIRQRhataLEELSEQLEQAKRFK--ANLEKNKQGLESDNKELAcevKVLQQVKAESEHKRKKLDAQVQELTAKVTEG 1271
Cdd:COG1579 68 IEEVEAR----IKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|.
gi 2024363113 1272 ERLRVELAEKANKLQNELDNVSSLLEEAEKK 1302
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
844-1291 |
2.38e-04 |
|
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: 46.37 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 844 LLQVTRQEEELQAKDEELMKVKEKQTKVEAEL-----------EEMERKHQQLLEEKNILAEqlqAETELFAEAEEMRAR 912
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAGTLLHF 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 913 LAAKKQELE---------EILH--DLESRVEEEEERNQI------LQNEKKKMQGHIQDLEEQLDEEEGARQKLQlekvT 975
Cdd:pfam12128 540 LRKEAPDWEqsigkvispELLHrtDLDPEVWDGSVGGELnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQ----S 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 976 AEAKIKKMEEEILLLedqNSKFLKEKKLMEDriAECTSQLAEEEEKAKNLAKlKNKQEMMITDLEERLKKEEKTRQELEK 1055
Cdd:pfam12128 616 AREKQAAAEEQLVQA---NGELEKASREETF--ARTALKNARLDLRRLFDEK-QSEKDKKNKALAERKDSANERLNSLEA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1056 AKRKLDgetTDLQDQIAELQAQIEELKIQLAKK----EEELQAALARGDEEAVQKNNALKvirelqAQIAELQEDLESEK 1131
Cdd:pfam12128 690 QLKQLD---KKHQAWLEEQKEQKREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDL 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1132 ASRNKAEKQKRDLSEELEALKTELEDTldttaaqqelrTKREQEVAELKKAIEE----ETKNHEAQIQEIRQRHATALEE 1207
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQ 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1208 LSEQLEQAKRFKANLEKNKQGLESDNKELACEvkvLQQVKAESEH-KRKKLDAQVQELTAKVTE----GERLRVELAEKA 1282
Cdd:pfam12128 830 LARLIADTKLRRAKLEMERKASEKQQVRLSEN---LRGLRCEMSKlATLKEDANSEQAQGSIGErlaqLEDLKLKRDYLS 906
|
....*....
gi 2024363113 1283 NKLQNELDN 1291
Cdd:pfam12128 907 ESVKKYVEH 915
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1033-1167 |
2.50e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.61 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1033 EMMITDLEERLKKE--EKTRQELEKAKRKLDGETTDLQD------------QIAELQAQIEELKIQLAKKEEELQAALAR 1098
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1099 GDEEAVQknnalkvIRELQAQIAELQEDLESEKA--SRNKAEKQKRDLSEELEALKTEL---EDTLDTTAAQQE 1167
Cdd:COG3524 244 LSPNSPQ-------VRQLRRRIAALEKQIAAERArlTGASGGDSLASLLAEYERLELERefaEKAYTSALAALE 310
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1076-1194 |
2.84e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1076 AQIEELKIQLAKKEEELQAALARGDEEAVQKnnalkvIRELQAQIAELQEDLESEKAsRNKAEKQkrdLSEELEALKTEL 1155
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALKA-RWEAEKE---LIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024363113 1156 EDTLDTTAAQQELRTKREQEVAELKKAIEEE-TKNHEAQI 1194
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAEV 520
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1681-1840 |
3.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1681 KLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLnerfr 1760
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1761 KTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEG---SVKSKFKATISTLEAKIAQLEEQLEQEAKER 1837
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAelaELEAELEEKKAELDEELAELEAELEELEAER 165
|
...
gi 2024363113 1838 AAA 1840
Cdd:COG1579 166 EEL 168
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1529-1667 |
3.11e-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: 45.05 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1529 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQ-NEEKKRMLVKQVRELEAELED 1607
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1608 ERKqrALAVAAKKKMEmDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARAS 1667
Cdd:cd22656 191 LNE--EYAAKLKAKID-ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
980-1302 |
3.26e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 980 IKKMEEEILLLE-------DQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMiTDLEERLKKEEKTRQE 1052
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEIL-EEQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1053 LEKA-KRKLDGETTDLQDQIAELQAQIEELKIQLA--KKEEELQAALARgdEEAVQKNNalkvIRELQAQIAELQEDLes 1129
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKLEK--ERSLLDAS----LRELESKFIVAQEDV-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1130 EKASRNKAEKqkrdLSEELEalktELEDTLDTTAAQQelrtkrEQEVAELKkaieeetknheaQIQEIRQRhataLEELS 1209
Cdd:PLN02939 288 SKLSPLQYDC----WWEKVE----NLQDLLDRATNQV------EKAALVLD------------QNQDLRDK----VDKLE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1210 EQLEQAKRFKANLEKnkqglesdnkelaceVKVLQQ-VKAESEHkrkkLDAQVQELTAKVTEGERLRVELAekanklqne 1288
Cdd:PLN02939 338 ASLKEANVSKFSSYK---------------VELLQQkLKLLEER----LQASDHEIHSYIQLYQESIKEFQ--------- 389
|
330
....*....|....
gi 2024363113 1289 lDNVSSLLEEAEKK 1302
Cdd:PLN02939 390 -DTLSKLKEESKKR 402
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1529-1930 |
3.34e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1529 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQARDEQNEEKKRMLVKQVRELEAELEDE 1608
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1609 RKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQlrklqaqmkdyqreleearASRDEIFAQSKESEKKLKGLEA- 1687
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-------------------TSIREISCQQHTLTQHIHTLQQq 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1688 -EILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQv 1766
Cdd:TIGR00618 388 kTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1767 dtlnsELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvKSKFKATISTLEAKIAQLEEqLEQEAKERAAANKLVRR 1846
Cdd:TIGR00618 467 -----SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1847 TEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeeeATRANASRRKLQRELDDATEANEGLSREVSTLKN 1926
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
....
gi 2024363113 1927 RLRR 1930
Cdd:TIGR00618 613 EQHA 616
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1600-1846 |
3.48e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1600 ELEAELeDERKQRALAVAAKKKMEMDLK---DLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1676
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1677 ES------EKKLKGLEAEILQLQEEFA-----------ASERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1735
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAeynsqlvslqtQPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1736 ARIAQleeeleeeqsnMELLNErFRKTTLQVDTLNSELaGERSAAQKSENArQQLERQnkelkakLQELEGSVKSKfkat 1815
Cdd:PRK11281 199 AEQAL-----------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQ-------LQLLQEAINSK---- 253
|
250 260 270
....*....|....*....|....*....|.
gi 2024363113 1816 isTLEAKIAQLEEQLEQEAKERAAANKLVRR 1846
Cdd:PRK11281 254 --RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
999-1382 |
3.87e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 45.44 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 999 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKE------EKTRQELEKAKRKLDGETTDLQDQIA 1072
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkkikRKKNSALSEALNGFKYEANFKSRLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1073 ELQAQIEELKIQLAkkEEELQAALARGDEEAVQKnNALKVIRELQAQIAELQEDLESEKASRNKA--EKQKR-DLSEELE 1149
Cdd:pfam13166 169 EIEKDNFNAGVLLS--DEDRKAALATVFSDNKPE-IAPLTFNVIDFDALEKAEILIQKVIGKSSAieELIKNpDLADWVE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1150 ALKTELEDTLDTTA-AQQELRTKReqeVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLeqakrfkanleknKQG 1228
Cdd:pfam13166 246 QGLELHKAHLDTCPfCGQPLPAER---KAALEAHFDDEFTEFQNRLQKLIEKVESAISSLLAQL-------------PAV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1229 LESDNKELACEVKVlQQVKAESEHKRKKLDAQVQELTAKVTEGERlRVELAEKANKLQNELDNVSSLLEEAEK---KGIK 1305
Cdd:pfam13166 310 SDLASLLSAFELDV-EDIESEAEVLNSQLDGLRRALEAKRKDPFK-SIELDSVDAKIESINDLVASINELIAKhneITDN 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1306 FAKDAASLESQLQdtQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1382
Cdd:pfam13166 388 FEEEKNKAKKKLR--LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
794-1382 |
3.89e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 794 QAVCRGYLARKAFAKKQQQLSALKILQRncAAYLKLrhwQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEA 873
Cdd:PRK10246 261 RRQQALQQALAAEEKAQPQLAALSLAQP--ARQLRP---HWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 874 eleemeRKHQQLLEEKNILAEQLQAETE-------------LFAEAEEMRARLAAKKQELEEILHDLES----------- 929
Cdd:PRK10246 336 ------KQSAELQAQQQSLNTWLAEHDRfrqwnnelagwraQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltad 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 930 ---RVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEillLEDQNSKFLKEKKL--M 1004
Cdd:PRK10246 410 evaAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQR---YKEKTQQLADVKTIceQ 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1005 EDRIAECTSQLAeeeekaknlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQIEEL 1081
Cdd:PRK10246 487 EARIKDLEAQRA----------QLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDAlekEVKKLGEEGAALRGQLDAL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1082 KIQLAKKEEELQAALArgDEEAVQKN-----NALKVIRELQAQIA---------ELQEDLESEK----ASRNKAEKQKRD 1143
Cdd:PRK10246 557 TKQLQRDESEAQSLRQ--EEQALTQQwqavcASLNITLQPQDDIQpwldaqeehERQLRLLSQRhelqGQIAAHNQQIIQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1144 LSEELEALKTELEDTLDTTA-------AQQELRTKREQEVAELKKaieeetknHEAQIQEIRQRHAtALEELSEQLEQAK 1216
Cdd:PRK10246 635 YQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSWQQ--------RQNELTALQNRIQ-QLTPLLETLPQSD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1217 RFKANLE----KNKQGLESDNKELACEVKVLQQvkAESEHKRKKLDAQVQ---ELTAKVTEG----------ERLRVELA 1279
Cdd:PRK10246 706 DLPHSEEtvalDNWRQVHEQCLSLHSQLQTLQQ--QDVLEAQRLQKAQAQfdtALQASVFDDqqaflaalldEETLTQLE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1280 EKANKLQNELDNVSSLLEEAEK----------KGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlq 1349
Cdd:PRK10246 784 QLKQNLENQRQQAQTLVTQTAQalaqhqqhrpDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNR---- 859
|
650 660 670
....*....|....*....|....*....|...
