|
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 ... |
863-1943 |
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: 1480.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 863 TRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDL 942
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 943 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1022
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1023 ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTK 1102
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1103 KEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1182
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1183 LRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAK 1262
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1263 TESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEE 1342
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1343 TRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQC 1422
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1423 LEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALS 1502
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1503 MARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1582
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1583 NMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQL 1662
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1663 RKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSL 1742
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1743 LEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGT 1822
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1823 VKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLE 1902
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1604804600 1903 EAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRL 1943
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-786 |
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: 1422.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkpvklqaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP---------------GELERQLLQANPILESFGNAKTVKNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14920 146 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd14920 226 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd14920 306 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd14920 386 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAFGATY 658
Cdd:cd14920 466 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAY 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd14920 546 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 739 FRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14920 626 FRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-786 |
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: 1306.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvklqAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKE--------------SGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYR-FLSNGNIPIPGQQD 337
Cdd:cd01377 147 KFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIK 417
Cdd:cd01377 227 AEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 418 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEK 497
Cdd:cd01377 307 VGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 498 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTK 577
Cdd:cd01377 386 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 578 -FQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRivgldqvagmnETAFGA 656
Cdd:cd01377 464 nFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 657 TYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 736
Cdd:cd01377 533 KKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIF 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1604804600 737 QEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd01377 613 AEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-786 |
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: 1234.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklQAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS-----------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14932 150 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd14932 230 ELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd14932 310 GRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd14932 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAFGAtY 658
Cdd:cd14932 470 QKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGA-F 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd14932 549 KTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 739 FRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14932 629 FRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-786 |
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: 1188.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvklqaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ------------------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14919 143 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd14919 223 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd14919 303 GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd14919 383 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAFGATY 658
Cdd:cd14919 463 QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd14919 543 KTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 739 FRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14919 623 FRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-786 |
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: 1172.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPkpvklqaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSH-----------GELEKQLLQANPILEAFGNAKTVKNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd15896 150 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd15896 230 DLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd15896 310 GRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNEtaFGATY 658
Cdd:cd15896 470 FKPKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd15896 548 KTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 739 FRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd15896 628 FRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-786 |
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: 1171.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvklqaqhaVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI---------------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14921 146 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd14921 226 EMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd14921 306 GRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd14921 386 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAFGATY 658
Cdd:cd14921 466 QKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSAS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd14921 546 KTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 739 FRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14921 626 FRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-786 |
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: 1163.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKPVKLqaqhaVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVL-----IGELEQQLLQANPILEAFGNAKTVKNDNSSRFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14911 155 KFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd14911 235 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd14911 315 GRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd14911 395 QQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrIVGLDQVAgMNETAFGAty 658
Cdd:cd14911 472 MK-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA-- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd14911 547 RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 739 FRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14911 627 FRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-786 |
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: 1141.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkpvklqaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP---------------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQdK 338
Cdd:cd14930 146 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd14930 225 ELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd14930 305 GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd14930 385 QQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAFGAty 658
Cdd:cd14930 465 QRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG-- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd14930 543 RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 739 FRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14930 623 FRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-786 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1100.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 87 VEDMAELTCLNEASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkpvklqaqhaVGELERQLLQANPILESFGNA 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-------------------VGRLEEQILQSNPILEAFGNA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 247 KTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLS 326
Cdd:pfam00063 142 KTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 327 NGN-IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVM 405
Cdd:pfam00063 222 QSGcYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDST 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 406 EFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNS 485
Cdd:pfam00063 302 ELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 486 FEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFV 565
Cdd:pfam00063 382 FEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 566 DKLIQEQGTHTKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQ 645
Cdd:pfam00063 459 DKLYSTFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAA 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 646 vagmNETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 725
Cdd:pfam00063 538 ----NESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRI 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 726 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:pfam00063 614 RRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-798 |
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: 1000.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 80 NPPKFTKVEDMAELTCLNEASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnippespkpvklqaQHAVGELERQLLQANPI 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS---------------------NTEVGSVEDQILESNPI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 240 LESFGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGF 319
Cdd:smart00242 140 LEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 320 NSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNT-AAQKLC 397
Cdd:smart00242 220 EDYRYLNQGGcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 398 HLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAG 477
Cdd:smart00242 300 ELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 478 FEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP 557
Cdd:smart00242 379 FEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFP 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 558 KATDKTFVDKLIQEQGTHTKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDv 637
Cdd:smart00242 456 KGTDQTFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 638 drivgldqvagmnetafGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 717
Cdd:smart00242 534 -----------------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYL 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 718 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFRTGVLAHLEEER 797
Cdd:smart00242 597 GVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
.
gi 1604804600 798 D 798
Cdd:smart00242 677 E 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1448 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 912.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 36 VWIPSERNGFEAASVREERGDEVVVELA---ENGKKAVVNKDDIQ--KMNPPKFTKVEDMAELTCLNEASVLYNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 191 VIQYLAHVASSHkgrkdhnippespkpvklqaQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVIGY 270
Cdd:COG5022 172 IMQYLASVTSSS--------------------TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 271 IVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQETMEAMH 349
Cdd:COG5022 232 ICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 350 IMSFGHEEILAMLKVVSSVLQFGNINFKKERNsDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTK 429
Cdd:COG5022 312 TIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 430 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFIL 509
Cdd:COG5022 391 EQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 510 EQEEYQREGIEWSFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVDKLIQ--EQGTHTKFQKPRQLKDK 587
Cdd:COG5022 470 EQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 588 adFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVgldqvagmnetafgatyktKKGMFRT 667
Cdd:COG5022 548 --FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPT 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 668 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 747
Cdd:COG5022 607 LGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILS 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 748 PNA----IPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFRTGVLAHLEEERDLKITDIIIYFQSVCRGYLARKAFAK 823
Cdd:COG5022 687 PSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQ 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 824 KQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEELQAKDEELVKVkerQLKVENELVEMERKHQqlieE 903
Cdd:COG5022 767 ALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEV----E 839
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 904 KNILAEQLHAETELFAEAEEmRVRLLSRKQELEEILhdleSRVEEEEERNQSLQNEKKKMQShiqdleeqldeeeAARQK 983
Cdd:COG5022 840 FSLKAEVLIQKFGRSLKAKK-RFSLLKKETIYLQSA----QRVELAERQLQELKIDVKSISS-------------LKLVN 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 984 LQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--ISEMTSQLTEEEEKAKNLGKVKNKQEmMMVDLEERLKKE 1061
Cdd:COG5022 902 LELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKLKE-TSEEYEDLLKKS 980
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1062 EKTRQELEKAKRKLD---AETTDLQDQIVELQAQIEELKfQLTKKEEELQAALARSDEETlqknnalkqvrelqahlAEL 1138
Cdd:COG5022 981 TILVREGNKANSELKnfkKELAELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSES-----------------TEL 1042
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1139 QEDLESEKMcRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNH--EAQIQEMRQRQ 1216
Cdd:COG5022 1043 SILKPLQKL-KGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLvkPANVLQFIVAQ 1121
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1217 ATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCdvkTLQQAKTESEHKRKKLEAQLQEfmaRATEAERTKgELAER 1296
Cdd:COG5022 1122 MIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDG---LFWEANLEALPSPPPFAALSEK---RLYQSALYD-EKSKL 1194
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1297 SHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQD----SEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEE 1372
Cdd:COG5022 1195 SSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVpteySTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSS 1274
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1373 ARRNLEKQLQMVQSQMFETKKKLEEDLGSmeGLEEVKRKLQKDVELTSQCLEEKtmamdKMEKTKNRLQQELDDLM 1448
Cdd:COG5022 1275 YKLEEEVLPATINSLLQYINVGLFNALRT--KASSLRWKSATEVNYNSEELDDW-----CREFEISDVDEELEELI 1343
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-786 |
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: 851.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhaVGELERQLLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS----------------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFL-----SNGNIPI 332
Cdd:cd00124 145 GKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 333 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNS--DQASMPDNTAAQKLCHLLGLNVMEFTRA 410
Cdd:cd00124 225 DGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 411 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFQLNSFEQM 489
Cdd:cd00124 305 LTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 490 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLI 569
Cdd:cd00124 385 CINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 570 QEQGTHTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvgelwkdvdrivgldqvagm 649
Cdd:cd00124 462 SAHGSHPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ---------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 650 netafgatyktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQG 729
Cdd:cd00124 519 ----------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAG 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 730 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd00124 577 YPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-786 |
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: 774.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespKPVKLQAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPG---------KKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKsDLLLEGFN--SYRFLSNGNIPIPGQQ 336
Cdd:cd14927 152 KFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRI 416
Cdd:cd14927 231 DGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 417 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNE 496
Cdd:cd14927 311 KVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 497 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GTH 575
Cdd:cd14927 390 KLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 576 TKFQKPR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdriVGLDQVAgmnET 652
Cdd:cd14927 467 PNFQKPRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTE---DP 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 653 AFGATYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 731
Cdd:cd14927 541 KSGVKEKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFP 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 732 NRIVFQEFRQRYEILTPNAIPK-GFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14927 621 NRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-786 |
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: 760.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKPVKLQaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMK-----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNSYR--FLSNGNIPIPGQQD 337
Cdd:cd14913 149 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAILSPRI 416
Cdd:cd14913 228 AEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 417 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNE 496
Cdd:cd14913 307 KVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 497 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI-QEQGTH 575
Cdd:cd14913 386 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 576 TKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivgldqVAGMNETA 653
Cdd:cd14913 463 NNFQKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 FGATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 732
Cdd:cd14913 534 GKKKVAKKKGsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPN 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 733 RIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14913 614 RILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-786 |
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: 741.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvKLQAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK---------------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIPIPGQQD 337
Cdd:cd14909 146 KFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIK 417
Cdd:cd14909 226 GEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 418 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEK 497
Cdd:cd14909 306 VGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 498 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GTHT 576
Cdd:cd14909 385 LQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 577 KFQKPRQLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivgLDQVAGMNETA 653
Cdd:cd14909 462 PFQKPKPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD------HAGQSGGGEQA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 FGATYKtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 733
Cdd:cd14909 536 KGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNR 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 734 IVFQEFRQRYEILTPNAIpKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14909 615 MMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-786 |
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: 722.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklQAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK-----------------QSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHL-KSDLLLEGFNSYRFLSNGNIPIPGQQD 337
Cdd:cd14934 144 KFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIK 417
Cdd:cd14934 224 GEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 418 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEK 497
Cdd:cd14934 304 VGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 498 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GTHT 576
Cdd:cd14934 383 LQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 577 KFQKPRQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdKFVGELWKDvdrivgldqvagmNETA 653
Cdd:cd14934 460 NFLKPKGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFK-------------EEEA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 FGATYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 732
Cdd:cd14934 526 PAGSKKQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPN 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 733 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14934 606 RLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-786 |
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: 716.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET-------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIP-IPGQQD 337
Cdd:cd01380 141 KYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIK 417
Cdd:cd01380 221 AAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 418 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQMCINYTNE 496
Cdd:cd01380 301 TRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 497 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHT 576
Cdd:cd01380 381 KLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 577 K--FQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvgelwkdvdrivgldqvagmnetaf 654
Cdd:cd01380 457 NkhFKKPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR-------------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 655 gatyktKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 734
Cdd:cd01380 509 ------KK----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRW 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 735 VFQEFRQRYEILTPNAIPKGfMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd01380 579 TYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-786 |
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: 700.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPkpvklqaqhAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTP---------GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--SYRFLSNGNIPIPGQQ 336
Cdd:cd14917 148 KFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAILSPR 415
Cdd:cd14917 227 DAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 416 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTN 495
Cdd:cd14917 306 VKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 496 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GT 574
Cdd:cd14917 385 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 575 HTKFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivgldqVAGMNET 652
Cdd:cd14917 462 SNNFQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 653 AFGATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 731
Cdd:cd14917 533 IEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 732 NRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14917 613 NRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-786 |
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: 697.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvklqaqhaVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK------------------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEhlKSDLLLEGFN--SYRFLSNGNIPIPGQQ 336
Cdd:cd14929 143 KFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRI 416
Cdd:cd14929 221 DAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 417 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNE 496
Cdd:cd14929 301 KVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 497 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GTH 575
Cdd:cd14929 380 KLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 576 TKFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivglDQVAGmNETA 653
Cdd:cd14929 457 VHFQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 FGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 733
Cdd:cd14929 529 FGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNR 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 734 IVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14929 609 LLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-786 |
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: 684.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnippespkpvklqAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN-------------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--SYRFLSNGNIPIPGQQ 336
Cdd:cd14916 149 KFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNTA-AQKLCHLLGLNVMEFTRAILSPR 415
Cdd:cd14916 228 DSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 416 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTN 495
Cdd:cd14916 307 VKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 496 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GT 574
Cdd:cd14916 386 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 575 HTKFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdrivgldQVAGMNET 652
Cdd:cd14916 463 SNNFQKPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 653 AFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 732
Cdd:cd14916 536 GKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPN 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 733 RIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14916 616 RILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-786 |
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: 682.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 101 VLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 181 GAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpVKLQaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFGKF 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEES--------GKMQ-----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 261 IRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIPIPGQQDKD 339
Cdd:cd14918 150 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 340 NFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd14918 230 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd14918 309 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI-QEQGTHTK 577
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 578 FQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdrivgldqVAGMNETAFG 655
Cdd:cd14918 465 FQKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 656 ATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 735
Cdd:cd14918 537 KGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 736 FQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14918 617 YGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-786 |
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: 680.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvKLQAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE-----------EITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14912 151 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAILSPRIK 417
Cdd:cd14912 231 EELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 418 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEK 497
Cdd:cd14912 310 VGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 498 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI-QEQGTHT 576
Cdd:cd14912 389 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 577 KFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAf 654
Cdd:cd14912 466 NFQKPKVVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGG- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 655 gatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 734
Cdd:cd14912 545 ----KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 735 VFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14912 621 LYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-786 |