gi 2024363113 1350 eqqeeeeearknleKQMLALQAQLAEAKKKVDD 1382
Cdd:PRK10246 860 --------------QQQQALMQQIAQATQQVED 878
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1450-1928 |
4.07e-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: 45.81 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1450 QKKFDQMLAEEKNISAryaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQnkQLRADMEDLMSSKDDVGKNVHE 1529
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD--QITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1530 LEKSKRTLeQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDER 1609
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1610 KQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEarasrdEIFAQSKESEKKLKGLEAEI 1689
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL------DGFERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1690 LQLQEEFAaserarRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMellneRFRKTTLQVDTL 1769
Cdd:TIGR00606 400 IERQEDEA------KTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL-----KFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1770 NSELAGERSAAQKSENARQQLERQNKELKAKLQElEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1849
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKE-VKSLQNE-KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1850 KLKEVFmqvEDERRHADQYKEQMEKANARmKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:TIGR00606 547 KDEQIR---KIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
851-1185 |
4.21e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.23 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 851 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLleEKNILA-------------EQLQAETELFAEAEEMRAR---LA 914
Cdd:pfam06160 99 EEDIKQILEELDELLESEEKNREEVEELKDKYREL--RKTLLAnrfsygpaideleKQLAEIEEEFSQFEELTESgdyLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 915 AKK--QELEEILHDLESRVEEEEERNQILQNEKKKmqghiqdleeqldeeegarqklQLEKVtaEAKIKKMEEEILLLED 992
Cdd:pfam06160 177 AREvlEKLEEETDALEELMEDIPPLYEELKTELPD----------------------QLEEL--KEGYREMEEEGYALEH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 993 QNskFLKEKKLMEDRIAECTSQLA--EEEEKAKNLAKLKNKqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1070
Cdd:pfam06160 233 LN--VDKEIQQLEEQLEENLALLEnlELDEAEEALEEIEER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELK--IQLAKKEEELQAALArgdeeavqknnalKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL 1148
Cdd:pfam06160 307 NKELKEELERVQqsYTLNENELERVRGLE-------------KQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQL 373
|
330 340 350
....*....|....*....|....*....|....*....
gi 2024363113 1149 EALKTELEDTLDTTAA--QQELRTKreQEVAELKKAIEE 1185
Cdd:pfam06160 374 EEIEEEQEEFKESLQSlrKDELEAR--EKLDEFKLELRE 410
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1065-1236 |
4.34e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.00 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1065 TDLQDQIAELQAQIEELKIQLakkeEELQAALARGDEEAVQKNNALkvIRELQAQIAELQEDLESEKASRNKAEKQKRDL 1144
Cdd:pfam08614 10 NRLLDRTALLEAENAKLQSEP----ESVLPSTSSSKLSKASPQSAS--IQSLEQLLAQLREELAELYRSRGELAQRLVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1145 SEELEALKTELEdtldttAAQQELRtKREQEVAELkkaiEEETKNHEAQIQEIRQRHATALEE---LSEQLEQAkrfkan 1221
Cdd:pfam08614 84 NEELQELEKKLR------EDERRLA-ALEAERAQL----EEKLKDREEELREKRKLNQDLQDElvaLQLQLNMA------ 146
|
170
....*....|....*
gi 2024363113 1222 lEKNKQGLESDNKEL 1236
Cdd:pfam08614 147 -EEKLRKLEKENREL 160
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1078-1216 |
4.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1078 IEELKIQLAKKEEELQAalargdEEAVQKNNALKVIRELQAQ--IAELQEDLESE-KASRNKAEKQKRDLSEELEALKTE 1154
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1155 LEDTldttaaqqelrTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSE----QLEQAK 1216
Cdd:PRK12704 102 LELL-----------EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisglTAEEAK 156
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1113-1371 |
5.01e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1113 IRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaieEETKNHEA 1192
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK----EERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1193 QIQEIRQRhATALEELSEQLEQAKRFKANLEKNKQGLE----------SDNKELACEVKVLQQ---VKAESEHKRKKLDA 1259
Cdd:COG1340 86 KLNELREE-LDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspEEEKELVEKIKELEKeleKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1260 QVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEkkgiKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIR 1339
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD----ELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270
....*....|....*....|....*....|..
gi 2024363113 1340 QLEEEKNNLQEQQEEEEEARKNLEKQMLALQA 1371
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
866-1142 |
5.15e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 866 EKQTKVEAELEEMERKHQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEK 945
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRD---ELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 946 KKMQGHIQDLEEQLDEEEGARQKLQlEKVTAEAKIKKMEEEILLLED--QNSKFLKEKklmEDRIAECTSQLAEEEEKAK 1023
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELA-ELNKAGGSIDKLRKEIERLEWrqQTEVLSPEE---EKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1024 NLAKLKNKqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEA 1103
Cdd:COG1340 154 KALEKNEK----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 2024363113 1104 VQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKR 1142
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1340-1886 |
5.32e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1340 QLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEenkKKLLKDMESLSQRLEEkAMAYDKLE 1419
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALREQAEL-NRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1420 KTKNRLQQELDDLMVDLdhqRQIVSNLekkqkkfdqmlaeeKNISARYAEERDRAEAEAREKETKalslaraleealeak 1499
Cdd:pfam05557 86 EALNKKLNEKESQLADA---REVISCL--------------KNELSELRRQIQRAELELQSTNSE--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1500 eeferqnkqlradMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRT---QLEELEDELQATEDAKLRLEvNMQAMKAQF 1576
Cdd:pfam05557 134 -------------LEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVK-NSKSELARI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1577 ---ERDLQARDEQNE------EKKRMLVKQVRELEAELEDERKQRALAVA---AKKKMEMDLK----------------- 1627
Cdd:pfam05557 200 pelEKELERLREHNKhlneniENKLLLKEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQswvklaqdtglnlrspe 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1628 DLEGQI------EAANKARDEAI-KQLRKLQAQMKDYQRELEEARAsrdeifaQSKESEKKLKGLEAEILQLQEEFAASE 1700
Cdd:pfam05557 280 DLSRRIeqlqqrEIVLKEENSSLtSSARQLEKARRELEQELAQYLK-------KIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1701 RARRHAEQERDELADEIANSASGKSaLLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAA 1780
Cdd:pfam05557 353 KERDGYRAILESYDKELTMSNYSPQ-LLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1781 QKSENARQQLERQnkELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAKeraaanklvrrtekKLKEVFMQVED 1860
Cdd:pfam05557 432 SLADPSYSKEEVD--SLRRKLETLELER-QRLREQKNELEMELERRCLQGDYDPK--------------KTKVLHLSMNP 494
|
570 580
....*....|....*....|....*.
gi 2024363113 1861 ERRHADQYKEQMEKANARMKQLKRQL 1886
Cdd:pfam05557 495 AAEAYQQRKNQLEKLQAEIERLKRLL 520
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1772-1884 |
5.45e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1772 ELAGERSAAQKSENARQ--QLERQNKELKAKLQELEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1849
Cdd:COG2433 398 EREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|....*
gi 2024363113 1850 KLKEvfmqVEDERRHADQYKEQMEkanaRMKQLKR 1884
Cdd:COG2433 477 LERE----LEEERERIEELKRKLE----RLKELWK 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1597-1787 |
5.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1597 QVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1676
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1677 ESEKKLKGLEA--------------------------EILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDE 1730
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1731 KRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENAR 1787
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1013-1620 |
5.68e-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: 45.33 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1013 SQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQlAKKEEEL 1092
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAA 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1093 QAALARGDEeavQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALkteledTLDTTAAQQELRTKR 1172
Cdd:COG3096 608 QDALERLRE---QSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL------SQPGGAEDPRLLALA 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1173 EQEVAELKKAIEEETKNHEAQIQEIR---QRHATALEELS---EQLEQAKRFKANL---EKNKQG-----LESDNKELAC 1238
Cdd:COG3096 679 ERLGGVLLSEIYDDVTLEDAPYFSALygpARHAIVVPDLSavkEQLAGLEDCPEDLyliEGDPDSfddsvFDAEELEDAV 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1239 EVKVLQQVKAESEHK------RKKLDAQVQELTAkvtEGERLRVELAEKA---NKLQNELDNVSSLLeeAEKKGIKFAKD 1309
Cdd:COG3096 759 VVKLSDRQWRYSRFPevplfgRAAREKRLEELRA---ERDELAEQYAKASfdvQKLQRLHQAFSQFV--GGHLAVAFAPD 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1310 AAslesqlqdtqELLQEetrqklnLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGT-IE 1388
Cdd:COG3096 834 PE----------AELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADrLE 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1389 GLEENKKKLLKDMESLSQ------RLEEKAMA-------YDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK-KQKKFD 1454
Cdd:COG3096 897 ELREELDAAQEAQAFIQQhgkalaQLEPLVAVlqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfSYEDAV 976
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1455 QMLAEEKNISARYAEERDRAEAEAREKETKAlslaraleealeakeefeRQNKQLRADMEDLMSSkddvgknvheLEKSK 1534
Cdd:COG3096 977 GLLGENSDLNEKLRARLEQAEEARREAREQL------------------RQAQAQYSQYNQVLAS----------LKSSR 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1535 RTLEQQVEEMRTQLEELedELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRM------LVKQVRELEAELEDE 1608
Cdd:COG3096 1029 DAKQQTLQELEQELEEL--GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCeaemdsLQKRLRKAERDYKQE 1106
|
650
....*....|..
gi 2024363113 1609 RKQralAVAAKK 1620
Cdd:COG3096 1107 REQ---VVQAKA 1115
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1128-1377 |
6.10e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1128 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRT-KREQEVAELkkaiEEETKNHEAQIQEIRQRhataLE 1206
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEfRQKNGLVDL----SEEAKLLLQQLSELESQ----LA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1207 ELSEQLEQAKRFKANLEKNKQGLESDNKELAcEVKVLQQVKAEsehkRKKLDAQVQELTAKVTEGERLRVELAEKANKLQ 1286
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELL-QSPVIQQLRAQ----LAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1287 NELDnvssllEEAEKKGIKFAKDAASLESQLQdtqeLLQEETRQKLNLSSRIRQLEEEKNNLQEQqeeeeeaRKNLEKQM 1366
Cdd:COG3206 305 AQLQ------QEAQRILASLEAELEALQAREA----SLQAQLAQLEARLAELPELEAELRRLERE-------VEVARELY 367
|
250
....*....|.
gi 2024363113 1367 LALQAQLAEAK 1377
Cdd:COG3206 368 ESLLQRLEEAR 378
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
801-1284 |
6.13e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 801 LARKAFAKKQQQLSALKILQRNCAAYlklrhwqwwrVFTKVKPllQVTRQEEELQAKD--EELMKVKEKQTKVEAELEEM 878
Cdd:pfam07111 201 LLRKQLSKTQEELEAQVTLVESLRKY----------VGEQVPP--EVHSQTWELERQEllDTMQHLQEDRADLQATVELL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 879 ERKHQQLleeKNILAEQLQAETELFAEAEEMRARLAAKKQEL-----EEIL--------HDLESRVEEEEERNQILQ--- 942
Cdd:pfam07111 269 QVRVQSL---THMLALQEEELTRKIQPSDSLEPEFPKKCRSLlnrwrEKVFalmvqlkaQDLEHRDSVKQLRGQVAElqe 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 943 ------NEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIaecTSQLA 1016
Cdd:pfam07111 346 qvtsqsQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWL---ETTMT 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1017 EEEEKAKNLAKLKN------KQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEE 1090
Cdd:pfam07111 423 RVEQAVARIPSLSNrlsyavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAH 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1091 ELQAALARGDEEA-VQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELedtldttAAQQELR 1169
Cdd:pfam07111 503 LIQQEVGRAREQGeAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL-------TQQQEIY 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1170 TKREQE-VAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELAceVKVLQQVKA 1248
Cdd:pfam07111 576 GQALQEkVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEG--QRLARRVQE 653
|
490 500 510
....*....|....*....|....*....|....*.
gi 2024363113 1249 ESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1284
Cdd:pfam07111 654 LERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDK 689
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
978-1193 |
6.76e-04 |
|
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: 43.44 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 978 AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAecTSQLAEEEEKAKNLAKLKnkqemmITDLEERLKKEEKTRQELEKAK 1057
Cdd:pfam12795 30 DKIDASKQRAAAYQKALDDAPAELRELRQELA--ALQAKAEAAPKEILASLS------LEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1058 RKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV-IRELQAQIAELQEDLESEKASRNK 1136
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAeLAALKAQIDMLEQELLSNNNRQDL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1137 AEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELKKAIEEETKNHEAQ 1193
Cdd:pfam12795 182 LKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1534-1688 |
6.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1534 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQARDEQNEEKKRMLVKQVRELEAELED 1607
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1608 ERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKg 1684
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 2024363113 1685 LEAE 1688
Cdd:PRK12704 184 EEAD 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
974-1204 |
7.23e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 974 VTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKaknLAKLKNKQEMMITDLEERLKKEEKTRQEL 1053
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1054 EKAKRKL--DGETTD-----------------------LQDQIAELQAQIEELKIQLAKKEEELQAalargdeeavQKNN 1108
Cdd:COG3883 89 GERARALyrSGGSVSyldvllgsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEA----------KLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1109 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETK 1188
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250
....*....|....*.
gi 2024363113 1189 NHEAQIQEIRQRHATA 1204
Cdd:COG3883 239 AAAAAASAAGAGAAGA 254
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1395-1854 |
7.25e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1395 KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM-----LAEEKNISARYAE 1469
Cdd:pfam05622 3 SEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLqkqleQLQEENFRLETAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1470 ERDRAEAEAREKETKALSLaraleealeakeeferQNKQLRADMEDLMSSKDDVGKNVHELEKSKRtLEQQVEEMRTQLE 1549
Cdd:pfam05622 83 DDYRIKCEELEKEVLELQH----------------RNEELTSLAEEAQALKDEMDILRESSDKVKK-LEATVETYKKKLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1550 ELEDelqATEDAKLRLEVNMQAM--KAQFERDLQ---ARDEQNEEKKRmlvkQVRELEAELEDERKQralavaaKKKMEM 1624
Cdd:pfam05622 146 DLGD---LRRQVKLLEERNAEYMqrTLQLEEELKkanALRGQLETYKR----QVQELHGKLSEESKK-------ADKLEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1625 DLKDLEGQIEAANKARD----------EAIKQLRKLQAQmkdyQRELEEARASRDEIFAQSKESEKKLKGLE--AEILQL 1692
Cdd:pfam05622 212 EYKKLEEKLEALQKEKErliierdtlrETNEELRCAQLQ----QAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1693 QEEFAASERARRHAEQERDELAdeiansasgkSALLDEKRRleariaqleeELEEEQSNMELLNERFRKTTLQVDTLNSE 1772
Cdd:pfam05622 288 QHENKMLRLGQEGSYRERLTEL----------QQLLEDANR----------RKNELETQNRLANQRILELQQQVEELQKA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1773 LAGERSAAQKSENARQQLERQNKELK---AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1849
Cdd:pfam05622 348 LQEQGSKAEDSSLLKQKLEEHLEKLHeaqSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVE 427
|
....*
gi 2024363113 1850 KLKEV 1854
Cdd:pfam05622 428 KAKSV 432
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1009-1152 |
7.39e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1009 AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELqaqiEELKIQLAKK 1088
Cdd:PRK12705 35 AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL----DNLENQLEER 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1089 EEELQAALARGDEEAVQKNNALKVIRELQAQ------IAELQEDLESEKASRNKAEKQKRDLSEELEALK 1152
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1640-1805 |
7.59e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1640 RDEAIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkGLEAEILQLQEEFAASERARRHAEQERDELADEiAN 1719
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1720 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNErfrkttlQVDTLNSELAGERSAAQKSENARQQLERQ------ 1793
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 2024363113 1794 --NKELKAKLQELE 1805
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
974-1082 |
7.91e-04 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 44.56 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 974 VTAEAKIKKMEEEILLledQNSKFLKEKKlmEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKtrQEL 1053
Cdd:pfam00012 480 VSAKDKGTGKEQEITI---EASEGLSDDE--IERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGD--KVP 552
|
90 100 110
....*....|....*....|....*....|....
gi 2024363113 1054 EKAKRKLDGETTDL-----QDQIAELQAQIEELK 1082
Cdd:pfam00012 553 EAEKSKVESAIEWLkdeleGDDKEEIEAKTEELA 586
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1000-1382 |
8.25e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.25 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1000 EKKLMEDRIAECTSQLAEEEEkaknlAKLKNKQEMMIT---------DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1070
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEA-----AKAQVLEELESTkrlieelklNLERAQTEEAQAKQDSELAKLRVEEMEQGIADE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 I-AELQAQIEELKIQLAKKEEELQAAlaRGDEEAVQKNNALKVI-RELQAQIAElqedlESEKASRnKAEKQKRDLSEEL 1148
Cdd:pfam05701 118 AsVAAKAQLEVAKARHAAAVAELKSV--KEELESLRKEYASLVSeRDIAIKRAE-----EAVSASK-EIEKTVEELTIEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1149 EALKTELEdtldttAAQQELRTKREQEVAeLKKAIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKANLEKNKQG 1228
Cdd:pfam05701 190 IATKESLE------SAHAAHLEAEEHRIG-AALAREQDKLNWEKELKQAEEE----LQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1229 LESDNKELACEVkvlqqvkaesehkrkklDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA--EKKGIKF 1306
Cdd:pfam05701 259 LLDLKAELAAYM-----------------ESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAkdEVNCLRV 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1307 AkdAASLESQLQDTQELLqEETRQKLNLSS-RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1382
Cdd:pfam05701 322 A--AASLRSELEKEKAEL-ASLRQREGMASiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEE 395
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1626-1884 |
8.31e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1626 LKDLEGQIEAANKARDEAIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKGLEAEILQLQEEFAASERarRH 1705
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1706 AEQERDeLADEIANS-----ASGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNERFRKTTLQVDTLNSELAGERS 1778
Cdd:PRK11637 120 AAQERL-LAAQLDAAfrqgeHTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1779 AAQKSENARQQLERQNKELKAKLQElegsVKSKFKATISTLEAKIAQLEEQLEQeakeraaanklVRRTEKKLKEVFMQV 1858
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQ----ARNERKKTLTGLESSLQKDQQQLSE-----------LRANESRLRDSIARA 252
|
250 260
....*....|....*....|....*..
gi 2024363113 1859 EDE-RRHADQYKEQMEKANARMKQLKR 1884
Cdd:PRK11637 253 EREaKARAEREAREAARVRDKQKQAKR 279
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1077-1245 |
8.61e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1077 QIEELKIQLAKKEEELQAALARGDEEavqknnaLKVIRELQAQIAELQEDLESEKASRNKAEKQKRDL-SEELEALKTEL 1155
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKE-------LELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1156 EDTLDTTAAQQELRTKREQEVAELKKAIEEETknheAQIQEIRqrhataleelsEQLEQAKRFkanLEKNKQGLESDNKE 1235
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLT----NKKSELN-----------TEIAEAEKK---LEQCRGFTFKEIEK 275
|
170
....*....|
gi 2024363113 1236 LACEVKVLQQ 1245
Cdd:smart00787 276 LKEQLKLLQS 285
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
978-1163 |
8.69e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 978 AKIKKMEEEILLLEDQ----NSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL 1053
Cdd:PHA02562 174 DKIRELNQQIQTLDMKidhiQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1054 EKAKRKLDGETTDLQDQIAELQ-----------------------AQIEELKIQLAKKEEELQAALARGDEEAVQKNNAL 1110
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctqqisegpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1111 ---KVIRELQAQIAELQEDLESE-------KASRNKAEKQKRDLSEELEALKTELEDTLDTTA 1163
Cdd:PHA02562 334 eqsKKLLELKNKISTNKQSLITLvdkakkvKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
978-1158 |
8.85e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 43.47 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 978 AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAEcTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAK 1057
Cdd:PRK06669 2 PKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKE-KERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1058 RKLDGETTDLQDQIAELQAQIEELKIQLAK-KEEELQAALARGDEEAVQKNNAlkvirELQAQIAELQEDLesekasRNK 1136
Cdd:PRK06669 81 EELLKKTDEASSIIEKLQMQIEREQEEWEEeLERLIEEAKAEGYEEGYEKGRE-----EGLEEVRELIEQL------NKI 149
|
170 180
....*....|....*....|..
gi 2024363113 1137 AEKQKRDLSEELEALKTELEDT 1158
Cdd:PRK06669 150 IEKLIKKREEILESSEEEIVEL 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
803-1185 |
8.99e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 803 RKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVkpLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKH 882
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 883 QQLLEEKNIlaEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEE 962
Cdd:COG4717 237 EAAALEERL--KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 963 EGARQKLQLEKVTAEAKIKKMEEEILLLEDQnskfLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1042
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1043 LKKEEktrqelekakrkldgettdlqdQIAELQAQIEELKIQLAKKEEELQAALARGDEEavqknnalkvirELQAQIAE 1122
Cdd:COG4717 391 LEQAE----------------------EYQELKEELEELEEQLEELLGELEELLEALDEE------------ELEEELEE 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1123 LQEDLESekasrnkAEKQKRDLSEELEALKTELEDTLDTTAAqQELRTKREQEVAELKKAIEE 1185
Cdd:COG4717 437 LEEELEE-------LEEELEELREELAELEAELEQLEEDGEL-AELLQELEELKAELRELAEE 491
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1588-1851 |
9.30e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1588 EEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARAS 1667
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1668 RDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEE 1747
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1748 EQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLE 1827
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260
....*....|....*....|....