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: 680.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKPVKLQaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQ-----GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNSYR--FLSNGNIPIPGQQD 337
Cdd:cd14923 150 FIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAILSPRI 416
Cdd:cd14923 229 SEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 417 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNE 496
Cdd:cd14923 308 KVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 497 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI-QEQGTH 575
Cdd:cd14923 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 576 TKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdriVGLDQVAGMNETA 653
Cdd:cd14923 464 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 FGatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 733
Cdd:cd14923 541 GG---KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 734 IVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14923 618 ILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-786 |
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: 677.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKLQaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQ-----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14910 151 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAILSPRIK 417
Cdd:cd14910 231 EELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 418 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEK 497
Cdd:cd14910 310 VGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 498 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GTHT 576
Cdd:cd14910 389 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 577 KFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdrivgldqVAGMNETAF 654
Cdd:cd14910 466 NFQKPKPAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 655 GATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 733
Cdd:cd14910 538 GKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 734 IVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14910 618 ILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-786 |
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: 671.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKLQaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQ-----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNSYRF--LSNGNIPIPGQQD 337
Cdd:cd14915 151 FIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAILSPRI 416
Cdd:cd14915 230 QEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 417 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNE 496
Cdd:cd14915 309 KVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 497 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ-GTH 575
Cdd:cd14915 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 576 TKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgldqvAGMNETA 653
Cdd:cd14915 465 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------TAEAEGG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 FGATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 732
Cdd:cd14915 537 GGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 733 RIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14915 617 RILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-786 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 638.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvklqaQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS--------------------ESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-IPIPGQQDK 338
Cdd:cd01378 142 YMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFkKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd01378 222 ADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 G---RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTN 495
Cdd:cd01378 301 GgggRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 496 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVDKLIQEQGT 574
Cdd:cd01378 381 EKLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 575 HTKFQKPRQLKD--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRivgldqvagmnet 652
Cdd:cd01378 458 HPHFECPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 653 afgatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 732
Cdd:cd01378 525 ------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAY 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 733 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd01378 599 RQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-786 |
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: 636.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGE--HLKSDLLLEGFNSYRFLS-NGNIPIPGQQ 336
Cdd:cd14883 138 FIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNIN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK-ERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPR 415
Cdd:cd14883 218 DKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 416 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQMCINYTN 495
Cdd:cd14883 298 INVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 496 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLIQEQGTH 575
Cdd:cd14883 377 EKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKH 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 576 TKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrIVGLDQVAGMNETAFG 655
Cdd:cd14883 454 PYYEKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTT 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 656 ATyKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 735
Cdd:cd14883 533 SR-GTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLT 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 736 FQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14883 611 FKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-786 |
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: 630.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG------------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-IPIPGQQDK 338
Cdd:cd01383 136 LIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKV 418
Cdd:cd01383 216 KKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 419 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKL 498
Cdd:cd01383 296 GGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 499 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF 578
Cdd:cd01383 376 QQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 579 QKPRqlkDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELwkdvdrivgldqVAGMNETAFGATY 658
Cdd:cd01383 453 KGER---GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF------------ASKMLDASRKALP 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 659 KTKKGMF----RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 734
Cdd:cd01383 517 LTKASGSdsqkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRM 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 735 VFQEFRQRYEILTPNAIpKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd01383 597 THQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-786 |
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 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVAsshkgrkdhnippespkpvklqaQHAVGE---LERQLLQANPILESFGNAKTVKNDNS 254
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----------------------GRAVTEgrsVEQQVLESNPLLEAFGNAKTVRNNNS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 255 SRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-IPIP 333
Cdd:cd01384 138 SRFGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 334 GQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKL---CHLLGLNVMEFTRA 410
Cdd:cd01384 218 GVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 411 ILSpRIKVGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQM 489
Cdd:cd01384 298 LCK-RVIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 490 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLI 569
Cdd:cd01384 376 CINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLY 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 570 QEQGTHTKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRivgldqvagm 649
Cdd:cd01384 453 QTLKDHKRFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR---------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 650 netafgatYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 728
Cdd:cd01384 521 --------EGTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCA 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 729 GFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIQALELDPnlFRIGQSKIFFR 786
Cdd:cd01384 593 GYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-786 |
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: 600.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS------------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-IPIPGQQD 337
Cdd:cd01381 137 KYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK--ERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPR 415
Cdd:cd01381 217 AAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 416 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFQLNSFEQMCINY 493
Cdd:cd01381 297 IFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 494 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVDKLIQEQ 572
Cdd:cd01381 377 ANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTH 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 573 GTHTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgldqvagmnet 652
Cdd:cd01381 453 GNNKNYLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI-------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 653 AFGATYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 732
Cdd:cd01381 518 SMGSETRKKS---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPI 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 733 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd01381 595 RHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-786 |
7.71e-179 |
|
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: 558.02 E-value: 7.71e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvklqaqhaVGELERQLLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG-----------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLegfnsyrflsngnipIPGQQD 337
Cdd:cd01382 138 GKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERN-SDQASMPDNTAAQKL---CHLLGLNVMEF-----T 408
Cdd:cd01382 203 VGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSdSGGGCNVKPKSEQSLeyaAELLGLDQDELrvsltT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 409 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFQLNSFEQ 488
Cdd:cd01382 283 RVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 489 MCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKL 568
Cdd:cd01382 361 FCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 569 IQEQGTHTKFQKPRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdri 640
Cdd:cd01382 438 HQKHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFES---- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 641 vgldqvagmnETAFGATYKTKKG--MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 718
Cdd:cd01382 514 ----------STNNNKDSKQKAGklSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSG 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 719 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd01382 584 MVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-786 |
1.58e-178 |
|
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: 557.08 E-value: 1.58e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavgeLERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG------------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNSYRFLSNGN-IPIPGQQD 337
Cdd:cd14872 137 KWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCH---LLGLNVMEFTRAILSP 414
Cdd:cd14872 215 VADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 415 RIKV-GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINY 493
Cdd:cd14872 295 LMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 494 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLIQEQG 573
Cdd:cd14872 375 TNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 574 THTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgLDQvagmneta 653
Cdd:cd14872 452 AKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQ-------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 fgatyKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 733
Cdd:cd14872 520 -----KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFR 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 734 IVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14872 592 YSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-786 |
1.04e-175 |
|
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: 550.15 E-value: 1.04e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhniPPESPKPVKLQAQHaVGELERQLLQANPILESFGNAKTVKNDN 253
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGA----SGEGEAASEAIEQT-LGSLEDRVLSSNPLLESFGNAKTLRNDN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 254 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIP 333
Cdd:cd14890 156 SSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 334 GQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmpDNTAAQKLCH---LLGLNVMEFTRA 410
Cdd:cd14890 236 SCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 411 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQMC 490
Cdd:cd14890 314 LLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 491 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVDK 567
Cdd:cd14890 393 INYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 568 LIQEQGT-------------HTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvgelw 634
Cdd:cd14890 471 LHASFGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 635 kdvdrivgldqvagmnetafgatyKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 714
Cdd:cd14890 542 ------------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQL 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 715 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14890 596 KYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-786 |
2.70e-171 |
|
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: 537.80 E-value: 2.70e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnippesPKPVKLQAQhavgelerQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------------QRRNNLVTE--------QILEATPLLEAFGNAKTVRNDNSSRFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNG-NIPIPGQQD 337
Cdd:cd01387 138 KYLEVFFEG-GVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK---ERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSP 414
Cdd:cd01387 217 ADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 415 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYT 494
Cdd:cd01387 297 VTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 495 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLIQEQGT 574
Cdd:cd01387 376 NENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHAL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 575 HTKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNetaf 654
Cdd:cd01387 453 NELYSKPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGK---- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 655 gATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 734
Cdd:cd01387 527 -GRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 735 VFQEFRQRYEILTPNAIPKGfMDGKQACERMIQALELDP-NLFRIGQSKIFFR 786
Cdd:cd01387 606 PFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-786 |
3.18e-169 |
|
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: 532.43 E-value: 3.18e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkpvklqaqhavgeleRQLLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI--------------------KKIIEVNPLLESFGNAKTVRNDNSSRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNSYRFL-SNGNIPIPGQQ 336
Cdd:cd14903 138 GKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGMS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASM--PDNTAAQKLCHLLGLNVMEFTRAILSP 414
Cdd:cd14903 216 DRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 415 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQMCINYT 494
Cdd:cd14903 296 TMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 495 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLiqeQGT 574
Cdd:cd14903 375 NEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKL---SSI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 575 HTKFQK----PRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrIVGLDQVAGMN 650
Cdd:cd14903 448 HKDEQDviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 651 ETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 730
Cdd:cd14903 523 LARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAY 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 731 PNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIQALELD-PNLFRIGQSKIFFR 786
Cdd:cd14903 603 PNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-786 |
2.25e-162 |
|
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: 513.19 E-value: 2.25e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVasshkgrkdhnippeSPKPVKLQAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVI---------------SQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLS-NGNIPIPGQQ 336
Cdd:cd14873 146 GKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTIS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKkerNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRI 416
Cdd:cd14873 226 DQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 417 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQMCINYTN 495
Cdd:cd14873 303 FLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYAN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 496 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQGTH 575
Cdd:cd14873 380 EKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANN 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 576 TKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgldqvAGMNETAFG 655
Cdd:cd14873 456 HFYVKPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLK 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 656 ATYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 735
Cdd:cd14873 526 CGSKHRR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRP 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 736 FQEFRQRYEILTPNAIPKGFMDGKqaCERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14873 603 FQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-786 |
4.62e-162 |
|
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: 513.85 E-value: 4.62e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLahVASSHKGrkdhnippespkpvklqaqHAVGeLERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG-------------------YGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLS-NGNIPIPGQQD 337
Cdd:cd01385 139 KFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKER-NSDQASMPDNTAAQKL-CHLLGLNVMEFTRAILSPR 415
Cdd:cd01385 219 KYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 416 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFQLNSFEQMCI 491
Cdd:cd01385 299 TVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 492 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLIQE 571
Cdd:cd01385 378 NYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 572 QGTHTKFQKPrQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELwkdvdriVGLDQVA---- 647
Cdd:cd01385 455 HKDNKYYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfrw 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 648 GMNETAFGATY--------------------------------KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCII 695
Cdd:cd01385 526 AVLRAFFRAMAafreagrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIK 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 696 PNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMiqalELDPNL 775
Cdd:cd01385 604 SNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL----NLDRDN 679
|
730
....*....|.
gi 1604804600 776 FRIGQSKIFFR 786
Cdd:cd01385 680 YQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-784 |
1.61e-161 |
|
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: 511.26 E-value: 1.61e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEIPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 171 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPPESpkpvklqaqhavgeLERQLLQANPILESFGNAKT 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN--------------VRDRVLESNPILEAFGNART 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 249 VKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFL--S 326
Cdd:cd14901 146 NRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 327 NGNIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF-KKERNSDQASMPDNTAAQKLCHLLGLNVM 405
Cdd:cd14901 226 QCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 406 EFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFQLN 484
Cdd:cd14901 306 VLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 485 SFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKAT 560
Cdd:cd14901 386 SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 561 DKTFVDKLIQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGElwkdvdri 640
Cdd:cd14901 459 DEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS-------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 641 vgldqvagmnetafgatyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 720
Cdd:cd14901 531 --------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 721 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERM-----IQALELDPNLFRIGQSKIF 784
Cdd:cd14901 585 EAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMsqlqhSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-748 |
2.76e-159 |
|
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: 505.38 E-value: 2.76e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS--------------------LVEAQVLESNPLLEAFGNARTLRNDNSSRF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFD---------VIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNG 328
Cdd:cd14888 140 GKFIELQFSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGAD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 329 NIP------------------------IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQ 384
Cdd:cd14888 220 AKPisidmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 385 ASMPDNTAAQKL---CHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR 461
Cdd:cd14888 300 GAVVSASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 462 TKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpA 541
Cdd:cd14888 380 SKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--E 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 542 NPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATL 621
Cdd:cd14888 457 KPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEV 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 622 LHQSTDKFVGELWKD-VDRIVGLdqvagmnetafgatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 700
Cdd:cd14888 535 IKNSKNPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQN 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1604804600 701 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 748
Cdd:cd14888 600 VPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-786 |
5.53e-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: 5.53e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEI---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKpvklqAQHAVGELERQLLQANPILESFGNAKTVKN 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKG-----AANAHESIEECVLLSNLILEAFGNAKTIRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 252 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-I 330
Cdd:cd14892 150 DNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 331 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF----KKERNSDQASMPDNTAaqKLCHLLGLNVME 406
Cdd:cd14892 230 EVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFeenaDDEDVFAQSADGVNVA--KAAGLLGVDAAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 407 FTRAILSPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIA 476
Cdd:cd14892 308 LMFKLVTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 477 GFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWF 556
Cdd:cd14892 388 GFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 557 P-KATDKTFVDKLIQEQ-GTHTKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvgelw 634
Cdd:cd14892 465 KrKTTDKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 635 kdvdrivgldqvagmnetafgatyktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 714
Cdd:cd14892 536 ------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQL 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 715 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IQALELDPNLFRIGQSKIFFR 786
Cdd:cd14892 579 IYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-786 |
2.10e-158 |
|
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: 501.81 E-value: 2.10e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVAsshkgrKDHNippespkpvklqaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN-----------------RTLEEKILQVNPLMEAFGNARTVINDNSSRFGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGagehLKSDLLLEGFNS-------YRFLSNGNIPI 332
Cdd:cd01379 139 YLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKLpenkpprYLQNDGLTVQD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 333 PGQQD--KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF----KKERNSDQASMPDNTAAQKLCHLLGLNVME 406
Cdd:cd01379 215 IVNNSgnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 407 FTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFQLN 484
Cdd:cd01379 295 LQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 485 SFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKT 563
Cdd:cd01379 375 SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 564 FVDKLiqEQGTHTKFQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGElwkdvdrivgl 643
Cdd:cd01379 451 LVEKF--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ----------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 644 dqvagmnetafgatyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGI 723
Cdd:cd01379 517 -----------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETT 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 724 RICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIQALELDPnlFRIGQSKIFFR 786
Cdd:cd01379 574 RIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-786 |
1.39e-156 |
|
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: 496.91 E-value: 1.39e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVASShkgrkDHnippespkpvklqaqhavGELERQLLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----DD------------------SDLLDKIVQINPLLEAFGNASTVMNDNSSRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQD 337
Cdd:cd14897 138 GKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFND 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 -------KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRA 410
Cdd:cd14897 218 seeleyyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 411 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFQLNSF 486
Cdd:cd14897 298 LISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 487 EQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVD 566
Cdd:cd14897 378 DQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 567 KLIQEQGTHTKFQKPrqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKdvdrivgldqv 646
Cdd:cd14897 455 KLNKYCGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 647 agmnetafgatyktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 726
Cdd:cd14897 522 -----------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIR 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 727 RQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIQALELDPnlFRIGQSKIFFR 786
Cdd:cd14897 579 RDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-746 |
2.33e-145 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 465.55 E-value: 2.33e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEIPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkdhnippESPKPVKLQAQHAVGELERQLLQANPILESF 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------------DNNLAASVSMGKSTSGIAAKVLQTNILLESF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 244 GNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEhlksdlllegfnsyr 323
Cdd:cd14900 149 GNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE--------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 324 flsngnipipGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSD-QASMPDNTAAQKL------ 396
Cdd:cd14900 214 ----------AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaa 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 397 CHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGI 472
Cdd:cd14900 284 ATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 473 LDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDE 552
Cdd:cd14900 364 LDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 553 ECWFPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSTdkfvge 632
Cdd:cd14900 441 ECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA------ 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 633 lwkdVDrivgldqvagmnetafgatyktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 712
Cdd:cd14900 507 ----VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLN 556
|
650 660 670
....*....|....*....|....*....|....
gi 1604804600 713 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 746
Cdd:cd14900 557 QLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-749 |
1.38e-142 |
|
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: 459.50 E-value: 1.38e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EIPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESpkpvKLQAQHAVGELERQLLQANPILESFGNAKTV 249
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSS----IRATSKSTKSIEQKILSCNPILEAFGNAKTV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 250 KNDNSSRFGKFIRINFD-VIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLE----GFNSYRF 324
Cdd:cd14907 157 RNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 325 LSNGNIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFK-KERNSDQASMPDNTAA-QKLCHLLGL 402
Cdd:cd14907 237 KKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 403 NVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDI 475
Cdd:cd14907 317 DEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 476 AGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIDLIERPanPPGVLALLDEE 553
Cdd:cd14907 397 FGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 554 CWFPKATDKTFVDKLIQEQGTHTKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGEL 633
Cdd:cd14907 474 CKLATGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 634 WkdvdriVGLDQVAGMNETAFGATYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 713
Cdd:cd14907 553 F------SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670
....*....|....*....|....*....|....*.
gi 1604804600 714 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 749
Cdd:cd14907 623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-786 |
1.09e-140 |
|
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: 453.59 E-value: 1.09e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 101 VLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSSR 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS------------------------QLEQQILQVNPLLEAFGNAQTVMNDNSSR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 257 FGKFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG--AGEHLKSDLLLEGFnsYRFLSN--GNIPI 332
Cdd:cd14889 139 FGKYIQLRFRN-GHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNgaGCKRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 333 PgQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFkkERNSDQASMPDNTAAQKL---CHLLGLNVMEFTR 409
Cdd:cd14889 216 V-QYWKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 410 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFQLNSFE 487
Cdd:cd14889 293 TLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 488 QMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATDKTFVDK 567
Cdd:cd14889 373 QACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 568 LIQEQGTHTKFQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWK-DVDRIVGLDQV 646
Cdd:cd14889 450 LNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPR 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 647 AGM---NETAFGATYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGI 723
Cdd:cd14889 528 AKLpqaGSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETI 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 724 RICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIQALELDPnlFRIGQSKIFFR 786
Cdd:cd14889 602 RIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-786 |
2.81e-139 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 449.11 E-value: 2.81e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 172 QSILCTGESGAGKTENTKKVIQYLAHvaSSHKGRKDHNipPESPKPVKLQAQHAVgELERQLLQANPILESFGNAKTVKN 251
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTT--RAVGGKKASG--QDIEQSSKKRKLSVT-SLDERLMDTNPILESFGNAKTLRN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 252 DNSSRFGKFIRINFDVIGY-IVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN- 329
Cdd:cd14891 151 HNSSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGc 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 330 IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNS----DQASMPDNTAAQKLCHLLGLNVM 405
Cdd:cd14891 231 VSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSegeaEIASESDKEALATAAELLGVDEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 406 EFTRAILSPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFQL- 483
Cdd:cd14891 311 ALEKVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETk 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 484 NSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIDLIErpANPPGVLALLDEECWFPK 558
Cdd:cd14891 389 NDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIA--SKPNGILPLLDNEARNPN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 559 ATDKTFVDKLIQEQGTHTKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQStDKFvgelwkdv 637
Cdd:cd14891 461 PSDAKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKF-------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 638 drivgLDQVAGMNEtafgatyktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 717
Cdd:cd14891 531 -----SDQMQELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCS 575
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 718 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14891 576 GILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-786 |
1.35e-133 |
|
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: 433.60 E-value: 1.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkpvklqaqhavgelerQLLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA--------------------KVIDVNPLLESFGNAKTTRNDNSSRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFL--SNGNIPIPGQ 335
Cdd:cd14904 138 GKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 336 QDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK--ERNSDQASMpdnTAAQKLCHLLGLNVMEFTRAILS 413
Cdd:cd14904 218 DDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKsdENGSRISNG---SQLSQVAKMLGLPTTRIEEALCN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 414 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINY 493
Cdd:cd14904 295 RSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 494 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKL---IQ 570
Cdd:cd14904 375 ANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 571 EQGTHTKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgldqvaGMN 650
Cdd:cd14904 451 TKKDNESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APS 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 651 ETAFGATYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 730
Cdd:cd14904 520 ETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 731 PNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIQAL-ELDPNLFRIGQSKIFFR 786
Cdd:cd14904 599 PSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-786 |
1.68e-133 |
|
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: 433.05 E-value: 1.68e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkpvklqaqhavgeleRQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL--------------------RQPEDVLPILESFGHAKTILNANASRFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNI-PIPGQQD 337
Cdd:cd14896 138 QVLRLHLQH-GVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKED 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK-ERNSDQ-ASMPDNTAAQKLCHLLGLNVMEFTRAILSPR 415
Cdd:cd14896 217 AQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSsERESQEvAAVSSWAEIHTAARLLQVPPERLEGAVTHRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 416 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQMCINYT 494
Cdd:cd14896 297 TETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 495 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLIQEQGT 574
Cdd:cd14896 377 SERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 575 HTKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGmnetaf 654
Cdd:cd14896 454 HPSYAKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------ 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 655 gatyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 734
Cdd:cd14896 526 ------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRV 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 735 VFQEFRQRYEILTpNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14896 594 PFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-786 |
4.28e-133 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 433.18 E-value: 4.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------IPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESpkpvklqaqhavGELERQLLQANPILESFGNAKT 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGK------------LSIMDRVLQSNPILEAFGNART 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 249 VKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGE--------HLKSDLLLEGFN 320
Cdd:cd14908 149 LRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 321 SYRFLSNGNIPIPGQ-QDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNsDQASMPDNTAAQK---- 395
Cdd:cd14908 229 EFHYTGQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclar 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 396 LCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGIL 473
Cdd:cd14908 308 VAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 474 DIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEE 553
Cdd:cd14908 387 DIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 554 CWFP-KATDKTFVDKLI--------QEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllh 623
Cdd:cd14908 464 CRLGiRGSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 624 qstdkfvgelwkdvdrivgldqvagmnetafgatyKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAG 703
Cdd:cd14908 536 -----------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPD 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 704 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMI 766
Cdd:cd14908 580 LVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLS 658
|
730 740
....*....|....*....|....
gi 1604804600 767 QALELDPNL----FRIGQSKIFFR 786
Cdd:cd14908 659 PAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-748 |
5.17e-130 |
|
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: 425.85 E-value: 5.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEIPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 169 REDQSILCTGESGAGKTENTKKVIQYLAHVasshkGRKDHNIPPESPKPVKLQaqhavgeleRQLLQANPILESFGNAKT 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-----GRDQSSTEQEGSDAVEIG---------KRILQTNPILESFGNAQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 249 VKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSN- 327
Cdd:cd14902 147 IRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSy 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 328 --GNIPIPGQQDKDN--FQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDqasmpDNTAAQKLC------ 397
Cdd:cd14902 227 gpSFARKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQE-----DATAVTAASrfhlak 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 398 --HLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGA 467
Cdd:cd14902 302 caELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEEL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 468 SFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVL 547
Cdd:cd14902 382 ATIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 548 ALLDEECWFPKATDKTFVDKLIQeqgTHTKfqkprqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTD 627
Cdd:cd14902 459 SLLDQECLMPKGSNQALSTKFYR---YHGG---------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 628 kfvgelwkDVDRIVGLDQVAGMNETAFGATYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKL 705
Cdd:cd14902 527 --------EVVVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1604804600 706 EPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 748
Cdd:cd14902 599 DRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-839 |
2.69e-125 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 415.97 E-value: 2.69e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 97 NEASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEI-PPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvklqaQHAVgelerqlLQANPILESFGNAKTVKNDNSS 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI------------QNAI-------MAANPVLEAFGNAKTIRNNNSS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 256 RFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQ 335
Cdd:PTZ00014 246 RFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGI 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 336 QDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF--KKERNSDQASM--PDNTAA-QKLCHLLGLNVMEFTRA 410
Cdd:PTZ00014 326 DDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 411 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFQLNSFEQMC 490
Cdd:PTZ00014 406 LTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLF 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 491 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLIQ 570
Cdd:PTZ00014 485 INITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNT 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 571 EQGTHTKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGldqvagmn 650
Cdd:PTZ00014 562 NLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG-------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 651 etafgatyKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 730
Cdd:PTZ00014 633 --------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGF 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 731 PNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFF-RTGV--LAHLEEERDLKITDIIIY 807
Cdd:PTZ00014 703 SYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAAkeLTQIQREKLAAWEPLVSV 782
|
730 740 750
....*....|....*....|....*....|..
gi 1604804600 808 FQSVCRGYLARKAFAKKqqqlsaLKVLQRNCA 839
Cdd:PTZ00014 783 LEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-786 |
3.93e-123 |
|
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: 405.15 E-value: 3.93e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPEspkpvKLQAqhavgelerqllqANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE-----KLNA-------------ALTVLEAFGNVRTALNGNATRFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSyrflSNGNIPIPGQQDK 338
Cdd:cd01386 139 QLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 D------NFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAI- 411
Cdd:cd01386 215 DkqkaaaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIf 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 412 -----------LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGfei 480
Cdd:cd01386 295 khhlsggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 481 FQLN---------SFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERP---ANPP---- 544
Cdd:cd01386 371 FQNPahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlr 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 545 -----GVLALLDEECWFPKATDKTFVDKLIQEQG--THTKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDP 613
Cdd:cd01386 451 dedrrGLLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENP 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 614 LNDNVATLLHQSTDKFvgelwkdvdrivgldqvAGMnetafgatykTKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRC 693
Cdd:cd01386 531 SAQNATQLLQESQKET-----------------AAV----------KRKSPCLQI----KFQVDALIDTLRRTGLHFVHC 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 694 IIPNHEkrAGKLEPH--------------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF---- 755
Cdd:cd01386 580 LLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnse 657
|
730 740 750
....*....|....*....|....*....|..
gi 1604804600 756 -MDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd01386 658 vADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
105-747 |
6.95e-123 |
|
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: 405.11 E-value: 6.95e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 105 LKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------IPPHIYAISESAYRCMLQ-------DRE 170
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhepgaSKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvklQAQHAVGEleRQLLQANPILESFGNAKTVK 250
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSS------------KRRRAISG--SELLSANPILESFGNARTLR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 251 NDNSSRFGKFIRINF-----DVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNS--YR 323
Cdd:cd14895 146 NDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAqeFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 324 FLSNGNIPI--PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSD---------------QAS 386
Cdd:cd14895 226 YISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 387 MPDNTAAQKL---CHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK 463
Cdd:cd14895 306 PSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 464 ----------RQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPC 533
Cdd:cd14895 386 falnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVC 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 534 IDLIErpANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWLMKNM 611
Cdd:cd14895 465 LEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 612 DPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAFGATYKTKKGmfrtVGQLYKESLTKLMATLRNTNPNFV 691
Cdd:cd14895 541 DQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYI 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 692 RCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 747
Cdd:cd14895 617 RCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-784 |
2.23e-122 |
|
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: 401.67 E-value: 2.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvklqaQHAVgelerqlLQANPILESFGNAKTVKNDNSSRF 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI------------QTAI-------MAANPVLEAFGNAKTIRNNNSSRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQD 337
Cdd:cd14876 139 GRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 338 KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKErnsDQASMPDntAA----------QKLCHLLGLNVMEF 407
Cdd:cd14876 219 VADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 408 TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFQLNSF 486
Cdd:cd14876 294 KRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 487 EQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVD 566
Cdd:cd14876 372 EQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 567 KLIQEQGTHTKFqKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGldqv 646
Cdd:cd14876 449 ACVSKLKSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG---- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 647 agmnetafgatyKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 726
Cdd:cd14876 524 ------------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLR 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 727 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIF 784
Cdd:cd14876 590 QLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-748 |
5.05e-117 |
|
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: 386.90 E-value: 5.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEIPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvklqaqhaVGELERQLLQANPILESFGNAKTVKNDNS 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKI---------------AERIEQRILNSNPVMEAFGNACTLRNNNS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 255 SRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIpg 334
Cdd:cd14880 146 SRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 335 qqDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTA---AQKLCHLLGLNVMEFTRAI 411
Cdd:cd14880 224 --EEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 412 LSPRIKVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQM 489
Cdd:cd14880 302 QIRTIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 490 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLI 569
Cdd:cd14880 382 CINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 570 QEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGM 649
Cdd:cd14880 459 ESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 650 NETAfgatyktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQG 729
Cdd:cd14880 539 SRAP-----------VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAG 607
|
650
....*....|....*....