gi 2024363113 1828 EQLEQEAKERAAANKLVRRTEKKL 1851
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAAL 293
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1012-1188 |
9.31e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1012 TSQLAEEEEKAKNLAKLKNKQEmmitdleERLKKEEKT--RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE 1089
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEA-------EAIKKEALLeaKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1090 EELQaalargdeeavQKNNALKvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEledtldtTAAQQ--- 1166
Cdd:PRK12704 103 ELLE-----------KREEELE---KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE-------EAKEIlle 161
|
170 180
....*....|....*....|..
gi 2024363113 1167 ELRTKREQEVAELKKAIEEETK 1188
Cdd:PRK12704 162 KVEEEARHEAAVLIKEIEEEAK 183
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
972-1372 |
9.92e-04 |
|
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: 44.23 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 972 EKVTAEAKIKKMEEeillLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMIT------DLEERLKK 1045
Cdd:NF033838 109 EKSEAELTSKTKKE----LDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTyktlelEIAESDVE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1046 EEKTRQELEKAKRKldgETTDlQDQIAELQAQIEELKIQlAKKEEELQAALARGDEEAVQKNNAlkvirELQAQIAELQE 1125
Cdd:NF033838 185 VKKAELELVKEEAK---EPRD-EEKIKQAKAKVESKKAE-ATRLEKIKTDREKAEEEAKRRADA-----KLKEAVEKNVA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1126 DLESEKASRnkaeKQKRDLSEEL--EALKTELEDTLDTTAAQQELRT---KREQEVAELKKAIEEETKNHEAQIQEIRQR 1200
Cdd:NF033838 255 TSEQDKPKR----RAKRGVLGEPatPDKKENDAKSSDSSVGEETLPSpslKPEKKVAEAEKKVEEAKKKAKDQKEEDRRN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1201 HATALEELSEqLEQAkrfkanleknkqglESDNKELACEVKVLQQVKAES--EHKRKKLDAQVQELTAKVTEGERL---R 1275
Cdd:NF033838 331 YPTNTYKTLE-LEIA--------------ESDVKVKEAELELVKEEAKEPrnEEKIKQAKAKVESKKAEATRLEKIktdR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1276 VELAEKANKLQNELDNVSSLLEEA---------EKKGIKFAKDAASLESQLQDTQellqeetrqklnlssrirQLEEekn 1346
Cdd:NF033838 396 KKAEEEAKRKAAEEDKVKEKPAEQpqpapapqpEKPAPKPEKPAEQPKAEKPADQ------------------QAEE--- 454
|
410 420
....*....|....*....|....*.
gi 2024363113 1347 nlqeqqeeeEEARKNLEKQMLALQAQ 1372
Cdd:NF033838 455 ---------DYARRSEEEYNRLTQQQ 471
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1012-1174 |
9.92e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1012 TSQLAEEEEKAkNLAKLKNKQEmmitdleeRLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1091
Cdd:pfam00529 55 DYQAALDSAEA-QLAKAQAQVA--------RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQID 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1092 LQAALARGDEEAVQKNNALkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEAL--KTELEDTLDTTAAQQELR 1169
Cdd:pfam00529 126 LARRRVLAPIGGISRESLV----TAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELK 201
|
....*
gi 2024363113 1170 TKREQ 1174
Cdd:pfam00529 202 LAKLD 206
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1000-1216 |
1.00e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.28 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1000 EKKLMEDRIAECTSQLAEE-EEKAKNLAKLKNKQEMMITDLEERLKK---EEKTRQELEKAKRKLDGETTDLQDQIAELQ 1075
Cdd:pfam13166 262 GQPLPAERKAALEAHFDDEfTEFQNRLQKLIEKVESAISSLLAQLPAvsdLASLLSAFELDVEDIESEAEVLNSQLDGLR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1076 AQIEELK------IQLAKKEEELQAALARGDE--EAVQKNNAlkVIRELQAQIAELQEDLESEKASRNKAEKQKrdLSEE 1147
Cdd:pfam13166 342 RALEAKRkdpfksIELDSVDAKIESINDLVASinELIAKHNE--ITDNFEEEKNKAKKKLRLHLVEEFKSEIDE--YKDK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1148 LEALKTELEDTLDTTAAQQELRTKREQEVAELkkaiEEETKNHEAQIQEIRQR-HATALEELSEQLEQAK 1216
Cdd:pfam13166 418 YAGLEKAINSLEKEIKNLEAEIKKLREEIKEL----EAQLRDHKPGADEINKLlKAFGFGELELSFNEEG 483
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1585-1708 |
1.01e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.74 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1585 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE------------AANKARDEAIKQLRKLQA 1652
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaaltkGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1653 QMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEilqlQEEFAASERARRHAEQ 1708
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1047-1323 |
1.06e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.53 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1047 EKTRQELEKAKRKLDgETTD----LQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAE 1122
Cdd:pfam04108 17 TDARSLLEELVVLLA-KIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1123 LQE-----------DLESEKASRNKAEKQKRDLSEELEALKTELeDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE 1191
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDL-KRFDDDLRDLQKELESLSSPSESISLIPTLLKELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1192 AQIQEIRQrHATALEELSEQLEQAKR-FKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTE 1270
Cdd:pfam04108 175 SLEEEMAS-LLESLTNHYDQCVTAVKlTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDE 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1271 GerlrVELAEKANKLQNELDNVSSLLEEAEKkgiKFAKDAASLESQLQDTQEL 1323
Cdd:pfam04108 254 L----LSALQLIAEIQSRLPEYLAALKEFEE---RWEEEKETIEDYLSELEDL 299
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1191-1427 |
1.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1191 EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELAcevkvlqqvkaeSEHKRKKLDAQVQELTAKVTE 1270
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD------------LSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1271 GERLRVELAEKANKLQNELDNVSSLLEEAEKKGIkfakdAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQE 1350
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1351 Q-QEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLeenkKKLLKDMESLSQRLEEKAMAYDKLEktkNRLQQ 1427
Cdd:COG3206 306 QlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEE 376
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1655-1853 |
1.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1655 KDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFaasERARRHAEQERDELADEIAnsasgksalldekrRL 1734
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEI---HKLRNEFEKELRERRNELQ--------------KL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1735 EARIAQLEeeleeeqsnmELLNERfrkttlqvdtlNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFK- 1813
Cdd:PRK12704 88 EKRLLQKE----------ENLDRK-----------LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELEr 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024363113 1814 -ATISTLEAKiAQLEEQLEQEAKERAAanKLVRRTEKKLKE 1853
Cdd:PRK12704 147 iSGLTAEEAK-EILLEKVEEEARHEAA--VLIKEIEEEAKE 184
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1189-1418 |
1.17e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1189 NHEAQIQEIRQRHATaleelsEQLEQAKRFKANLEKnKQGLESDNKELacevKVLQQVKAESEHKrkkldAQVQELTAKV 1268
Cdd:PHA02562 180 NQQIQTLDMKIDHIQ------QQIKTYNKNIEEQRK-KNGENIARKQN----KYDELVEEAKTIK-----AEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1269 TEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgIKFAKDAA---SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1345
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1346 NNLQEQQEEEEEARK-----------------NLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRL 1408
Cdd:PHA02562 323 DELEEIMDEFNEQSKkllelknkistnkqsliTLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
250
....*....|
gi 2024363113 1409 EEKAMAYDKL 1418
Cdd:PHA02562 403 YHRGIVTDLL 412
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
836-944 |
1.19e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 836 RVFTKVKPLLQVTRQEEELQAKDEELmkVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAA 915
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 2024363113 916 KKQELEEILHDLESRVEEEEERNQILQNE 944
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
966-1210 |
1.21e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 43.63 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 966 RQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKE--KKLMEDRIAECTSQLAEEEEKAKNlaklknkqemmITDLEERL 1043
Cdd:COG5391 306 FEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVfaKRLEQNQNSILNEGVVQAETLRSS-----------LKELLTQL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1044 KKEEKTRQELEKAKRKLdgetTDLQDQIaelQAQIEELKIQLAKKEEElqaalarGDEEAVQKNNALKVIRELQAQIAEL 1123
Cdd:COG5391 375 QDEIKSRESLILTDSNL----EKLTDQN---LEDVEELSRSLRKNSSQ-------RAVVSQQPEGLTSFSKLSYKLRDFV 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1124 QEDleSEKASRNKAEKQKRDLSEELEALKTELEDTldTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHAT 1203
Cdd:COG5391 441 QEK--SRSKSIESLQQDKEKLEEQLAIAEKDAQEI--NEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKS 516
|
....*..
gi 2024363113 1204 ALEELSE 1210
Cdd:COG5391 517 VKEQLDR 523
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
993-1823 |
1.31e-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: 43.89 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 993 QNSKFLKEKKLMEDRIAECTSQLAEEEekaknLAKLKNK-----QEMMITDLEERLKkeektrqeLEKAKRKLDGETTDL 1067
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKSELSKIYEDD-----IDALYNElssivKENAIDNTEDKAK--------LDDLKSKIDKEYDKI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1068 QDQiaelqaQIEELKIQLAKKEEelqaalargdeeavQKNNALKVIRELQAQI-AELQEDLESEKASRNKAEKQkrdLSE 1146
Cdd:TIGR01612 713 QNM------ETATVELHLSNIEN--------------KKNELLDIIVEIKKHIhGEINKDLNKILEDFKNKEKE---LSN 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1147 ELEALKTELEDTLDTTAAQQELRTKREQEVAeLKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFK------- 1219
Cdd:TIGR01612 770 KINDYAKEKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKddflnkv 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1220 ---ANLEKN-KQGLESDNKELAcevKVLQQVKAESEhkrkklDAQVQELTAKVTEGERLrveLAEKANKLQNELDNVSSL 1295
Cdd:TIGR01612 849 dkfINFENNcKEKIDSEHEQFA---ELTNKIKAEIS------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTL 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1296 LEEAEKkgIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlqeqQEEEEEARKNLEKQMLALQAQLAE 1375
Cdd:TIGR01612 917 KKVDEY--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKD----KFDNTLIDKINELDKAFKDASLND 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1376 AKKKVDDDLGTIEGLEENKKKLLKDMesLSQRLEEKamaydklEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQ 1455
Cdd:TIGR01612 991 YEAKNNELIKYFNDLKANLGKNKENM--LYHQFDEK-------EKATNDIEQKIEDA-------NKNIPNIEIAIHTSIY 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1456 MLAEE------KNISARYAEERDRAEA------EAREKetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDV 1523
Cdd:TIGR01612 1055 NIIDEiekeigKNIELLNKEILEEAEInitnfnEIKEK----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKI 1127
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1524 GKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFERDLQARDEQNEekkrmLVKQVRE 1600
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAE 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1601 LEAELEDERKQRALAVAAKKKMEmdlKDLEGQIEAANKARDEAIKQlrkLQAQMKDYqreleearasrDEIFAQSKESEK 1680
Cdd:TIGR01612 1202 IEKDKTSLEEVKGINLSYGKNLG---KLFLEKIDEEKKKSEHMIKA---MEAYIEDL-----------DEIKEKSPEIEN 1264
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1681 KLkGLEAEILQLQEEFAAS-ERARRH--AEQERDELADEIANSA-------SGKSALLDEKRRLEARIAQleeeleeEQS 1750
Cdd:TIGR01612 1265 EM-GIEMDIKAEMETFNIShDDDKDHhiISKKHDENISDIREKSlkiiedfSEESDINDIKKELQKNLLD-------AQK 1336
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1751 NMELLNERFRKTTLQVDTLnsELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKS-KFKATISTLEAKI 1823
Cdd:TIGR01612 1337 HNSDINLYLNEIANIYNIL--KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKiKDDINLEECKSKI 1408
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1526-1854 |
1.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1526 NVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkrmlvkqVRELEAEL 1605
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--------LESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1606 EDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGL 1685
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1686 EAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQ 1765
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1766 VDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVR 1845
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
....*....