gi 1604804600 730 FPNRIVFQEFRQRYEILTP 748
Cdd:cd14880 608 FPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-749 |
3.43e-114 |
|
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: 380.48 E-value: 3.43e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEIPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 177 TGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaQHAVGELERQLLQANPILESFGNAKTVKNDNSSR 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNN-------------NNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 257 FGKFIRINFDVIGYIV-GANIETYLLEKSR-AIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEG-FNSYRFL-------- 325
Cdd:cd14906 148 FGKFLKIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvis 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 326 ------SNGNIPIPGQQDKD-NFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERN-SDQASMPDNTAA--QK 395
Cdd:cd14906 228 sfksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDfSKYAYQKDKVTAslES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 396 LCHLLGLNVMEFTRAILSPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TK 463
Cdd:cd14906 308 VSKLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 464 RQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANp 543
Cdd:cd14906 388 KKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 544 pGVLALLDEECWFPKATDKTFVDKLIQE-QGTHTKFQkpRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLL 622
Cdd:cd14906 466 -GILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 623 HQSTDKFVGELWKdvdrivgldqvagMNETAFGATYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRA 702
Cdd:cd14906 542 LASSNFLKKSLFQ-------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDC 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1604804600 703 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 749
Cdd:cd14906 608 NNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-786 |
1.20e-111 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 371.45 E-value: 1.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEIPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 176 CTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnippeSPKPVKLQAQHAVGElerQLLQANPILESFGNAKTVKNDNSS 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMH-----------SSNTSQRSIADKIDE---NLKWSNPVMESFGNARTVRNDNSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 256 RFGKFIRINFD-VIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDL-LLEGFNSYRFLSNGNI--- 330
Cdd:cd14875 147 RFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvr 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 331 -PIPGQ--QDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNsDQASMPDNTAAQKLCHLLGLNVMEF 407
Cdd:cd14875 227 rGVDGKtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 408 TRAILsprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFQLNSF 486
Cdd:cd14875 306 RECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 487 EQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVD 566
Cdd:cd14875 383 EQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 567 KLIQEQGTHTK-FQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELwkdvdrivgLDQ 645
Cdd:cd14875 460 NLWDQWANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LST 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 646 VAGMNETAfgatyktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 725
Cdd:cd14875 530 EKGLARRK------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIAL 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 726 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIQALE-----LDPNlFRIGQSKIFFR 786
Cdd:cd14875 598 KRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-786 |
1.21e-110 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 368.06 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EIPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 173 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKND 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST-----------------------DVQSLILGSNPLLESFGNAKTLRNN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 253 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNI-P 331
Cdd:cd14886 138 NSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 332 IPGQQDKDNFQETMEAMHIMsFGHEEILAMLKVVSSVLQFGNINFKKERN--SDQASMPDNTAA-QKLCHLLGLNVMEFT 408
Cdd:cd14886 218 APGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 409 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFQLNS 485
Cdd:cd14886 297 QAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 486 FEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECwfpkatdktfv 565
Cdd:cd14886 373 YEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQC----------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 566 dkLIQeQGTHTKFQKPRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELW 634
Cdd:cd14886 439 --LIQ-TGSSEKFTSSCKSKIKNNsfipgkgsqcnFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 635 KDVDRIVGLdqvagmnetafgatyktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 714
Cdd:cd14886 516 SDIPNEDGN-----------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQL 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 715 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14886 577 ISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-743 |
6.09e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 354.02 E-value: 6.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEIPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 168 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPPESPKPVKLQAQhavgeLERQLLQANPILESFGNAK 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTT-----IEEQVLQSNPILEAFGNAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 248 TVKNDNSSRFGKFIRINF-DVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG-----AGEHLKSDLLLEGFNS 321
Cdd:cd14899 155 TVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 322 YRFLSNG--NIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF-----KKERNS--DQASMPDNTA 392
Cdd:cd14899 235 FRLLNQSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 393 A-----QKLCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT----- 462
Cdd:cd14899 315 GafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 463 ---------KRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPC 533
Cdd:cd14899 395 gadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRAC 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 534 IDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL---IQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKN 610
Cdd:cd14899 474 LELFEH--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKN 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 611 MDPLNDNVATLLHQSTDKFVGELWK-DVDRIVGLDQVAGMNETAFGATYKTKKGMFrTVGQLYKESLTKLMATLRNTNPN 689
Cdd:cd14899 552 KDSFCESAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATTPR 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 690 FVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 743
Cdd:cd14899 631 YVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-786 |
2.47e-94 |
|
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: 323.14 E-value: 2.47e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhavgeLERQLLQANPILESFGNAKTVK 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-------------------LEARLLQSGPVLEAFGNAHTVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 251 NDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLlegfnsyrflsngni 330
Cdd:cd14887 142 NANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS--------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 331 piPGQQDKD--NFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTA--------AQKLCHLL 400
Cdd:cd14887 207 --AGEGDPEstDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 401 -------GLNVMEFTRAILS--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVH 453
Cdd:cd14887 285 evkclssGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 454 RINKALDRTKR-------------QGASFIGILDIAGFEIFQ---LNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQRE 517
Cdd:cd14887 365 RINAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 518 G--IEWSFIDFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVDKL 568
Cdd:cd14887 445 GvfQNQDCSAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 569 IQEQGTHTKFQK--PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKFVgelwkdvdRIVGLDQV 646
Cdd:cd14887 525 NKNIINSAKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKN 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 647 AGMNetafgaTYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 726
Cdd:cd14887 596 SGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVM 666
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 727 RQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 786
Cdd:cd14887 667 ADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-750 |
4.68e-94 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 317.61 E-value: 4.68e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeIPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT------------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDviGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLlegfNSYRFLSNGNIPIPGQQDKD 339
Cdd:cd14898 134 RIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 340 NFQETMEAMHIMSFGHEEILAMlkvvsSVLQFGNINFKkerNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKVG 419
Cdd:cd14898 208 MTCSAMKSLGIANFKSIEDCLL-----GILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVK 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 420 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQ 499
Cdd:cd14898 280 GETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 500 QLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLiqeqgthTKFQ 579
Cdd:cd14898 357 NDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 580 KPRqLKDKADFCII--HYAGKVDYKADEWLMKNMDPlndnvatllhqstdkfvGELwkdvdRIVGLDQVagmnetafgAT 657
Cdd:cd14898 426 NGF-INTKARDKIKvsHYAGDVEYDLRDFLDKNREK-----------------GQL-----LIFKNLLI---------ND 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 658 YKTKKGMFRtvgqLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 737
Cdd:cd14898 474 EGSKEDLVK----YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKD 549
|
650
....*....|...
gi 1604804600 738 EFRQRYEILTPNA 750
Cdd:cd14898 550 RFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-786 |
5.40e-90 |
|
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: 308.28 E-value: 5.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEIPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSS 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT-----------------------TFDSRFKHVNCILEAFGHAKTTLNDLSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 256 RFGKFIRINF-DVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNG----NI 330
Cdd:cd14878 138 CFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 331 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRA 410
Cdd:cd14878 218 TAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 411 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFQLNSFE 487
Cdd:cd14878 298 LTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 488 QMCINYTNEKLQQLFNHTMFILEQEEYQREGIewsfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWF 556
Cdd:cd14878 378 QLCVNMTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQM 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 557 PKATDKTFVDKL---IQEQGTHTKFQKPRQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQST 626
Cdd:cd14878 445 IWSVEPNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 627 DKFVGELwkdvdrivgldqvagmnetafgatYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 706
Cdd:cd14878 525 NVVINHL------------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFD 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 707 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACERMIQALELDPnlFRIGQSKIFF 785
Cdd:cd14878 578 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFL 655
|
.
gi 1604804600 786 R 786
Cdd:cd14878 656 K 656
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-785 |
1.58e-89 |
|
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: 306.78 E-value: 1.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 96 LNEASVLYNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEIPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKPVKLQAQhavgelerqLLQANPILESFGN 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTKLSSQ---------ISAAEFVLDSFGN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 246 AKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFL 325
Cdd:cd14879 138 AKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 326 SNGN----IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF--KKERNSDQASMpDNTAA-QKLCH 398
Cdd:cd14879 218 ASYGchplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 399 LLGLNVMEFtRAILSPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGIL 473
Cdd:cd14879 297 FLGVSPEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 474 DIAGfeiFQL------NSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVL 547
Cdd:cd14879 372 DFPG---FQNrsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 548 ALLDEEC-WFPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllh 623
Cdd:cd14879 446 GILDDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL--------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 624 qSTDkFVgelwkdvdrivgldqvagmnetafgatyktkkGMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAG 703
Cdd:cd14879 517 -SPD-FV--------------------------------NLLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPN 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 704 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaiPKGFMDGKQACERMIQALELDpnlFRIGQSKI 783
Cdd:cd14879 562 SFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR---GSAAERIRQCARANGWWEGRD---YVLGNTKV 635
|
..
gi 1604804600 784 FF 785
Cdd:cd14879 636 FL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-786 |
3.46e-87 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 299.62 E-value: 3.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAhvasshKGRKDHNippespkpvklqaqhavgELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN------------------EISNTLWDSNFILEAFGNAKTLKNNNSSRYG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14937 133 KYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFgHEEILAMLKVVSSVLQFGNINFK---KERNSDQASMPDNT--AAQKLCHLLGLNVMEFTRAILS 413
Cdd:cd14937 213 KDFGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 414 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFQLNSFEQMCINY 493
Cdd:cd14937 292 TEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 494 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVDKLIQEQG 573
Cdd:cd14937 371 ANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 574 THTKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMneta 653
Cdd:cd14937 447 KHEKYASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLI---- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 654 fgaTYKtkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPNR 733
Cdd:cd14937 522 ---TFK------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYK 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 734 IVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQAlELDPNLFRIGQSKIFFR 786
Cdd:cd14937 586 YTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-738 |
3.40e-78 |
|
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: 274.48 E-value: 3.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------IPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshkgrkdhnippespkpvklQAQHAVGELERQLLQANPILESFGNAKTVK 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----------------------QTDSQMTERIDKLIYINNILESMSNATTIK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 251 NDNSSRFGKFIRINFDVI---------GYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG-AGEHLKSDLLLEGFN 320
Cdd:cd14884 139 NNNSSRCGRINLLIFEEVentqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 321 SYRFLSN----------GNIPIPG----------QQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKer 380
Cdd:cd14884 219 VYGLLNPdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 381 nsdqasmpdntaaqkLCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD 460
Cdd:cd14884 297 ---------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 461 RTKRQGA-----------SFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlD 529
Cdd:cd14884 362 KCKEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-S 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 530 LQPCIDLIERpanppgVLALLDE-----ECWFPKATDKTFVD-----KLIQEQGTHTK-FQKPR--------QLKDKADF 590
Cdd:cd14884 441 YSDTLIFIAK------IFRRLDDitklkNQGQKKTDDHFFRYllnneRQQQLEGKVSYgFVLNHdadgtakkQNIKKNIF 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 591 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGElwkdvdrivgldqvagmnetafgATYKTKKGMFRTVGQ 670
Cdd:cd14884 515 FIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSK 571
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 671 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 738
Cdd:cd14884 572 KYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-773 |
6.21e-74 |
|
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: 260.43 E-value: 6.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRHEIPPHIYA-------ISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpkpvklqaqhavgELERQLLQANPILESFGNAKTVKND 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET-------------DAFKHLAAAFTVLRSLGSAKTATNS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 253 NSSRFGKFIRINFdVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--SYRFLSNGNI 330
Cdd:cd14881 128 ESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 331 PIPGQQDKDNFQETMEAMHIMSFgheEILAMLKVVSSVLQFGNINFkKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRA 410
Cdd:cd14881 207 RQNEAEDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 411 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFQ 482
Cdd:cd14881 283 LTTRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 483 LNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATD 561
Cdd:cd14881 359 PSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 562 KTFVDKLIQEQGTHTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvgelwkdvdriv 641
Cdd:cd14881 435 ESYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN--------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 642 gldqvagmneTAFGatyktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 721
Cdd:cd14881 499 ----------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLE 559
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 722 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQ--ALELDP 773
Cdd:cd14881 560 TVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-744 |
2.76e-71 |
|
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: 255.67 E-value: 2.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 102 LYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEIPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 172 QSILCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnippESPKPVKLQAQHAVGELERQLLQANPILESFGNAKTVKN 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDE-----------TEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 252 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAgEH---LKSDLLL-EGFNSYRFLSN 327
Cdd:cd14893 153 RNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 328 -----GNIPIpgqqDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF------KKERN-------SDQASMPD 389
Cdd:cd14893 232 adplaTNFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQSCAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 390 NTAAQKL--CHLLGLNVMEF-----TRAILSpriKVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL- 459
Cdd:cd14893 308 KDPAQILlaAKLLEVEPVVLdnyfrTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILg 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 460 ---DRTKRQG----ASFIGILDIAGFEIF--QLNSFEQMCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWSF 523
Cdd:cd14893 385 gifDRYEKSNivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 524 IDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKAD------------FC 591
Cdd:cd14893 465 VDITSEQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 592 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvgelwkdVDRIVGLDQVAGmNETAFGATYKTKKG----MFRT 667
Cdd:cd14893 543 VQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAA-ASSEKAAKQTEERGstssKFRK 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 668 VGQLYKESLT--------------KLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 733
Cdd:cd14893 614 SASSARESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVH 693
|
730
....*....|.
gi 1604804600 734 IVFQEFRQRYE 744
Cdd:cd14893 694 LTYGHFFRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-786 |
6.48e-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: 250.01 E-value: 6.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 105 LKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 184 KTENTKKVIQYLAHV-ASSHKGRKDHnippespkpvklqaqhavgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 262
Cdd:cd14905 85 KSENTKIIIQYLLTTdLSRSKYLRDY------------------------ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 263 INFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSN-GNIPIPGQQDKDNF 341
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 342 QETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKErnSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKVGRD 421
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 422 YVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQL 501
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 502 FNHTMFILEQEEYQREGIEW-SFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF-Q 579
Cdd:cd14905 367 YLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 580 KPRQlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKF-------------VGELWKDVD-------- 638
Cdd:cd14905 440 KPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakks 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 639 --RIVGL---------DQVAGMNETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKL 705
Cdd:cd14905 514 plSIVKVllscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTF 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 706 EPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIQALELDPNLFRIGQSKIF 784
Cdd:cd14905 594 DVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIF 671
|
..
gi 1604804600 785 FR 786
Cdd:cd14905 672 LR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-786 |
2.58e-69 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 246.71 E-value: 2.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrheippHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 178 GESGAGKTENTKKVIQYLAhvasshkgrkdhnippESPKPvKLQAQHAVGelerqllqANPILESFGNAKTVKNDNSSRF 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT----------------SQPKS-KVTTKHSSA--------IESVFKSFGCAKTLKNDEATRF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 258 GKFIRINFDViGYIVGANIE-TYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQ 336
Cdd:cd14874 126 GCSIDLLYKR-NVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 337 DKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSD---QASMPDNTAAQK-LCHLLGLNVMEFTrAIL 412
Cdd:cd14874 205 DVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 413 SPRIKVGrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFQLNSFEQMCIN 492
Cdd:cd14874 284 LPKSEDG-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLIN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 493 YTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDF----GLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL 568
Cdd:cd14874 357 SVNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHC 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 569 IQEQGTHTKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKdvdrivgldqvag 648
Cdd:cd14874 432 NLNHTDRSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------------- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 649 mNETAfgatykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 728
Cdd:cd14874 498 -SYSS------NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIK 570
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 729 GFPNRIVFQEFRQRYEILTPNAIPKgFMDGKQACERMIQALELD-PNLFRIGQSKIFFR 786
Cdd:cd14874 571 GYPVKISKTTFARQYRCLLPGDIAM-CQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-746 |
4.88e-61 |
|
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: 222.69 E-value: 4.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhaVGElerQLLQANPILESFGNAKTVKNDNSSRFGK 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG---------------------ATG---RVESSIKAILALVNAGTPLNADSTRCIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 260 FIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG--AGEHLKSDLLLEGFNsYRFL--SNGNIPIPGQ 335
Cdd:cd14882 138 QYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKLK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 336 QDKDN-------FQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKerNSDQASMPDNTAAQKLCHLLGLNVMEFT 408
Cdd:cd14882 217 YRRDDpegnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 409 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFQL 483
Cdd:cd14882 295 WALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 484 NSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECwfPKATDKT 563
Cdd:cd14882 372 NRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQN 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 564 FVDKLIQEQgtHTKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivgl 643
Cdd:cd14882 447 YIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 644 DQVAGMnetafgatyKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 720
Cdd:cd14882 515 SQVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVL 579
|
650 660
....*....|....*....|....*.
gi 1604804600 721 EGIRICRQGFPNRIVFQEFRQRYEIL 746
Cdd:cd14882 580 DTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-784 |
3.23e-58 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 215.86 E-value: 3.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKLQAQHAVGELERQLLQANPILESFGNAKTVKNDNSSRFG 258
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 259 KFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPIPGQQDK 338
Cdd:cd14938 162 KFCTIHIEN-EEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 339 DNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNI--------------------NFKKE------RNSDQASMPDNTA 392
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkksllmgknqcgqNINYEtilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 393 AQKL-CHLLGLNVMEFTRAILSPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 469
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 470 IGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANppGVLAL 549
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 550 LDEECWFPKATDKTFVDKLIQEQGTHTKF--QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTD 627
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 628 KFVGEL-----WKDVDRIVGLDQVAGM--NETAFGATYKTKKGMFRTvgqLYKESLTKLMATLRNTNPNFVRCIIPNHEK 700
Cdd:cd14938 558 EYMRQFcmfynYDNSGNIVEEKRRYSIqsALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 701 RA-GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIQALELDPNLFRIG 779
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 1604804600 780 QSKIF 784
Cdd:cd14938 707 NNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-270 |
3.78e-57 |
|
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: 195.64 E-value: 3.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 200 SSHKGRKDHNIppeSPKPVKLQaqhavGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVIGY 270
Cdd:cd01363 81 FNGINKGETEG---WVYLTEIT-----VTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1120-1949 |
1.69e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 145.20 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1120 QKNNALKQVRELQAHLA-------ELQEDLESEKMCRSKAEKLKrDLSEELEALKTELEdTLDTTAAQQELRSKREQEva 1192
Cdd:TIGR02168 173 RRKETERKLERTRENLDrledilnELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELEELQEEL-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1193 elkkaideetknheAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKL 1272
Cdd:TIGR02168 249 --------------KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1273 EAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEEtRQKLNLSTQ 1352
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL-RSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1353 irQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFE-TKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMD 1431
Cdd:TIGR02168 394 --QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1432 KMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEarEKDTKALSMAraleeal 1511
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD--EGYEAAIEAA------- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1512 eakeelerfnkqLRAEMEDL-MSSKDDVGKNVHELEKS---KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAM 1587
Cdd:TIGR02168 543 ------------LGGRLQAVvVENLNAAKKAIAFLKQNelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1588 KAQFDRDLQA---------RDEQGEEKKRLLVKQVREMEAELE------------DERKQRTLAVASK-KKLEMDLNELE 1645
Cdd:TIGR02168 611 DPKLRKALSYllggvlvvdDLDNALELAKKLRPGYRIVTLDGDlvrpggvitggsAKTNSSILERRREiEELEEKIEELE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1646 GQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARasrdeifTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQER 1725
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELS-------RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1726 DELADEISNSASGKSSLLEEKRRLEARIAQleeeleeEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQM 1805
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1806 ERQNKDLKAKLAELEGTVKSkFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKE 1885
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1886 QMEKANSRMKQLKRQLEEAEEEATRANAT-RRKLQRELDDA-------TEASEGLTREVSSLKNRLRRGGPV 1949
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1019-1847 |
2.28e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.17 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1019 LEDRISEMTSQ---LTEEEEKAKNLGKVKNKQE-----MMMVDLEERLKKEEKTRQELEKAKRKLDAettdLQDQIVELQ 1090
Cdd:TIGR02168 191 LEDILNELERQlksLERQAEKAERYKELKAELRelelaLLVLRLEELREELEELQEELKEAEEELEE----LTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1091 AQIEELK---FQLTKKEEELQAALARSDEEtlqKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALK 1167
Cdd:TIGR02168 267 EKLEELRlevSELEEEIEELQKELYALANE---ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1168 TELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATaLEELSEQLEQAKRFKSNLEKNKQSLEND 1247
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1248 NkelscdvktlqqakteSEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDK 1327
Cdd:TIGR02168 423 I----------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1328 LNSKLQDSEELRQEetrqKLNLSTQIRQLEVDRNTLleqqeeeeearrnleKQLQMVQSQMFETKKK----LEEDLGS-- 1401
Cdd:TIGR02168 487 LQARLDSLERLQEN----LEGFSEGVKALLKNQSGL---------------SGILGVLSELISVDEGyeaaIEAALGGrl 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1402 ----MEGLEEVKrklqKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAeekT 1477
Cdd:TIGR02168 548 qavvVENLNAAK----KAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---Y 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1478 ISAQYAEERDRAEAEAREKDTKALSM----------ARALEEALEAKEELERFNKqlRAEMEDLmsskddvGKNVHELEK 1547
Cdd:TIGR02168 621 LLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITGGSAKTNSSILER--RREIEEL-------EEKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1548 SKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQGEEKKRLLVKQVREMEAELEDERKQR 1627
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1628 TLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQL 1707
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1708 QEDHAASERARRHAEQERDELADEIsnsasgkSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTE 1787
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1788 LAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQ 1847
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
864-1753 |
9.90e-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: 122.86 E-value: 9.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 864 RQEEELQakdeeLVKVKERQLKVENELVEMERKHQQLiEEKNILAEQLHaetELFAEAEEMRVRLLS-RKQELEEILHDL 942
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQLKSL-ERQAEKAERYK---ELKAELRELELALLVlRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 943 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1022
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1023 ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTK 1102
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1103 KEEELQAalarsdeetlqknnalkqvreLQAHLAELQEDLESEKMCRSKAEKlkRDLSEELEALKTELEDTLDTTAAQQE 1182
Cdd:TIGR02168 405 LEARLER---------------------LEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1183 LRSKREQEVAELKKAIDEEtknhEAQIQEMRQRQAtALEELSEQLEQAKRFKSNLEKNKQSLENDNKELScdvktlQQAK 1262
Cdd:TIGR02168 462 ALEELREELEEAEQALDAA----ERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLS------ELIS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1263 TESEHkRKKLEAQLQEFMA-----RATEAERTKGELAERSHKLQT--ELD-------NACTMLEVAEKKG-LKLAKEVDK 1327
Cdd:TIGR02168 531 VDEGY-EAAIEAALGGRLQavvveNLNAAKKAIAFLKQNELGRVTflPLDsikgteiQGNDREILKNIEGfLGVAKDLVK 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1328 LNSKLQDSEELR------QEETRQKLNLSTQIRQlevdRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGS 1401
Cdd:TIGR02168 610 FDPKLRKALSYLlggvlvVDDLDNALELAKKLRP----GYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1402 MEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKT 1477
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1478 ISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQ---LRAEMEDLMSSKDDVGKNVHELEKSKRTLEQ 1554
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1555 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQgEEKKRLLVKQVREMEAELEDERKQRTLAVASK 1634
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL-RSELEELSEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1635 KKLEMDLNELEGQIEaankgrdeavkqlRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAAS 1714
Cdd:TIGR02168 925 AQLELRLEGLEVRID-------------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
|
890 900 910
....*....|....*....|....*....|....*....
gi 1604804600 1715 ERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARI 1753
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-727 |
9.20e-27 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 119.46 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 105 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYSENIIEMYRGKKRHE--IPPHIYAISE---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 160 ----SAYRCMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVAS----------------------------------- 200
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQpalskgseetckvsgstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 201 -----------SHKGRKDHNI-----PPES-------PKPVKLQAQHAVG------------ELERQL------------ 233
Cdd:cd14894 166 rteeartiallEAKGVEKYEIvlldlHPERwdemtsvSRSKRLPQVHVDGlffgfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 234 ----LQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVIGY---IVGANIETYLLEKSRAIRQA------KDERTFHI 298
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 299 FYQLLAGAGEH-----LKSDLLLEGFN--SYRFLSNGNIPIPG--------QQDKDNFQETMEAMHIMSFGHEEILAMLK 363
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 364 VVSSVLQFGNINFKKERNSDQASMPDN---TAAQKLCHLLGLNVMEFTRAIL---SPRIKVGRDYVQKAQTKEQADFAVE 437
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLmtkSVSLQSTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 438 ALAKATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQl 501
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 502 fnhtmfileqEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVdKLIQE 571
Cdd:cd14894 565 ----------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFV-RNIYD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 572 QGTHTKFQKPRQLKDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRiv 641
Cdd:cd14894 634 RNSSRLPEPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ-- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 642 gLDQVAGMNETAFGATYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 721
Cdd:cd14894 712 -LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIR 789
|
....*.
gi 1604804600 722 GIRICR 727
Cdd:cd14894 790 QMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1033-1873 |
1.29e-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: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1033 EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALA 1112
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1113 RSDEETLQ-KNNALKQVRELQAHLAELQEDLESekmCRSKAEKLKRDLsEELEALKTELEDTLDTTAAQQELRSKREQEV 1191
Cdd:TIGR02169 273 LLEELNKKiKDLGEEEQLRVKEKIGELEAEIAS---LERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1192 AELKKAIDEETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKK 1271
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAE----LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1272 LEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEElrqeetrqklnlst 1351
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR-------------- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1352 QIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVqsqmfetkkkleedLGSMEGLEEVKRKLQKDVE------LTSQCLEE 1425
Cdd:TIGR02169 491 ELAEAEAQARASEERVRGGRAVEEVLKASIQGV--------------HGTVAQLGSVGERYATAIEvaagnrLNNVVVED 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1426 KTMAMDKMEKTK------------NRLQQELDDL--------------MVDLDHQRQ-----------IVSNLEKKQKKF 1468
Cdd:TIGR02169 557 DAVAKEAIELLKrrkagratflplNKMRDERRDLsilsedgvigfavdLVEFDPKYEpafkyvfgdtlVVEDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1469 DQL--------LAE-----------EKTISAQYAEERDRAEAEAREKDtkalSMARALEEALEAKEELERFNKQLRAEME 1529
Cdd:TIGR02169 637 GKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1530 DLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrdlQARDEQGEEKKRLL 1609
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLS 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1610 VKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQ 1689
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1690 SKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQgnmel 1769
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----- 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1770 lndrfrksniqvdnlntELAGERSAAQKSENARQQMERQNKDLkaklaeleGTVKSKFKASIAALEAKILQLEDQLEQEA 1849
Cdd:TIGR02169 945 -----------------EIPEEELSLEDVQAELQRVEEEIRAL--------EPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
|
890 900
....*....|....*....|....
gi 1604804600 1850 KERAAANKIVRRTEKKLKEVMMQV 1873
Cdd:TIGR02169 1000 EERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
985-1755 |
4.96e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 117.48 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 985 QLDKVTAEaKIKKMEEDILLLEDQNSKF---LKEKKLLEDRISEMTSQLTEEEEKaknlgkvknkQEMMMVDLEERLKKE 1061
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEGyelLKEKEALERQKEAIERQLASLEEE----------LEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1062 EKTRQELEKAKRKLDAETTD----LQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAE 1137
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1138 LQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID----------EETKNHEA 1207
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlqeelqrlsEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1208 QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKL---EAQLQEFMARAT 1284
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1285 EAERTKGELA----------------ERSHKLQTE------LDNACTMLEVAEKKGLKLAKEV----------DKLNSKL 1332
Cdd:TIGR02169 508 GGRAVEEVLKasiqgvhgtvaqlgsvGERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRRkagratflplNKMRDER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1333 QDSEELRQEETRQ-KLNLSTQIRQLE-----VDRNTLLeqQEEEEEARRnlekqlQMVQSQMFETKKKLEEDLGSMEGLE 1406
Cdd:TIGR02169 588 RDLSILSEDGVIGfAVDLVEFDPKYEpafkyVFGDTLV--VEDIEAARR------LMGKYRMVTLEGELFEKSGAMTGGS 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1407 EVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKTISAQY 1482
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERL 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1483 AEERDRAEAEAREKDTKALSMARALEEALEAKEELErfnkQLRAEMEDLMSSKDDVGknVHELEKSKRTLEQQVEEMRTQ 1562
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLH----KLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEAR 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1563 LEELEDELQATEDAKLRLEVNMQAMKAQFdRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLN 1642
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1643 ELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKE------NEKKLKGLEAEILQLQEDHAASER 1716
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEP 972
|
810 820 830
....*....|....*....|....*....|....*....