gi 2024363113 1846 RTEKKLKEV 1854
Cdd:COG4372 351 LDNDVLELL 359
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1781-1971 |
1.44e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1781 QKSENARQQLERQNKELKAKLQELEGSVkSKFKA---------TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKL 1851
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL-EEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1852 KEVFMQVEDERRHAdqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateaneglsrevstLKNRLRRG 1931
Cdd:COG3206 250 GSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA--------------LRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024363113 1932 GPITFSSSRSGRRQLHIEGASLELSDDDAESKGSDVNEAQ 1971
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1597-1884 |
1.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1597 QVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLR-------KLQAQMKDYQRELEEARASRD 1669
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKelreeaqELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1670 EIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKsALLDEKRRLEARIAQLEEELEEEQ 1749
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1750 SNMELLNErFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELegsvkskfKATISTLEAKIAQLEEQ 1829
Cdd:COG1340 161 KLKELRAE-LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELHEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1830 LEQEAKEraaanklVRRTEKKLKEVFMQVEDERRHADQyKEQMEKANARMKQLKR 1884
Cdd:COG1340 232 IIELQKE-------LRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1071-1223 |
1.61e-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: 42.80 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1071 IAELQAQIEELKIQLAKkeeeLQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1150
Cdd:pfam00529 53 PTDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1151 LKTELED------TLDTT-AAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLE 1223
Cdd:pfam00529 129 RRVLAPIggisreSLVTAgALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1037-1273 |
1.65e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1037 TDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE----EELQAALARGDEEAVQ---KNNA 1109
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQErllaAQLDAAFRQGEHTGLQlilSGEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1110 LKVIRELQAQIAEL----QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEE 1185
Cdd:PRK11637 151 SQRGERILAYFGYLnqarQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1186 EtknhEAQIQEIRQRHAtaleELSEQLEQAKR-FKANLEKnkqglesdnkelacEVKVLQQVKAesehkrKKLDAQVQEL 1264
Cdd:PRK11637 231 D----QQQLSELRANES----RLRDSIARAEReAKARAER--------------EAREAARVRD------KQKQAKRKGS 282
|
....*....
gi 2024363113 1265 TAKVTEGER 1273
Cdd:PRK11637 283 TYKPTESER 291
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1017-1288 |
1.67e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1017 EEEEKAKNLAKLKNKQEmmitdlEERLKKEEKTRQEleKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1096
Cdd:PRK05035 442 EQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1097 ARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKA-----SRNKAEKQkrdlseELEALKTELEDTLDTTAAQQELRTK 1171
Cdd:PRK05035 514 PDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAvaaaiARAKAKKA------AQQAANAEAEEEVDPKKAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1172 ReqevAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKqgLESDNKELAcevkvlqqVKAESE 1251
Cdd:PRK05035 588 R----AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPE--EPVDPRKAA--------VAAAIA 653
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024363113 1252 HKRKKLDAQVQELTAKVTEGERLRVELAE-----KANKLQNE 1288
Cdd:PRK05035 654 RAKARKAAQQQANAEPEEAEDPKKAAVAAaiaraKAKKAAQQ 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1507-1726 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1507 KQLRADMEDLMSSKDDVGKnvhELEKSKrtleQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERdlQARDEQ 1586
Cdd:COG3883 26 SELQAELEAAQAELDALQA---ELEELN----EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1587 NEEKKRMLVKQVreLEAELEDERKQRALAV-----AAKKKMEmDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQREL 1661
Cdd:COG3883 97 RSGGSVSYLDVL--LGSESFSDFLDRLSALskiadADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1662 EEARASRDEIFAQSKESEKKlkgLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSA 1726
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAA---AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1018-1616 |
1.92e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1018 EEEKAKNLAKLKNKQEMMITDL----EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQ 1093
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1094 AALARgdEEAVQKNNALKVIRELQAQIAEL--QEDLESEKASRnkaeKQKRDLSEELEALKTELEDTLDTTAAQQELRTK 1171
Cdd:pfam07111 215 AQVTL--VESLRKYVGEQVPPEVHSQTWELerQELLDTMQHLQ----EDRADLQATVELLQVRVQSLTHMLALQEEELTR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1172 REQEVAELKKaieEETKNHEAQIQEIRQRHATALEELSEQ----LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1247
Cdd:pfam07111 289 KIQPSDSLEP---EFPKKCRSLLNRWREKVFALMVQLKAQdlehRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1248 AESEhkrkkldaqVQELTAKVTEGERLRVELAEKANKLQneldnvsslLEEAEKKgIKFAKDA-ASLESQLQDTQELLQE 1326
Cdd:pfam07111 366 AEVE---------VERMSAKGLQMELSRAQEARRRQQQQ---------TASAEEQ-LKFVVNAmSSTQIWLETTMTRVEQ 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1327 ETRQKLNLSSRIRQLEEEKNNLqeqqeEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGT-IEGLEENKKKLLKDMEsLS 1405
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKVHTI-----KGLMARKVALAQLRQESCPPPPPAPPVDADLSLeLEQLREERNRLDAELQ-LS 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1406 QRL--EEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfdqmlaeekniSARYAEERDRAEAEAREKET 1483
Cdd:pfam07111 501 AHLiqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLE------------VARQGQQESTEEAASLRQEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1484 KALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELEDELQATEDAKL 1563
Cdd:pfam07111 569 TQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQE-KERNQELRRLQDEARKEEGQRL 647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1564 rlevnmqamkaqferdlqARDEQNEEKKRMLVKQVRELEAELEDERKQRALAV 1616
Cdd:pfam07111 648 ------------------ARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
975-1096 |
1.98e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 42.72 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 975 TAEAKIKKMEEEILLLEDQnskflkekklmedrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELE 1054
Cdd:smart00435 274 THEKSMEKLQEKIKALKYQ--------------LKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEE 339
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2024363113 1055 KAKRkldgettdlqdQIAELQAQIEELKIQLAKKEEELQAAL 1096
Cdd:smart00435 340 KKKK-----------QIERLEERIEKLEVQATDKEENKTVAL 370
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1233-1667 |
2.02e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1233 NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVtEGERLRVELAEKANKLqneldnvsslleeaekkgikfakdaas 1312
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM-EQERLRQEKEEKAREV--------------------------- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1313 lesqlqdtqellqeETRQKLNLSSRIRQLEEEKnnlqeqqeeeeearknlEKQMLALQAQLAEAKKKvdddlgTIEGLEE 1392
Cdd:pfam17380 313 --------------ERRRKLEEAEKARQAEMDR-----------------QAAIYAEQERMAMERER------ELERIRQ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1393 NKKKllKDMESLSQrlEEKAMAYDK---LEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARyae 1469
Cdd:pfam17380 356 EERK--RELERIRQ--EEIAMEISRmreLERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1470 erdraEAEAREKETKALSLARALEEALEAKEEFERQNKqlradMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLE 1549
Cdd:pfam17380 429 -----QEEARQREVRRLEEERAREMERVRLEEQERQQQ-----VERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKIL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1550 ELEdelqatedaklrLEVNMQAMKaqferdlqardeQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEM-DLKD 1628
Cdd:pfam17380 498 EKE------------LEERKQAMI------------EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeERRR 553
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2024363113 1629 LEGQIEAANKARD--EAIKQLRKLQAQMKDYQRELEEARAS 1667
Cdd:pfam17380 554 IQEQMRKATEERSrlEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1548-1928 |
2.07e-03 |
|
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: 43.09 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1548 LEELEDELQATEDAKLRLEvnmqamKAQFErDLQARdeQNEEKKRMLVKQVRE---------LEAELEDERKQRALAVAA 1618
Cdd:pfam05701 69 LEELESTKRLIEELKLNLE------RAQTE-EAQAK--QDSELAKLRVEEMEQgiadeasvaAKAQLEVAKARHAAAVAE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1619 KKKMEMDLKDLEGQIEAANKARDEAIKQLRklqaqmkdyqreleearasrdEIFAQSKESEKKLKGLEAEILQLQEEFAA 1698
Cdd:pfam05701 140 LKSVKEELESLRKEYASLVSERDIAIKRAE---------------------EAVSASKEIEKTVEELTIELIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1699 SERARRHAEQERDELA----DEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL-NERFRKTTLQVDTLNSEL 1773
Cdd:pfam05701 199 AHAAHLEAEEHRIGAAlareQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLlDLKAELAAYMESKLKEEA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1774 AGERSAAQKSENARQQLERQNKELkaklQELEGSVKsKFKATISTLEAKIAQLEEQLEQEAKERAAanklVRRTEKKLKE 1853
Cdd:pfam05701 279 DGEGNEKKTSTSIQAALASAKKEL----EEVKANIE-KAKDEVNCLRVAAASLRSELEKEKAELAS----LRQREGMASI 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1854 VFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:pfam05701 350 AVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRL 428
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1067-1305 |
2.18e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1067 LQDQIAELQAQIEELKIQLAKKEEELqaalargdeeAVQKNNaLKVIRELQAQ-IAELQEDLESEKASRNKAEKQKRDLS 1145
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQI----------KTYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1146 EELEALKTELEdtlDTTAAQQELRTKREQ---EVAELKKAIEEETKNHE------------AQIQEIRQRHA-------- 1202
Cdd:PHA02562 241 DELLNLVMDIE---DPSAALNKLNTAAAKiksKIEQFQKVIKMYEKGGVcptctqqisegpDRITKIKDKLKelqhslek 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1203 --TALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEhkrkKLDAQVqelTAKVTEGERLRVELAE 1280
Cdd:PHA02562 318 ldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE----ELQAEF---VDNAEELAKLQDELDK 390
|
250 260 270
....*....|....*....|....*....|.