gi 1604804600 1717 ARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1755
Cdd:TIGR02169 973 VNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1069-1755 |
3.36e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.18 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1069 EKAKRKLDAETTDL---QDQIVELQAQIEELkfqltkkeeELQAALAR------SDEETLQKNNALKQVRELQAHLAELQ 1139
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPL---------ERQAEKAEryrelkEELKELEAELLLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1140 EDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEEtknheaqiQEMRQRQATA 1219
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------EERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1220 LEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHK 1299
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1300 LQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEK 1379
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1380 QLQmvqsqmfetkkKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKtmamdKMEKTKNRLQQELDDLMVDldhqrqivs 1459
Cdd:COG1196 478 ALA-----------ELLEELAEAAARLLLLLEAEADYEGFLEGVKAA-----LLLAGLRGLAGAVAVLIGV--------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1460 nlEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKA-----LSMARALEEALEAKEELERFNKQLRAEMEDLMSS 1534
Cdd:COG1196 533 --EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1535 KD----DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLV 1610
Cdd:COG1196 611 ADaryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1611 KQVREMEAELEDERKQRTLAvaskkklEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQS 1690
Cdd:COG1196 691 EELELEEALLAEEEEERELA-------EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1691 kENEKKLKGLEAEI--------LQLQEDHAASERARRHAEQERDeladeisnsasgkssLLEEKRRLEARIAQ 1755
Cdd:COG1196 764 -ELERELERLEREIealgpvnlLAIEEYEELEERYDFLSEQRED---------------LEEARETLEEAIEE 820
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1189-1943 |
8.96e-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: 110.21 E-value: 8.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1189 QEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHK 1268
Cdd:pfam15921 85 HQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1269 RKKLEAQLQEFMARATEAERTKGEL-------AERSHKLQTELDNACTM----LEVAEKKGLK-LAKEVDKLNSKL---Q 1333
Cdd:pfam15921 165 LEDSNTQIEQLRKMMLSHEGVLQEIrsilvdfEEASGKKIYEHDSMSTMhfrsLGSAISKILReLDTEISYLKGRIfpvE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1334 DSEELRQEETRQKLNLSTQ-----IRQL----EVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEG 1404
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQqhqdrIEQLisehEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLES 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1405 --------LEEVKR-------KLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK-- 1467
Cdd:pfam15921 325 tvsqlrseLREAKRmyedkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrl 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1468 FDQLLAEEKTISAQYAEERDR----AEAEAREKDTKALSMARALEEALEAKEELERFNK--QLRAEMEdlmSSKDDVGKN 1541
Cdd:pfam15921 404 WDRDTGNSITIDHLRRELDDRnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvsSLTAQLE---STKEMLRKV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1542 VHELEKSKRTLE---QQVEEMRTQLEELEDELQAT--EDAKLRLEVNMQAmkaqfdRDLQARDEQGEekkrllvkQVREM 1616
Cdd:pfam15921 481 VEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEITKLRSRVDLKL------QELQHLKNEGD--------HLRNV 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1617 EAELEDERKQRTlavASKKKLEMDLNELEGQIE-AANKGRDEAVKQLRK--LQAQMKDYQRELEEARASRDEIFTQSKEN 1693
Cdd:pfam15921 547 QTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1694 EKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEkrrleariaqleeeleeeqgnMELLNDR 1773
Cdd:pfam15921 624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED---------------------YEVLKRN 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1774 FRKSNIQVD----NLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEA 1849
Cdd:pfam15921 683 FRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNAN 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1850 KERaaanKIVRRTEKKLKEVMMQVEDERrhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRAN----------------A 1913
Cdd:pfam15921 762 KEK----HFLKEEKNKLSQELSTVATEK---NKMAGELEVLRSQERRLKEKVANMEVALDKASlqfaecqdiiqrqeqeS 834
|
810 820 830
....*....|....*....|....*....|
gi 1604804600 1914 TRRKLQRELDDATEASEGLTREvSSLKNRL 1943
Cdd:pfam15921 835 VRLKLQHTLDVKELQGPGYTSN-SSMKPRL 863
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1060-1755 |
1.05e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.77 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1060 KEEKTRQELEKAKRKLDaettdlqdqivELQAQIEELKFQLTKKEEELQAAL-----------ARSDEETLQKNNALKQV 1128
Cdd:TIGR02169 171 KKEKALEELEEVEENIE-----------RLDLIIDEKRQQLERLRREREKAEryqallkekreYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1129 RELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKREQEVAELKKAID------EE 1201
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAekerelED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1202 TKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMA 1281
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1282 RATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKL-------AKEVDKLNSKLQDSEELRQEETRQKLNLSTQIR 1354
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELeeekedkALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1355 QLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVE------LTSQCLEEKTM 1428
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1429 AMDKMEKTK------------NRLQQELDDL--------------MVDLDHQRQ-----------IVSNLEKKQKKFDQL 1471
Cdd:TIGR02169 560 AKEAIELLKrrkagratflplNKMRDERRDLsilsedgvigfavdLVEFDPKYEpafkyvfgdtlVVEDIEAARRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1472 --------LAE-----------EKTISAQYAEERDRAEAEAREKDtkalSMARALEEALEAKEELERFNKQLRAEMEDLM 1532
Cdd:TIGR02169 640 rmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1533 SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrdlQARDEQGEEKKRLLVKQ 1612
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1613 VREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKE 1692
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1693 N-------EKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1755
Cdd:TIGR02169 873 LeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1337-1949 |
1.79e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1337 ELRQEETRQKLN--------LSTQIRQLEVDRNTlleqqeeeeeARRNLEKQLQmvqsqmfETKKKLEEDLGSMEGLEEV 1408
Cdd:COG1196 178 ERKLEATEENLErledilgeLERQLEPLERQAEK----------AERYRELKEE-------LKELEAELLLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1409 KRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDR 1488
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1489 AEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1568
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1569 ELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEmDLNELEGQI 1648
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE-EAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1649 EAANKGRDEAVKQLRKLQAQMKDYQRELEEARAsrdeiftqsKENEKKLKGLEAEILQLQEDHAASERARRHA------- 1721
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKA---------ALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqn 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1722 -----EQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQ 1796
Cdd:COG1196 551 ivvedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1797 KSENARQQMERQNKDLKAKLAELEGtvkskFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDE 1876
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEG-----GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1877 RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEAS----EGLTREVSSLKNRLRRGGPV 1949
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppdlEELERELERLEREIEALGPV 782
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
981-1570 |
3.47e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 104.38 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 981 RQKLQLDKV-TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLK 1059
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1060 KEEKTRQELEKAKR---KLDAETTDLQDQIVELQAQIEELKfqltKKEEELQAALARSDEetlqknnaLKQVRELQAHLA 1136
Cdd:PRK03918 232 ELEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKELKE--------LKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1137 ELQEDLESEKmcrSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ---EVAELKKAID--EETKNHEAQIQE 1211
Cdd:PRK03918 300 EFYEEYLDEL---REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1212 MRQRQA-TALEELSEQLEQAKRFK-------SNLEKNKQSLENDNKELSCDVKTLQQAKTE--------SEHKRKKLeaq 1275
Cdd:PRK03918 377 LKKRLTgLTPEKLEKELEELEKAKeeieeeiSKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKEL--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1276 LQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEK--KGLKLAKEVDKLNSKLQ--DSEELRQ-----EETRQK 1346
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKkyNLEELEKkaeeyEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1347 LN-LSTQIRQLEVDrntlLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDlgSMEGLEEVKRKLQKDVELTSQCLEE 1425
Cdd:PRK03918 534 LIkLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEEL--GFESVEELEERLKELEPFYNEYLEL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1426 KtmamdKMEKTKNRLQQELDDLMVDLDhqrQIVSNLEKKQKKFDQLLAEEKTISAQYAEErdraeaEAREKDTKALSMAR 1505
Cdd:PRK03918 608 K-----DAEKELEREEKELKKLEEELD---KAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1506 ALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1570
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1559 |
8.08e-22 |
|
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: 103.60 E-value: 8.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 861 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKN-------ILAEQLHAETELFAEAEEMRVRLLSRKQ 933
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleqqkqILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 934 ELEEILHDLESR-------VEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLE 1006
Cdd:TIGR02168 334 ELAEELAELEEKleelkeeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1007 DQNSKFLKEKKLLEDRISEMTSQLTEE--EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD---AETTD 1081
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAqlqARLDS 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1082 LQDQIVELQAQIEELKFQLTKKE----------------------------EELQAALARSDEETLQKNNALKQVRELQA 1133
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSglsgilgvlselisvdegyeaaieaalgGRLQAVVVENLNAAKKAIAFLKQNELGRV 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1134 HLAELQE----DLESEKMCRSKAEKLKRDLSEELEALKTELEDTL-----------DTTAAQQELRSKREQEVAELKK-- 1196
Cdd:TIGR02168 574 TFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvdDLDNALELAKKLRPGYRIVTLDgd 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1197 ------AIDEETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRK 1270
Cdd:TIGR02168 654 lvrpggVITGGSAKTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1271 KLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLS 1350
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1351 TQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVEL-------TSQCL 1423
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEAL 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1424 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERDRAEAEAREKDTKALS 1502
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1503 MARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1559
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
822-1417 |
6.29e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 822 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRLftkvkpllQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQL 900
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 901 IEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshIQDLEEQLDEEEAA 980
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 981 RQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1060
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1061 EEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQE 1140
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1141 DLESEKMCR---------SKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQE 1211
Cdd:COG1196 513 ALLLAGLRGlagavavliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1212 MRQRQATALEELSEQLEQAKRFKSNLEKNKQslendnkelscdVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKG 1291
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLL------------GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1292 ELAERSHKLQTELdnactmlevAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEE 1371
Cdd:COG1196 661 SLTGGSRRELLAA---------LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1604804600 1372 EARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVE 1417
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1032-1735 |
1.05e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1032 EEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKaKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAAL 1111
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1112 ARSDEETLQKNNALKQVRELQAHLAELQEDLESEKmcrsKAEKLKRDlSEELEAlKTELEDTLDTTAAQQELRSKREQEV 1191
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK----KAEEAKKK-ADAAKK-KAEEAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1192 AELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLE-----NDNKELSCDVKTLQQAKTESE 1266
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAakkkaDEAKKKAEEKKKADEAKKKAE 1441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1267 HKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEK--KGLKLAKEVDKLNSKLQDSEELRQEETR 1344
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1345 QKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLE 1424
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1425 EKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ----KKFDQLLAEEKTISAQYAEERDRAEAEAR--EKDT 1498
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAK 1681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1499 KALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGK----NVHELEKSKRTLEQ---QVEEMRTQLEELEDELQ 1571
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaeeeNKIKAEEAKKEAEEdkkKAEEAKKDEEEKKKIAH 1761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1572 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKklEMDLNELEGQIEAA 1651
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSK 1839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1652 NKGRDEAvkqlrklqaqmkdyqRELEEARASRDEIftqSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADE 1731
Cdd:PTZ00121 1840 NMQLEEA---------------DAFEKHKFNKNNE---NGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
....
gi 1604804600 1732 ISNS 1735
Cdd:PTZ00121 1902 IPNN 1905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
991-1622 |
1.44e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 991 AEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGkvknkqemmmvdleERLKKEEKTRQELEK 1070
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1071 AKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEkmcRS 1150
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1151 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAElKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQA 1230
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1231 KRFKSNLEKNKQSLENDNKELscDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDnactm 1310
Cdd:COG1196 459 EALLELLAELLEEAALLEAAL--AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG----- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1311 LEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQmvqsqmfe 1390
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL-------- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1391 tkkkLEEDLgsmEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQ 1470
Cdd:COG1196 604 ----VASDL---READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1471 LLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKR 1550
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1551 TLEQQVEEMRTQLEELEDELQATEDaklrleVNMQAMkaqfdrdlqarDEQGEEKKRL--LVKQVREMEAELED 1622
Cdd:COG1196 757 PEPPDLEELERELERLEREIEALGP------VNLLAI-----------EEYEELEERYdfLSEQREDLEEARET 813
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1314-1945 |
8.42e-19 |
|
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: 93.70 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1314 AEKKGLKLAKEV-DKLNSKLQDSEELRQEETRQKLNLSTQIRQlevdrNTLLEQQEEEEEARrnLEKQLQMVQSQMFETK 1392
Cdd:pfam01576 9 AKEEELQKVKERqQKAESELKELEKKHQQLCEEKNALQEQLQA-----ETELCAEAEEMRAR--LAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1393 KKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL 1472
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1473 AEektISAQYAEERDRAEAEAREKdTKALSMAraleealeakeelerfnkqlrAEMEDLMSSKDdvgKNVHELEKSKRTL 1552
Cdd:pfam01576 162 SE---FTSNLAEEEEKAKSLSKLK-NKHEAMI---------------------SDLEERLKKEE---KGRQELEKAKRKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1553 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVA 1632
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1633 SKKKLEMDLNELEGQIEAAnKGRDEAVKQLR-KLQAQMKDYQRELE-EARASRDEIFTQSKENEKKLKGLEAEILQLQED 1710
Cdd:pfam01576 293 QRRDLGEELEALKTELEDT-LDTTAAQQELRsKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1711 HAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAG 1790
Cdd:pfam01576 372 KANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1791 ERSAAQKSENARQQMERQNKDLKAKLAElEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVM 1870
Cdd:pfam01576 452 AEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1871 MQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
866-1732 |
1.03e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.50 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 866 EEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESR 945
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 946 VEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISE 1025
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1026 MTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRkldaettDLQDQIVELQAQIEELKFQLTKKEE 1105
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE-------ELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1106 ELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTtaaqQELRS 1185
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----QELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1186 KREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSeQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTES 1265
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS-QKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1266 EHKRKKLEAQLQEFMARATEAErTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKE----VDKLNSKLQDSEELRQE 1341
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVE-ERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1342 ETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQ 1421
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1422 CLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERDRAEAEAREKDTKA 1500
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEeEKSRLKKEEKEEEKSELSLKEKELAE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1501 LSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRL 1580
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1581 EVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVK 1660
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1661 QLRKLQAQMKDYQRE-LEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEI 1732
Cdd:pfam02463 939 ELLLEEADEKEKEENnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
864-1414 |
1.32e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 864 RQEEELQAKD--EELVKVKERQL-KVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQE---LEE 937
Cdd:PRK03918 180 RLEKFIKRTEniEELIKEKEKELeEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrkLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 938 ILHDLESRVEEEEERNQSLQNEKKKMqshiqdleeqldeeeaarQKLQLDKVTAEAKIKKMEEdillLEDQNSKFLKEKK 1017
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKEL------------------KELKEKAEEYIKLSEFYEE----YLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1018 LLEDRISEMTSQLTEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLD------AETTDLQ-DQIVELQ 1090
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEAKAKKEelerlkKRLTGLTpEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1091 AQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHL----AELQEDLESEKMCRSKAE-----KLKRDLSE 1161
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELLEEYTAElkrieKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1162 ELEALKTELEDTLDTTAAQQELRskREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLE-QAKRFKSNLEKn 1240
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgEIKSLKKELEK- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1241 KQSLENDNKELSCDVKTLQQAKTESEHKRKK--------LEAQLQEF------MARATEAERTKGELAERSHKLQTELDN 1306
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELepfyneYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1307 ACTMLEVAEKKGLKLAKEVDKLNSKLqdSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQmvqs 1386
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE---- 704
|
570 580
....*....|....*....|....*...