gi 2024363113 1281 KANKLQN------ELDNVSSLLEEAekkGIK 1305
Cdd:PHA02562 391 IVKTKSElvkekyHRGIVTDLLKDS---GIK 418
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1040-1220 |
2.23e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.11 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1040 EERLKKEEKTRQELEKAKRKLDGETtdlQDQIAELQAQIEELKI------QLAKKEEELQaalargDEEAVQKNNALKVI 1113
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIK------DKQEKLMRRCKKVL 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1114 RELQAQIAELqedLESEkasrnkaekqkRDLSEELEALKTELEdTLDttAAQQELRTKREQEVAELKKAIEEETKN---- 1189
Cdd:pfam10168 617 QRLNSQLPVL---SDAE-----------REMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSIRKKSslsl 679
|
170 180 190
....*....|....*....|....*....|....
gi 2024363113 1190 ---HEAQIQEIRQRHAtalEELSEQLEQAKRFKA 1220
Cdd:pfam10168 680 sekQRKTIKEILKQLG---SEIDELIKQVKDINK 710
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1530-1734 |
2.30e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1530 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1608
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1609 RKQRALAVAAKKKMEMDLKDLEGQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARASRDE-- 1670
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1671 -IFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1734
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1610-1863 |
2.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1610 KQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEI 1689
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1690 LQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTL 1769
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1770 NSELagERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1849
Cdd:COG4372 170 EQEL--QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250
....*....|....
gi 2024363113 1850 KLKEVFMQVEDERR 1863
Cdd:COG4372 248 KEELLEEVILKEIE 261
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
884-1411 |
2.32e-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: 42.81 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 884 QLLEEKNILaEQLQAETELfAEAEEMRARLaakkqELEEILHDLESRVEEEEERNQILQNEKKKMQGhiqdleeqldeee 963
Cdd:pfam05557 3 ELIESKARL-SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQKRIRLLEK------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 964 garqklqlEKVTAEAKIKKMEEEILLL---EDQNSKFLKEKKLMEDRIAECTSQLAEEeekaknLAKLKNKQEMMITDLE 1040
Cdd:pfam05557 63 --------REAEAEEALREQAELNRLKkkyLEALNKKLNEKESQLADAREVISCLKNE------LSELRRQIQRAELELQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1041 ERLKKEEKTRQELEKAKRKLdgetTDLQDQIAELQAQIEELKIQLAKKEEelqaaLARGDEEAVQKNNALKVIRELQAQI 1120
Cdd:pfam05557 129 STNSELEELQERLDLLKAKA----SEAEQLRQNLEKQQSSLAEAEQRIKE-----LEFEIQSQEQDSEIVKNSKSELARI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1121 AELQEDLESEKASRNKAEKQKRD---LSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaieeetknheaQIQEI 1197
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQ------------SWVKL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1198 RQRHATAL---EELSEQLEQAKRFKANLEKNKQGLESDnkelaceVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERL 1274
Cdd:pfam05557 268 AQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLTSS-------ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1275 RVELAEKANKLQNELDNVSSLLEEAEKKgIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLqeqqee 1354
Cdd:pfam05557 341 VRRLQRRVLLLTKERDGYRAILESYDKE-LTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGY------ 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024363113 1355 eeearkNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKlLKDMESLSQRLEEK 1411
Cdd:pfam05557 414 ------KQQAQTLERELQALRQQESLADPSYSKEEVDSLRRK-LETLELERQRLREQ 463
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1415-1857 |
2.52e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1415 YDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeEKNISARYAEERDRAEAEAREKETKALsLARALEE 1494
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1495 ALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1574
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1575 QFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQM 1654
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1655 KDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1734
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1735 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKA 1814
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2024363113 1815 TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQ 1857
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
888-1091 |
2.52e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 888 EKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLEsrveeeeernQILQNEKKKMQGHIQDLEEQLDEEEGARQ 967
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA----------KTIKAEIEELTDELLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 968 KLQLEKVTAEAKIKKMEEEILLLEDQN------SKFLKEKKLME---DRIAECTSQLAEEEEKAKNLAKLKN---KQEMM 1035
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYEKGGvcptctQQISEGPDRITkikDKLKELQHSLEKLDTAIDELEEIMDefnEQSKK 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1036 ITDLEERLKKEEKTRQ-------ELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1091
Cdd:PHA02562 339 LLELKNKISTNKQSLItlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
871-1047 |
2.74e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 871 VEAELEEMERKHQQLLEEKNILAEQlQAETELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMqg 950
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKE-HEERELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEA-- 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 951 hiqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEILLLEdqnsKFLKEkklmEDRIAEctsQLAEEEEKAKNLAKLKN 1030
Cdd:COG2433 454 ----------------RSEERREIRKDREISRLDREIERLE----RELEE----ERERIE---ELKRKLERLKELWKLEH 506
|
170
....*....|....*..
gi 2024363113 1031 KQEMMITDLEERLKKEE 1047
Cdd:COG2433 507 SGELVPVKVVEKFTKEA 523
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1076-1301 |
2.85e-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: 41.63 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1076 AQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL 1155
Cdd:pfam06008 12 PAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1156 EDTLDT-TAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQ-LEQAKRFKANLEKNKQGLESDN 1233
Cdd:pfam06008 92 KNLIDNiKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAeLKAAQDLLSRIQTWFQSPQEEN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1234 KELAcevKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1301
Cdd:pfam06008 172 KALA---NALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1004-1183 |
2.86e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1004 MEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKK------EEKTRQELEKaKRKLDGETTDLQDQIAELQAQ 1077
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLalekgrEDLAREALER-KAELEAQAEALEAQLAQLEEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1078 IEELKIQLAKKEEELQAALARGDEEAVQKNNAlkvirELQAQIAELQEDLESEKASR--NKAEKQKRDLSEELEALKT-E 1154
Cdd:COG1842 114 VEKLKEALRQLESKLEELKAKKDTLKARAKAA-----KAQEKVNEALSGIDSDDATSalERMEEKIEEMEARAEAAAElA 188
|
170 180
....*....|....*....|....*....
gi 2024363113 1155 LEDTLDTTAAQQELRTKREQEVAELKKAI 1183
Cdd:COG1842 189 AGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1578-1716 |
2.88e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1578 RDLQARDEQNEEKKRMLVKQVRELEAELeDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDY 1657
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAEL-DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1658 -------QRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADE 1716
Cdd:pfam00529 133 apiggisRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1012-1150 |
2.93e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1012 TSQLAEEEEKAKNLAKlknKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1091
Cdd:COG2268 194 IAEIIRDARIAEAEAE---RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024363113 1092 LQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1150
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEA 329
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1036-1128 |
2.95e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.45 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1036 ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRE 1115
Cdd:pfam11932 15 LDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERE 94
|
90
....*....|...
gi 2024363113 1116 LQAQIAELQEDLE 1128
Cdd:pfam11932 95 LVPLMLKMLDRLE 107
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
852-949 |
2.97e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 852 EELQAKDEEL-MKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQaetELFAEAE-EMRARLAAKKQELEEIL----- 924
Cdd:PRK00409 519 NELIASLEELeRELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEkEAQQAIKEAKKEADEIIkelrq 595
|
90 100 110
....*....|....*....|....*....|....*.
gi 2024363113 925 -----------HDLESRVEEEEERNQILQNEKKKMQ 949
Cdd:PRK00409 596 lqkggyasvkaHELIEARKRLNKANEKKEKKKKKQK 631
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1533-1688 |
3.00e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1533 SKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD-LQARDEQNEEKKRMLVKQVRELEAE------- 1604
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEaESSREQLQELEEQLATERSARREAEaelerlq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1605 ------LEDERKQRALAVAAKKKMEMDLKDLEGQIEA---ANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1675
Cdd:pfam09787 121 eelrylEEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
|
170
....*....|...
gi 2024363113 1676 KESEKKLKGLEAE 1688
Cdd:pfam09787 201 ERMEQQIKELQGE 213
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1599-1713 |
3.25e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1599 RELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEifaqSKES 1678
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR----EIRK 463
|
90 100 110
....*....|....*....|....*....|....*
gi 2024363113 1679 EKKLKGLEAEILQLQEEFAASERARRHAEQERDEL 1713
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1637-1883 |
3.35e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1637 NKARDEAIKQLRKLQA-QMKDYQRELEEARASR--------DEIFAQSKESEKKLKGLEAEILQLqeEFAASERARRHAE 1707
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEELSNERLRKlrslltklSEALDKLRSYLPKLNPLREEKKKV--SVKSLEELIKDVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1708 QERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEeqsNMELLNERFRKTTLQ-VDTLNSELAGERSAAQKSENA 1786
Cdd:PRK05771 93 EELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNF---DLDLSLLLGFKYVSVfVGTVPEDKLEELKLESDVENV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1787 -----------------RQQLERQNKELK-AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEqeakeraaanklvrRTE 1848
Cdd:PRK05771 170 eyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------------SLL 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 2024363113 1849 KKLKEVFMQVEDERRHADQYKEQM-EKANARMKQLK 1883
Cdd:PRK05771 236 EELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1417-1620 |
3.36e-03 |
|
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: 42.51 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1417 KLEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKNISAryaeERDRAEAEAREKETKALSLARALEEAL 1496
Cdd:NF012221 1566 RAEADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEESRAVTKELTTLAQGLDALD 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1497 EAKEEFERQNKQLRAD-----MEDLMSSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1570
Cdd:NF012221 1634 SQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKqLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDID 1713
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 1571 AMKAQFE-RDLQARDEQNEEKKRmlvKQVRELEAELEDERKQRALAVAAKK 1620
Cdd:NF012221 1714 DAKADAEkRKDDALAKQNEAQQA---ESDANAAANDAQSRGEQDASAAENK 1761
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1577-1886 |
3.37e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1577 ERDLQARDEQNEE---KKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDL-----------EGQIEAANKARDE 1642
Cdd:COG5185 161 IKDIFGKLTQELNqnlKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGsestllekakeIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1643 AIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEfaASERARRHAEQERDELADEIANSAS 1722
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFEN--TKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1723 GKSALLDEkrrLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQ---QLERQNKELKA 1799
Cdd:COG5185 319 AAAEAEQE---LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSfkdTIESTKESLDE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1800 KLQELEGSVKSKFKA---TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYK------- 1869
Cdd:COG5185 396 IPQNQRGYAQEILATledTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAydeinrs 475
|
330
....*....|....*....
gi 2024363113 1870 --EQMEKANARMKQLKRQL 1886
Cdd:COG5185 476 vrSKKEDLNEELTQIESRV 494
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
966-1182 |
3.47e-03 |
|
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: 42.51 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 966 RQKLQLEKVTAEAKIKKMEEEillLE--DQNskflkekKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERL 1043
Cdd:NF012221 1571 RQRLEQEKQQQLAAISGSQSQ---LEstDQN-------ALETNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAG 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1044 KKEEKTRQELekAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgDEEAVQKNnalkvirelQAQIAEL 1123
Cdd:NF012221 1641 ESGDQWRNPF--AGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAK-SEAGVAQG---------EQNQANA 1708
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1124 QEDLESekaSRNKAEKQKRD-LSEELEALKTELEDTLDTTAAQQelRTKREQEVAELKKA 1182
Cdd:NF012221 1709 EQDIDD---AKADAEKRKDDaLAKQNEAQQAESDANAAANDAQS--RGEQDASAAENKAN 1763
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1013-1256 |
3.68e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1013 SQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLA------ 1086
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSedgtqk 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1087 --------------KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE---DLESEKASRNKAEKQKRDLSEELE 1149
Cdd:pfam15905 153 kmsslsmelmklrnKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEKIEEKSETEKLLEYITELS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1150 ALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEirqrhataLEELSEQLEQAKRFKANLEKNKQgl 1229
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD--------LNEKCKLLESEKEELLREYEEKE-- 302
|
250 260
....*....|....*....|....*..
gi 2024363113 1230 ESDNKELACEVKVLQQVKAESEHKRKK 1256
Cdd:pfam15905 303 QTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
965-1268 |
3.72e-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: 42.20 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 965 ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEE-EKAKNLAKLKNK--QEMMITDLEE 1041
Cdd:pfam15964 390 LRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEmDVTKVCGEMRYQlnQTKMKKDEAE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1042 RLKKEEKTR---------QELEKAKRKLDGETTDL-QDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQK---NN 1108
Cdd:pfam15964 470 KEHREYRTKtgrqleikdQEIEKLGLELSESKQRLeQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQsfsNE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1109 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-QELRTKREQEVAELkkaiEEET 1187
Cdd:pfam15964 550 AKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKlEEITQKSRSEVEQL----SQEK 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1188 KNHEAQIQEIRQRHatalEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAK 1267
Cdd:pfam15964 626 EYLQDRLEKLQKRN----EELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
.
gi 2024363113 1268 V 1268
Cdd:pfam15964 702 V 702
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1165-1376 |
3.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1165 QQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ 1244
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1245 QVKAESEHKRKKLDAQ-VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQEL 1323
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1324 LQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEA 1376
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1520-1655 |
4.00e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1520 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVR 1599
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1600 ELEAELEDERKQRALAVAAKkkmemDLKDLEGQIEAANKARDEAIKQLRKLQAQMK 1655
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1036-1152 |
4.03e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1036 ITDLEERLKKEEKTRQELEKAKRKLD-GETTDLQDQIAELQAQIEELKIQLAKKEEELQAAlargdEEAVQKNNALKviR 1114
Cdd:smart00787 177 LRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEL-----ESKIEDLTNKK--S 249
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024363113 1115 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1152
Cdd:smart00787 250 ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1334-1431 |
4.12e-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: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1334 LSSRIRQLEEEKNNLQEQQEEEEEAR-KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKA 1412
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90
....*....|....*....
gi 2024363113 1413 MAYDKLEKTKNRLQQELDD 1431
Cdd:COG0542 496 ELEEELAELAPLLREEVTE 514
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1045-1152 |
4.41e-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: 41.20 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1045 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALAR--GDEEAVQK-------NNALKVIRE 1115
Cdd:cd22656 104 ADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAleTLEKALKDlltdeggAIARKEIKD 183
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024363113 1116 LQAQIAELQEDLESE-KASRNKAEKQKRDLSEELEALK 1152
Cdd:cd22656 184 LQKELEKLNEEYAAKlKAKIDELKALIADDEAKLAAAL 221
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1446-1929 |
4.50e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1446 LEKKQKKFDQMLAEEKNISARYAEE---RDRAEAEAREKETKALsLARALEEALEAKEEFERQNKQLRADMEDLMSS--- 1519
Cdd:NF041483 169 LDESRAEAEQALAAARAEAERLAEEarqRLGSEAESARAEAEAI-LRRARKDAERLLNAASTQAQEATDHAEQLRSStaa 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1520 -KDDVGKNVHELEkskRTLEQQVEEMRTQLEELEdelqaTEDAKLRLEVNMQAMKAqferdLQARDEQNEEKKRMLVKQV 1598
Cdd:NF041483 248 eSDQARRQAAELS---RAAEQRMQEAEEALREAR-----AEAEKVVAEAKEAAAKQ-----LASAESANEQRTRTAKEEI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1599 RELEAELEDErkqralAVAAKKKMEMDLKDLEGQieaANKARDEAIKQLRKLQAQmkDYQRELEEARASRDEIFAQSKES 1678
Cdd:NF041483 315 ARLVGEATKE------AEALKAEAEQALADARAE---AEKLVAEAAEKARTVAAE--DTAAQLAKAARTAEEVLTKASED 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1679 EKKLKGLEAEilqlqeefaASERARRHAEQERDELADEIANSASG-KSALLDEKRRLEARIAQleeeleeeqsnmelLNE 1757
Cdd:NF041483 384 AKATTRAAAE---------EAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE--------------LQE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1758 RFRKTTLQVDTLNSELA--GERSAAQKSENARQQLERQNKELKAKLqelegsvkSKFKATISTLEAKIAQLEEQLEQEAK 1835
Cdd:NF041483 441 EARRLRGEAEQLRAEAVaeGERIRGEARREAVQQIEEAARTAEELL--------TKAKADADELRSTATAESERVRTEAI 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1836 ERAA-----ANKLVRRT----EKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRE 1906
Cdd:NF041483 513 ERATtlrrqAEETLERTraeaERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAE 592
|
490 500
....*....|....*....|....*
gi 2024363113 1907 --LDDATEANEGLSREVSTLKNRLR 1929
Cdd:NF041483 593 eaLADARAEAERIRREAAEETERLR 617
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1141-1308 |
4.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1141 KRDLSEELEALKTELEDTLDttAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA 1220
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1221 NLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELT------AKVTEGERLRVELAEKANKLQNELDnvss 1294
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeeAKEILLEKVEEEARHEAAVLIKEIE---- 179
|
170
....*....|....
gi 2024363113 1295 llEEAEKKGIKFAK 1308
Cdd:PRK12704 180 --EEAKEEADKKAK 191
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
967-1167 |
4.89e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.43 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 967 QKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKnLAKLKNKQEMM------ITDLE 1040
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQ-AALTKGNEELArealaeKKSLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1041 ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQL--AKKEEELQAALARGDEEAvqknnalkVIRELQa 1118
Cdd:pfam04012 97 KQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLkaAKAQEAVQTSLGSLSTSS--------ATDSFE- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024363113 1119 QIAELQEDLESEKASRNKAEkQKRDLSEELEALKTELEDTLDTTAAQQE 1167
Cdd:pfam04012 168 RIEEKIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
851-1118 |
5.16e-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: 42.03 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 851 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 926
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 927 LEsrveeEEERNqiLQNEKKKMQghiqdleeqldeeeGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1006
Cdd:pfam15921 676 YE-----VLKRN--FRNKSEEME--------------TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1007 RIAECTSQLAEEEEKAKNLaklknKQEMMITDLEERLKKEEKTR--QELEKA---KRKLDGETTDLQDQIAELQAQIEEL 1081
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFL-----EEAMTNANKEKHFLKEEKNKlsQELSTVateKNKMAGELEVLRSQERRLKEKVANM 809
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2024363113 1082 KIQLAKKE---EELQAALARGDEEAVQ-KNNALKVIRELQA 1118
Cdd:pfam15921 810 EVALDKASlqfAECQDIIQRQEQESVRlKLQHTLDVKELQG 850
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1345-1559 |
5.64e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1345 KNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD---DLGTIEgLEENKKKLLKDMESLSQRLEEKAMAYDKLEKT 1421
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqKNGLVD-LSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1422 KNRLQQELDDLMVDLDHQRQ--IVSNLEKKQKKFDQMLAEeknISARYAEE-RDRAEAEAREKETKAL---SLARALEEA 1495
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAE---LSARYTPNhPDVIALRAQIAALRAQlqqEAQRILASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024363113 1496 LEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELekskRTLEQQVEEMRTQLEELEDELQATE 1559
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARELYESLLQRLEEAR 378
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1063-1142 |
5.68e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1063 ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKR 1142
Cdd:PRK11448 136 PPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1630-1731 |
5.85e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.96 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1630 EGQIEAANKARDEAIKQLrklqaqmKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAAS-ERARRHAEQ 1708
Cdd:cd06503 36 AESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAEIEQ 106
|
90 100
....*....|....*....|...
gi 2024363113 1709 ERDELADEIANSASGKSALLDEK 1731
Cdd:cd06503 107 EKEKALAELRKEVADLAVEAAEK 129
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1630-1731 |
6.03e-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: 39.39 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1630 EGQIEAANKARDEAikqlrklQAQMKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAA-SERARRHAEQ 1708
Cdd:COG0711 37 ADGLAEAERAKEEA-------EAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAEIEQ 107
|
90 100
....*....|....*....|...
gi 2024363113 1709 ERDELADEIANSASGKSALLDEK 1731
Cdd:COG0711 108 ERAKALAELRAEVADLAVAIAEK 130
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
982-1157 |
6.47e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 41.65 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 982 KMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEE-----EKAKNLAKLKNK-QEMMITDLEErlkKEEKTRQELEk 1055
Cdd:COG5192 525 KSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEfeelkKKWSSLAQLKSRfQKDATLDSIE---GEEELIQDDE- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1056 akrklDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvQKNNALKviRELQAQIaELQEDLESEKASRN 1135
Cdd:COG5192 601 -----KGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETER-EENARKK--EELRGNF-ELEERGDPEKKDVD 671
|
170 180
....*....|....*....|..