gi 1604804600 1387 QMFETKKKLEEDLGSMEGLEEVKRKLQK 1414
Cdd:PRK03918 705 EREKAKKELEKLEKALERVEELREKVKK 732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1209-1820 |
7.37e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1209 IQEMRQRqataLEELSEQLEQAKRFKsnleknkqslendnkelscdvkTLQQAKTESEHKRKKLEaqLQEFMARATEAER 1288
Cdd:COG1196 195 LGELERQ----LEPLERQAEKAERYR----------------------ELKEELKELEAELLLLK--LRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1289 TKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLleqqe 1368
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1369 eeEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLE-----------EVKRKLQKDVELTSQCLEEKTMAMDKMEKTK 1437
Cdd:COG1196 322 --EEELAELEEELEELEEELEELEEELEEAEEELEEAEaelaeaeeallEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1438 NR---LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEA------REKDTKALSMARALE 1508
Cdd:COG1196 400 AQleeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEeallelLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1509 EALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK 1588
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1589 AQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQ 1668
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1669 MKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEisnsasgksslLEEKRR 1748
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA-----------EEEEER 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1749 LEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENA-RQQMERQNKDLKAKLAELE 1820
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdLEELERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1544-1869 |
7.67e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1544 ELEKSKRTLE---QQVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaqfdRDLQARDEQGEEKKRLLVKQVREMEAEL 1620
Cdd:TIGR02169 171 KKEKALEELEeveENIERLDLIIDEKRQQLERLRREREKAE-----------RYQALLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1621 EDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKL--------QAQMKDYQRELEEARASRDEIFTQSKE 1692
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1693 NEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLND 1772
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1773 RFRKSNIQVDNLNTELagersaaQKSENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEAKER 1852
Cdd:TIGR02169 400 EINELKRELDRLQEEL-------QRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQEL 471
|
330
....*....|....*..
gi 1604804600 1853 AAANKIVRRTEKKLKEV 1869
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKL 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
992-1592 |
8.02e-16 |
|
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: 83.53 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 992 EAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKA 1071
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1072 KRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQaalarSDEETLQKNNalKQVRELQAHLAELQEDLESEKMCRSK 1151
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL-----NIQKNIDKIK--NKLLKLELLLSNLKKKIQKNKSLESQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1152 AEKLKRDLSEeleaLKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQrQATALEELSEQLEQAK 1231
Cdd:TIGR04523 220 ISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ-NNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1232 RFKSNLEKNKQslENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTML 1311
Cdd:TIGR04523 295 SEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1312 EVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEAR-------RNLEKQLQMV 1384
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIiknnseiKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1385 QSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1464
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1465 QKKFDQLLA--EEKTISAQYAEERDRAEAEAREKDTKALSMaraleeaLEAKEELERFNKQLRAEMEDLMSSKDDVGKNV 1542
Cdd:TIGR04523 533 KKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1543 HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFD 1592
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
931-1471 |
2.92e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 931 RKQELEEIL---HDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVtaeaKIKKMEEDILLLED 1007
Cdd:PRK03918 177 RIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1008 QNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEmMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIV 1087
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1088 ELQAQIEELKfQLTKKEEELQAALARSDEetlqKNNALKQVRELQAHLaelqEDLESEKMCRSKaEKLKRDLsEELEALK 1167
Cdd:PRK03918 332 ELEEKEERLE-ELKKKLKELEKRLEELEE----RHELYEEAKAKKEEL----ERLKKRLTGLTP-EKLEKEL-EELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1168 TELEDTLDTTAAQqelRSKREQEVAELKKAIDEETKNH-----------EAQIQEMRQRQATALEELSEQLEQAKRFKSN 1236
Cdd:PRK03918 401 EEIEEEISKITAR---IGELKKEIKELKKAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1237 LEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTeLDNACTMLEVAEK 1316
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1317 KGLKLAKEVDKLNSKLQDSE-ELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRnLEKQLQMVQSQMFETKKKL 1395
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLkELEELGFESVEELEERLKELEPFYNEYLELKDAEKELER-EEKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1396 EEDLGSMEG----LEEVKRKL-QKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQ 1470
Cdd:PRK03918 636 AETEKRLEElrkeLEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
.
gi 1604804600 1471 L 1471
Cdd:PRK03918 716 L 716
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
861-1755 |
3.17e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 82.02 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 861 QVTRQEEELQAKDEELVKVKERQLKVEnelvEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLL-SRKQELEEIL 939
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIE----HNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFqGTDEQLNDLY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 940 HDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLL 1019
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1020 EDRISEMTSQLTEEEEK------AKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQaQI 1093
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEdeaktaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ-QL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EELKFQLTKKEEELQAALArsDEETLQKNNALKQVRELQAHLAELQEDLESEKmcRSKAEKLKrDLSEELEALKTELEDT 1173
Cdd:TIGR00606 467 EGSSDRILELDQELRKAER--ELSKAEKNSLTETLKKEVKSLQNEKADLDRKL--RKLDQEME-QLNHHTTTRTQMEMLT 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1174 LDTTAAQQELRSKREQEVAEL---------KKAIDEETKNHEAQIQEMRQRQATALEELsEQLEQAKRFKSNLEKNKQSL 1244
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKEL-ASLEQNKNHINNELESKEEQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1245 ENDNKELSCDVKTLQQAKTESEHKRKKLE-------------AQLQEFMARATEAE-----------RTKGELAERSHKL 1300
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlagatAVYSQFITQLTDENqsccpvcqrvfQTEAELQEFISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1301 QTELDNACTMLEVAEKKGLKLAKEVDKLNSKLqdseELRQEETRQKlnlstqIRQLEVDRNTLLEQQEEEEEARRNLEKQ 1380
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLA----PGRQSIIDLK------EKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1381 LQMVQSQMFETK--KKLEEDLGSMEGLEEVKRKLQKDVELTSQCLE--EKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQ 1456
Cdd:TIGR00606 771 ETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1457 IVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEA---EAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMS 1533
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1534 SKDDVGKNVH-ELEKSKRTLEQQVEEMRTQLEELEDelqATEDAKLRLEVNMQAMKAQFdrdlqardEQGEEKKRLLVKQ 1612
Cdd:TIGR00606 931 SKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL--------EECEKHQEKINED 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1613 VREMEAELeDERKQRTLAVASKKKLEMDLNELEgQIEAANKGRDEAVKQLRKLQaQMKDYQRELEEARASRDE---IFTQ 1689
Cdd:TIGR00606 1000 MRLMRQDI-DTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLKEMGQMQVLQ-MKQEHQKLEENIDLIKRNhvlALGR 1076
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1690 SKENEKKLKGLEAEIlqlqedhaaSERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1755
Cdd:TIGR00606 1077 QKGYEKEIKHFKKEL---------REPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMK 1133
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1054-1729 |
5.47e-15 |
|
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: 81.42 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1054 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVR-ELQ 1132
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRsELE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1133 A----HLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETknheAQ 1208
Cdd:pfam12128 326 AledqHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL----AK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1209 IQEMRQRQATALEELSEQLE----------------QAKRFKSNLEKNKQSL--------ENDNKELSCD-VKTLQQAKT 1263
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALEselreqleagklefneEEYRLKSRLGELKLRLnqatatpeLLLQLENFDErIERAREEQE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1264 ESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLK-LAKEV---DKLNSKLQDSE--- 1336
Cdd:pfam12128 482 AANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEApdwEQSIGKVISPEllh 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1337 ------ELRQEETRQKLNL-STQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQsqmfETKKKLEEDLGSMEG-LEEV 1408
Cdd:pfam12128 562 rtdldpEVWDGSVGGELNLyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR----EKQAAAEEQLVQANGeLEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1409 KRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDdlmvdlDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDR 1488
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA------ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1489 AEAEAREK-----DTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEemrtql 1563
Cdd:pfam12128 712 ARTEKQAYwqvveGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE------ 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1564 eeledelqatedaklRLEVNMQAMkAQFDRDLQardEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKkleMDLNE 1643
Cdd:pfam12128 786 ---------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQLARLIADTK---LRRAK 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1644 LEGQIEAANKGRDEAVKQLRKLQAQMKDYQR-----ELEEARASRDEIFTQSKENEKKLKGLEAEILQLQE-------DH 1711
Cdd:pfam12128 844 LEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEhfknviaDH 923
|
730
....*....|....*...
gi 1604804600 1712 AASERArRHAEQERDELA 1729
Cdd:pfam12128 924 SGSGLA-ETWESLREEDH 940
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
880-1711 |
5.49e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.32 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 880 KERQLKVENELVEMERKHQQLIEEKNilaeQLHAETELFaeaeeMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNE 959
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESN----ELHEKQKFY-----LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 960 KKKMQSHIQDLEEQldeeeaarqklqldkvtaeakiKKMEEDilLLEDQNSKFLKEKKLL---EDRISEMTSQLTEEEEK 1036
Cdd:pfam15921 144 RNQLQNTVHELEAA----------------------KCLKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1037 AknlGKVKNKQEMMMVDLEERLKkeektrQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQ--------LTKKEEELQ 1108
Cdd:pfam15921 200 S---GKKIYEHDSMSTMHFRSLG------SAISKILRELDTEISYLKGRIFPVEDQLEALKSEsqnkiellLQQHQDRIE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1109 AALARSDEE----TLQKNNALKQVRELQAHLAELQEDLESEK---MCR-SKAEKLKRDLSEELEALKTELEDTLDTTAAQ 1180
Cdd:pfam15921 271 QLISEHEVEitglTEKASSARSQANSIQSQLEIIQEQARNQNsmyMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1181 QELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscDVKTLQQ 1260
Cdd:pfam15921 351 LVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL--DDRNMEV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1261 AKTESEHKRKKLEAQLQefMARATEAERTKGELAERSHKLQTELDNACTMLEvaekkglklaKEVDKLNSKLQDSEElrQ 1340
Cdd:pfam15921 429 QRLEALLKAMKSECQGQ--MERQMAAIQGKNESLEKVSSLTAQLESTKEMLR----------KVVEELTAKKMTLES--S 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1341 EETRQKLNLSTQIRqlevdrntlleqqeeeeearrnlEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQkdvELTS 1420
Cdd:pfam15921 495 ERTVSDLTASLQEK-----------------------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR---NVQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1421 QClEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKA 1500
Cdd:pfam15921 549 EC-EALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1501 LSMARALEEALEAKEELERFNKQLRAEMEDLM----SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedA 1576
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS---A 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1577 KLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVK--QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKG 1654
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1655 RDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDH 1711
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQH 841
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1374-1945 |
8.03e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1374 RRNLEKQLQMVQSQMFETKKK-LEEDLGSMEG-LEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRlQQELDDLMVDL 1451
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdLHERLNGLESeLAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1452 DHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERD--RAEAEAREKDTKALSMARALEEALEAkeelerfnkQLRAEME 1529
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARREELEDRDE---------ELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1530 DLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqardEQGEEKKRLL 1609
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV----------------------EDRREEIEEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1610 VKQVREMEAELEDerkqrtlavaskkkLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDE---- 1685
Cdd:PRK02224 390 EEEIEELRERFGD--------------APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcp 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1686 ----------IFTQSKENEKKLKGLEAEILQLQEDHAASErarrhaeqERDELADEISNSASGKSSLLEEKRRLEARIAQ 1755
Cdd:PRK02224 456 ecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1756 LEEELEEEQGNMELLNDRfrksniqVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSkfKASIAALE 1835
Cdd:PRK02224 528 RRETIEEKRERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES--LERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1836 AKILQLEDQLEqeakeraaankivRRTEKklKEVMMQVEDERRhadqykEQMEKANSRMKQLKRQLEEAEEEATRANATR 1915
Cdd:PRK02224 599 AAIADAEDEIE-------------RLREK--REALAELNDERR------ERLAEKRERKRELEAEFDEARIEEAREDKER 657
|
570 580 590
....*....|....*....|....*....|....*
gi 1604804600 1916 -----RKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:PRK02224 658 aeeylEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
930-1888 |
1.78e-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: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 930 SRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaARQKLQLDKVTAEAKIKKMEEDILLLEDQN 1009
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-------KLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1010 SKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAEttdlqdqIVEL 1089
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE-------EEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1090 QAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTE 1169
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1170 LedtLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNK 1249
Cdd:pfam02463 379 K---KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1250 ELSCDVKTLQQAKTESehKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLN 1329
Cdd:pfam02463 456 QELKLLKDELELKKSE--DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1330 SKLQDSEELRQEETRQklnlstqirqlEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVK 1409
Cdd:pfam02463 534 LGVAVENYKVAISTAV-----------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1410 RKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKqkkfdqlLAEEKTISAQYAEERDRA 1489
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEG-------LAEKSEVKASLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1490 EAEAREKDTKALSMARALEEALEAKEElerfNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1569
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIK----KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1570 LQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQGEEKKRLLVKQVREMEAELEDERKqrtlAVASKKKLEMDLNELEGQIE 1649
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEKEL---AEEREKTEKLKVEEEKEEKLKAQEEELR----ALEEELKEEAELLEEEQLLI 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1650 AANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKgleaeilqlqedhaaserarrhaEQERDELA 1729
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELL-----------------------LKEEELEE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1730 DEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQN 1809
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1810 KDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQME 1888
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
866-1418 |
1.85e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 79.29 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 866 EEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHaetelfaeaeemrvRLLSRKQELEEILHDLESR 945
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN--------------LLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 946 VEEEEERNQSLQ--NEK-KKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSkflKEKKLLEDR 1022
Cdd:TIGR04523 196 LLKLELLLSNLKkkIQKnKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN---KIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1023 ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTR-QELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLT 1101
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1102 KKEEELQaalaRSDEETLQKNNALKQVRELQAHLAELQEDLESEK----MCRSKAEKLKRDLSEELEALKTELEDTLDTt 1177
Cdd:TIGR04523 353 NSESENS----EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndleSKIQNQEKLNQQKDEQIKKLQQEKELLEKE- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1178 aaQQELRSKREQEVAELKKAIDEETKnHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscdvKT 1257
Cdd:TIGR04523 428 --IERLKETIIKNNSEIKDLTNQDSV-KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL----KK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1258 LQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTmlevaEKKGLKLAKEVDKLNSKLQDSEE 1337
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF-----ELKKENLEKEIDEKNKEIEELKQ 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1338 LRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQmvqsqmfETKKKLEEDLGSMEGLEEVKRKLQKDVE 1417
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE-------KAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
.
gi 1604804600 1418 L 1418
Cdd:TIGR04523 649 Q 649
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
859-1341 |
1.96e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 859 LLQVTRQEEELQAKDeelvkVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLlsrkQELEEI 938
Cdd:PRK02224 189 LDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 939 LHDLESRVEEEEERNQSLQNEkkkMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAkikkmeedillLEDQNSKFLKEKKL 1018
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLDDADAEA-----------VEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1019 LEDRISEMTSQLTEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKF 1098
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDAD-------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1099 QLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKM-------------------------CRSKAE 1153
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1154 KLKRDLS----------------EELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID---EETKNHEAQIQEMRQ 1214
Cdd:PRK02224 479 ELEAELEdleeeveeveerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEelrERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1215 RQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKelscdVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELA 1294
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1604804600 1295 ERSHKLQTELDNActMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQE 1341
Cdd:PRK02224 634 ERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
915-1251 |
3.44e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.57 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 915 TELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMqshiqdleeqlDEEEAARQKLQLDKVTAEAK 994
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-----------GEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 995 IKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNL------GKVKNKQEMMMvDLEERLKKEEKTRQEL 1068
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshSRIPEIQAELS-KLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1069 EKAKRKLDAETTDLQDQIVELQAQIEELKFQ---LTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESE 1145
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1146 KmcrSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKnhEAQIQEMRQRQATALEELS- 1224
Cdd:TIGR02169 898 L---RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRALEp 972
|
330 340 350
....*....|....*....|....*....|...