gi 2024363113 1136 KAEKQKRDLSEELEALKTELED 1157
Cdd:COG5192 672 WYTEEKRKIEEQLKINRSEFET 693
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
863-1010 |
7.14e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 863 KVKEKQTKVEAELEEMERKHQQLLEEKnilaEQLQAETEL--FAEAEEMRARLAAKKQELEEilhdLESRVEEEEERNQI 940
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEK----EALKKEQDEasFERLAELRDELAELEEELEA----LKARWEAEKELIEE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 941 LQNEKKKMQGHIQDLEEQLDEEEGARQKLQL------EKVTAE--AKI---------KKMeeeillLEDQNSKFLKekkl 1003
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAElapllrEEVTEEdiAEVvsrwtgipvGKL------LEGEREKLLN---- 542
|
....*..
gi 2024363113 1004 MEDRIAE 1010
Cdd:COG0542 543 LEEELHE 549
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1090-1247 |
7.20e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1090 EELQAALARGDEEAVQ--KNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaqqE 1167
Cdd:cd22656 98 ELIDDLADATDDEELEeaKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD-----E 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1168 LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1247
Cdd:cd22656 173 GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQ 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1157 |
7.29e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 846 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 925
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 926 DLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAE-AKIKKMEEEILLLEDQNSKFLKEKKLM 1004
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1005 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1084
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1085 LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELED 1157
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1643-1886 |
7.33e-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: 40.47 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1643 AIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEE-----------FAASERARRHAEqerd 1711
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtlakaqqvNAESERTLGHAK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1712 ELADEIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLnselagERSAAQKSENa 1786
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEA------ELKAAQDLLS- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1787 rqQLERQNKELKAKLQELEGSVKSKfkatISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHAD 1866
Cdd:pfam06008 159 --RIQTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKN 232
|
250 260
....*....|....*....|
gi 2024363113 1867 QYKEQMEKANARMKQLKRQL 1886
Cdd:pfam06008 233 QLEETLKTARDSLDAANLLL 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
867-1342 |
7.35e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 867 KQTKVEAELEEMER-KHQQLLEEKNILAEQLQAETELFAEAEEMRAR---LAAKKQELEEILHDLESRVEEEEERNQILq 942
Cdd:pfam05557 3 ELIESKARLSQLQNeKKQMELEHKRARIELEKKASALKRQLDRESDRnqeLQKRIRLLEKREAEAEEALREQAELNRLK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 943 neKKKMQGHIQDLEEQLDEEEGARQ-KLQLEKVTAEAKIKKMEEEILLLEDQNSKF-LKEKKLMEDRIAECTSQLAEEEE 1020
Cdd:pfam05557 82 --KKYLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQRAELELQSTNSELEeLQERLDLLKAKASEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1021 KAKNLAKLKNKQemmITDLEERLKKEEKTRQELEKAKRKLdGETTDLQDQIAELQAQIEEL------KIQLAKKEEELQA 1094
Cdd:pfam05557 160 KQQSSLAEAEQR---IKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLnenienKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1095 ALARgdeeavqknnalkvIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL---EALKTELEDTLDTTAAQQELRTK 1171
Cdd:pfam05557 236 KLER--------------EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1172 REQEVAELKKAI---EEETKNHEAQIQEIRQRhataLEELSEQLE--QAKRFKANLEKN--KQGLESDNKELACE----- 1239
Cdd:pfam05557 302 LTSSARQLEKARrelEQELAQYLKKIEDLNKK----LKRHKALVRrlQRRVLLLTKERDgyRAILESYDKELTMSnyspq 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1240 --------VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELaeKANKLQNELDNVSSLLEEAEkkgikfakdaa 1311
Cdd:pfam05557 378 llerieeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL--QALRQQESLADPSYSKEEVD----------- 444
|
490 500 510
....*....|....*....|....*....|.
gi 2024363113 1312 SLESQLQDTQELLQEETRQKLNLSSRIRQLE 1342
Cdd:pfam05557 445 SLRRKLETLELERQRLREQKNELEMELERRC 475
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
975-1200 |
7.46e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 975 TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEmmitdlEERLKKEEKTRQELE 1054
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAE------EKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1055 KAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASR 1134
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024363113 1135 NKAEKQKRdLSEELEALKTELEDTLDTTAAQQELRTKREQEVAElKKAIEEETKNHEAQIQEIRQR 1200
Cdd:TIGR02794 211 AKAEAEAA-AAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR-GAAAGSEVDKYAAIIQQAIQQ 274
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
846-986 |
7.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 846 QVTRQEEELQAKDEelmkVKEKQTKVEAELEEMERKHQQ----LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELE 921
Cdd:PRK12704 52 EAIKKEALLEAKEE----IHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024363113 922 EILHDLEsrveeeeernQILQNEKKKMQgHIQDLEEQLdeeegARQKLqLEKVTAEAK------IKKMEEE 986
Cdd:PRK12704 128 KKEEELE----------ELIEEQLQELE-RISGLTAEE-----AKEIL-LEKVEEEARheaavlIKEIEEE 181
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1525-1924 |
7.66e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1525 KNVHELEKSKRTLEQQVEEMRTQLEELEDElqateDAKLRLEVNmQAMK--AQFERDLQARDEQNEEKKRMLVKQVRELE 1602
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-----EEKNREEVE-ELKDkyRELRKTLLANRFSYGPAIDELEKQLAEIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1603 AELE--DERKQRALAVAAKK---KMEMDLKDLEGQIEAA----NKARDEAIKQLRKLQA---QMKDYQRELEEarasrDE 1670
Cdd:pfam06160 160 EEFSqfEELTESGDYLEAREvleKLEEETDALEELMEDIpplyEELKTELPDQLEELKEgyrEMEEEGYALEH-----LN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1671 IFAQSKESEKKLKGLEAEILQLqeEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1750
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1751 NMELLNERFrkttlqvdTLNselAGERSAAQKSENARQQLERQNKELKAKLQELEG---SVKSKFK---ATISTLEAKIA 1824
Cdd:pfam06160 313 ELERVQQSY--------TLN---ENELERVRGLEKQLEELEKRYDEIVERLEEKEVaysELQEELEeilEQLEEIEEEQE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1825 QLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKANARMKQLKRQLeeaeeeatraNASR 1900
Cdd:pfam06160 382 EFKESLQSLRKDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVSDEIEDLADEL----------NEVP 449
|
410 420
....*....|....*....|....*..
gi 2024363113 1901 ---RKLQRELDDATEANEGLSREVSTL 1924
Cdd:pfam06160 450 lnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1578-1884 |
8.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1578 RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLK-------DLEGQIEAANKARDEAIKQLRKL 1650
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelaQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1651 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA----DEIANSASGKSA 1726
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldelLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1727 LLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEG 1806
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024363113 1807 SVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKR 1884
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1592-1734 |
9.21e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1592 RMLVKQVRELEAELEDERKQRALAVAAKKKMEMdlkdLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEAR------ 1665
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarr 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024363113 1666 ---ASRDEIFAQSKESEKKL-KGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1734
Cdd:pfam00529 130 rvlAPIGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1001-1888 |
9.93e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1001 KKLMEDRIAECTSQLAEEEEKAKN---------LAKLKNKQEMMITDLEERLK--------KEEKTRQELEKAKRKLDGE 1063
Cdd:NF041483 333 EQALADARAEAEKLVAEAAEKARTvaaedtaaqLAKAARTAEEVLTKASEDAKattraaaeEAERIRREAEAEADRLRGE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1064 TTDLQDQIA--------ELQAQIEELKIQ---LAKKEEELQA-ALARGDE-------EAVQK-NNALKVIRELQAQIAEL 1123
Cdd:NF041483 413 AADQAEQLKgaakddtkEYRAKTVELQEEarrLRGEAEQLRAeAVAEGERirgearrEAVQQiEEAARTAEELLTKAKAD 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1124 QEDLESekASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE-LRTKREQEVAELKKAIEEETKN-HEAQIQEIRQRH 1201
Cdd:NF041483 493 ADELRS--TATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEEVRAAAERAARElREETERAIAARQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1202 ATALEELSeqleqakRFKANLEKNKQGLESDNKELACEVKVLQQVKA-ESEHKRKKLDAQVQELTAKV-TEGERLRVELA 1279
Cdd:NF041483 571 AEAAEELT-------RLHTEAEERLTAAEEALADARAEAERIRREAAeETERLRTEAAERIRTLQAQAeQEAERLRTEAA 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1280 EKANKLQNELDNVS-SLLEEAekkgikfAKDAASLESQLQDTQELLQEETRqklnlSSRIRQLEEEKNNLQEQQEEEEEA 1358
Cdd:NF041483 644 ADASAARAEGENVAvRLRSEA-------AAEAERLKSEAQESADRVRAEAA-----AAAERVGTEAAEALAAAQEEAARR 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1359 RKNLEKqmlALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKA--MAYDKLEKTKNRLQQelddlmvdl 1436
Cdd:NF041483 712 RREAEE---TLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVEEAdrRATELVSAAEQTAQQ--------- 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1437 dhQRQIVSNLEKKqkkfdqmlAEEKNISARYAEER--DRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADME 1514
Cdd:NF041483 780 --VRDSVAGLQEQ--------AEEEIAGLRSAAEHaaERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAA 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1515 DLMSSKDdVGKNVHELEKSKRTLEQQVEEMRTqleELEDELQATEDAKLRLEVnmqamkaqferdlQARDEQNEEKKRML 1594
Cdd:NF041483 850 KALAERT-VSEAIAEAERLRSDASEYAQRVRT---EASDTLASAEQDAARTRA-------------DAREDANRIRSDAA 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1595 VKQVREL-EAELEDERKQRALAVAAKKKmemdlkdLEGQIEAANKARDEAIKQLRKLQAqmkDYQRELEEARASRDEIFA 1673
Cdd:NF041483 913 AQADRLIgEATSEAERLTAEARAEAERL-------RDEARAEAERVRADAAAQAEQLIA---EATGEAERLRAEAAETVG 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1674 QSKESEKKLKGlEAEILQLQEEfAASERARRHAEQERDELADEIANSASgksalldeKRRLEAriaqleeeleeeqsnme 1753
Cdd:NF041483 983 SAQQHAERIRT-EAERVKAEAA-AEAERLRTEAREEADRTLDEARKDAN--------KRRSEA----------------- 1035
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024363113 1754 llnerfrktTLQVDTLNSELAGErsAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQE 1833
Cdd:NF041483 1036 ---------AEQADTLITEAAAE--ADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTD 1104
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024363113 1834 AKE-----RAAANKLVRRTEKKLKEVFMQVED-----ERRHADQYKEQMEKANARMKQLKRQLEE 1888
Cdd:NF041483 1105 ADEllvgaRRDATAIRERAEELRDRITGEIEElheraRRESAEQMKSAGERCDALVKAAEEQLAE 1169
|
|
| |