gi 1604804600 1225 ------EQLEQAKRFKSNLEKNKQSLENDNKEL 1251
Cdd:TIGR02169 973 vnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1061-1945 |
3.84e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1061 EEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALarsDEETLQKNNALKQVRELQAHLAELQE 1140
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAL---EYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1141 DLESEKmcrskaEKLKRDLSEELEALKTELEDtldttaaqqelrskrEQEVAELKKAIDEETKNHEAQIQEMRQRQATAL 1220
Cdd:pfam02463 237 ERIDLL------QELLRDEQEEIESSKQEIEK---------------EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1221 EELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKL 1300
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1301 QTELDNACTMLEVAEK-KGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEK 1379
Cdd:pfam02463 376 LAKKKLESERLSSAAKlKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1380 QLQMVQSQMFETKKKLEEdlgsMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQrqiVS 1459
Cdd:pfam02463 456 QELKLLKDELELKKSEDL----LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIS---AH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1460 NLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRA--EMEDLMSSKDD 1537
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvlEIDPILNLAQL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1538 VGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREME 1617
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1618 AELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAvkQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKL 1697
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE--AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1698 KGLEAEILQLQEDHAASERARRHAEQERDELADEIS-NSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRK 1776
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEElRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1777 SNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAAN 1856
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1857 KIVRR-----TEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEG 1931
Cdd:pfam02463 927 AEILLkyeeePEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
890
....*....|....
gi 1604804600 1932 LTREVSSLKNRLRR 1945
Cdd:pfam02463 1007 LIRAIIEETCQRLK 1020
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1185-1945 |
4.14e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1185 SKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDnkelscDVKTLQQAKTE 1264
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE------DARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1265 SEHKRKKLEAQLQEfmARATEAERtKGELAERshklqteLDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETR 1344
Cdd:PTZ00121 1149 EDAKRVEIARKAED--ARKAEEAR-KAEDAKK-------AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1345 QklnlSTQIRQLEVDRNTllEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKdveltSQCLE 1424
Cdd:PTZ00121 1219 K----AEDAKKAEAVKKA--EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE-----LKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1425 EKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL--AEEKTISAQYAEERDRAEAEAREKDTKALS 1502
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1503 MARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKsKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1582
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1583 NMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRtlAVASKKKLEmdlnELEGQIEAANKGrDEAVKQL 1662
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK--AEEAKKKAD----EAKKAAEAKKKA-DEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1663 RKLQAqmkDYQRELEEARASRDEIFTQSKENEKKLKglEAEILQLQEDHAASERARRhAEQERDELADEISNSASGKSSL 1742
Cdd:PTZ00121 1520 EAKKA---DEAKKAEEAKKADEAKKAEEKKKADELK--KAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEAR 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1743 LEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQmERQNKDLKAKLAELEGT 1822
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1823 VKSKfkasiaALEAKilqledQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKR--- 1899
Cdd:PTZ00121 1673 DKKK------AEEAK------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeae 1740
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1900 -------QLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:PTZ00121 1741 edkkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1464 |
4.39e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 864 RQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNilAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLE 943
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 944 SRveeeEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEdillledqnSKFLKEKKLLEDRI 1023
Cdd:PTZ00121 1456 AK----KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---------KKKADEAKKAEEAK 1522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1024 SEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaETTDLQDQIVELQAQIEELKFQ---- 1099
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmk 1599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1100 LTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKmcrSKAEKLKRdlSEELEALKTELEdtldttaA 1179
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------A 1667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1180 QQELRSKREQEvaELKKAIDEETKNHEAQIQEmrQRQATALEEL----SEQLEQAKRFKSNLEKNKQSLENDNKELSCDV 1255
Cdd:PTZ00121 1668 KKAEEDKKKAE--EAKKAEEDEKKAAEALKKE--AEEAKKAEELkkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1256 KTLQQAKTESEHKrKKLEAQLQEFMARATEAERTKGELAErshklqteldnactmlEVAEKKGLKLAKEVDKLNSKLQDS 1335
Cdd:PTZ00121 1744 KKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIE----------------EELDEEDEKRRMEVDKKIKDIFDN 1806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1336 EELRQEETRQ--------KLNLSTQIRQLEVDRNTLLEQQEEEEEAR--RNLEKQLQMVQSQMFETKKKLEEDLgsMEGL 1405
Cdd:PTZ00121 1807 FANIIEGGKEgnlvindsKEMEDSAIKEVADSKNMQLEEADAFEKHKfnKNNENGEDGNKEADFNKEKDLKEDD--EEEI 1884
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1406 EEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQElDDLMVDLDHQRQIVSNLEKK 1464
Cdd:PTZ00121 1885 EEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD-EYIKRDAEETREEIIKISKK 1942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1657 |
5.12e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 859 LLQVTRQEEELQAKDEELVKVKERqLKVENELVEmerKHQQLIEEKNILA--EQLHAETELFAEAEEMRVRLLSRKQELE 936
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLER-LRREREKAE---RYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 937 EILHDLESRVEEEEERNQSLQNEKKKMqshiqdleEQLDEEEAARQKLQLDKVTAEakIKKMEEDILLLEDQNSKFLKEK 1016
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI--------KDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1017 KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEEL 1096
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1097 KFQLTKKEEELQaalaRSDEETLQKNNALKQVRE-----------LQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEA 1165
Cdd:TIGR02169 405 KRELDRLQEELQ----RLSEELADLNAAIAGIEAkineleeekedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1166 LKTELE------DTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALE----------------EL 1223
Cdd:TIGR02169 481 VEKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1224 SEQLEQAKRFK----SNLEKNK-QSLENDNKELSCD-----------------------------VKTLQQAKTESEHKR 1269
Cdd:TIGR02169 561 KEAIELLKRRKagraTFLPLNKmRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMGKYR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1270 K-KLEAQLQEFMARATEAERTKGELAERSHKLQTELdnactmLEVAEKKGlKLAKEVDKLNSKLQDSEELRQEETRQKLN 1348
Cdd:TIGR02169 641 MvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL------QRLRERLE-GLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1349 LSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVE-----LTSQCL 1423
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1424 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKAlsm 1503
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL--- 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1504 araleealeakEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMR-------TQLEELEDELQATEDA 1576
Cdd:TIGR02169 871 -----------EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRkrlselkAKLEALEEELSEIEDP 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1577 KLRLEvnmqamkaqfdrdlqaRDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRD 1656
Cdd:TIGR02169 940 KGEDE----------------EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
.
gi 1604804600 1657 E 1657
Cdd:TIGR02169 1004 A 1004
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
904-1478 |
5.37e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.75 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 904 KNILAEQLHAETELFAEAEEMRVRLLSRKQELEeilhDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK 983
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELK----NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 984 LQLDKVTAEAKIKKMEEDILLLEDQNSK--------------FLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEM 1049
Cdd:TIGR04523 101 LNSDLSKINSEIKNDKEQKNKLEVELNKlekqkkenkknidkFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1050 MMVDLEER-----------------LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALA 1112
Cdd:TIGR04523 181 EKLNIQKNidkiknkllklelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1113 RSDEETLQKNNALKQVRELQAHLAELQEDL-----ESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1187
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1188 EQEVAELKKAIDEETKNHEAQIQEMRQRQaTALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEH 1267
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1268 KRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKL 1347
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1348 NLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSM--EGLEEVKRKLQKDVELTSQCLEE 1425
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKS 579
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1426 KTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKTI 1478
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNI 636
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1213-1935 |
8.57e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1213 RQRQATALEELSEQLEQAKRFKSNLEKNKQSLENdnkelscdvktLQQAKTESEHKRKKLEaqlqEFMARATEAERTKGE 1292
Cdd:PRK03918 133 RQGEIDAILESDESREKVVRQILGLDDYENAYKN-----------LGEVIKEIKRRIERLE----KFIKRTENIEELIKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1293 LAERSHKLQTELDNActmlevaEKKGLKLAKEVDKLNSKLQDSEELRQEETrqklNLSTQIRQLEVDRntlleqqeeeee 1372
Cdd:PRK03918 198 KEKELEEVLREINEI-------SSELPELREELEKLEKEVKELEELKEEIE----ELEKELESLEGSK------------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1373 arRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELtSQCLEEKTMAMDKMEKTKNRLQQELDDLmvdld 1452
Cdd:PRK03918 255 --RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL-SEFYEEYLDELREIEKRLSRLEEEINGI----- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1453 hQRQIvSNLEKKQKKFDQLLAEEKTISAQYAEerdraeaeaREKDTKALSMARALEEALeakeelerfnKQLRAEMEDLm 1532
Cdd:PRK03918 327 -EERI-KELEEKEERLEELKKKLKELEKRLEE---------LEERHELYEEAKAKKEEL----------ERLKKRLTGL- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1533 sSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFDRDLQARDEQGEEKKRLLvkq 1612
Cdd:PRK03918 385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL--- 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1613 vREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGR--DEAVKQLRKLQAQMKDYQRE-LEEARASRDEIFTQ 1689
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEK 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1690 SKENEKKLKGLEAEILQLQE---DHAASERARRHAEQERDELADEISNSasGKSSLLEEKRRLEariaqleeeleeeqgN 1766
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEEL--GFESVEELEERLK---------------E 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1767 MELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLE 1846
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1847 QEAKERAAANKIVRRTEKKLKEVMMQVEdERRHADQYKEQMEKANSRMKQLKRQLEEAeeeatRANATRRKLQRELDDAT 1926
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKVKKY-----KALLKERALSKVGEIAS 750
|
....*....
gi 1604804600 1927 EASEGLTRE 1935
Cdd:PRK03918 751 EIFEELTEG 759
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
859-1665 |
9.66e-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: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 859 LLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETEL----FAEAEEMRVRLLSRKQE 934
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 935 LEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLD-KVTAEAKIKKMEEDILLLEDQNSKFL 1013
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLlKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1093
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EELKF--------QLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLS--EEL 1163
Cdd:pfam02463 528 HGRLGdlgvavenYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIlnLAQ 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1164 EALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQS 1243
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1244 LENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERShklqtELDNACTMLEVAEKKGLKLAK 1323
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL-----KQKIDEEEEEEEKSRLKKEEK 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1324 EVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEvdrntlleqqeeeeearRNLEKQLQMVQSQMFETKKKLEEDLGSME 1403
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL-----------------KAQEEELRALEEELKEEAELLEEEQLLIE 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1404 GLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQivSNLEKKQKKFDQLLAEEKTISAQYA 1483
Cdd:pfam02463 826 QEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE--LEEQKLKDELESKEEKEKEEKKELE 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1484 EERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDdvgknvhELEKSKRTLEQQVEEMRTQL 1563
Cdd:pfam02463 904 EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-------EEEERNKRLLLAKEELGKVN 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1564 EELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNE 1643
Cdd:pfam02463 977 LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDP 1056
|
810 820
....*....|....*....|..
gi 1604804600 1644 LEGQIEAANKGRDEAVKQLRKL 1665
Cdd:pfam02463 1057 FSGGIEISARPPGKGVKNLDLL 1078
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
867-1582 |
2.87e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.54 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 867 EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETElfAEAEEMRVRLLSRK---QELEEILHDLE 943
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 944 SRVEEEEERNQSLQNEK-KKMQSHIQDLEEQLDEEEAARQ------KLQLDKVTAEAKiKKMEediLLLEDQNSKflkek 1016
Cdd:pfam15921 198 EASGKKIYEHDSMSTMHfRSLGSAISKILRELDTEISYLKgrifpvEDQLEALKSESQ-NKIE---LLLQQHQDR----- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1017 klLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEErlkkeeKTRQELEKAKRKLdaetTDLQDQIVELQAQIEEL 1096
Cdd:pfam15921 269 --IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE------QARNQNSMYMRQL----SDLESTVSQLRSELREA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1097 KFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDT 1176
Cdd:pfam15921 337 KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1177 TAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSE---QLEQAK----RFKSNLEKNKQSLENDNK 1249
Cdd:pfam15921 417 LRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKemlrKVVEELTAKKMTLESSER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1250 ELSCDVKTLQQAK-------TESEHKRKKLEAQLQEFM----------ARATEAERTKGELAERSHKLQTELDNACTMLE 1312
Cdd:pfam15921 497 TVSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQhlknegdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1313 VAEKKG----------LKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQlq 1382
Cdd:pfam15921 577 LVGQHGrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQE-- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1383 mvQSQMFETKKKLEEDLGSM-EGLEEVKRKLQKDVEltsqcleektmamdKMEKTKNRLQQELDDLMVDLDHQRQIVSNL 1461
Cdd:pfam15921 655 --RDQLLNEVKTSRNELNSLsEDYEVLKRNFRNKSE--------------EMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1462 EKKQKKFDQL-LAEEKTISAQyaeerdRAEAEAREKDTKALSMARALEEALEAKEELERfnKQLRAEMEDLMSSKDDVGK 1540
Cdd:pfam15921 719 EGSDGHAMKVaMGMQKQITAK------RGQIDALQSKIQFLEEAMTNANKEKHFLKEEK--NKLSQELSTVATEKNKMAG 790
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1604804600 1541 NVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1582
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1061-1751 |
3.56e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.08 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1061 EEKTRQELEKAKRKLDA-ETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLqknnALKQVRELQAHLAELQ 1139
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE----VLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1140 EDLESEKMCRSKAEKLKRDLSEELEALK---TELEDTLDTTAAQQELRSKREQEVAELKKAIDEEtknhEAQIQEMRQRQ 1216
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRerlEELEEERDDLLAEAGLDDADAEAVEARREELEDR----DEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1217 ATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAER 1296
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1297 SHKLQTELDnactmlevaekkglklakevdklnsklqdseELRQEETrqklnlstqirQLEVDRNTlleqqeeeeeARRN 1376
Cdd:PRK02224 414 LEELREERD-------------------------------ELREREA-----------ELEATLRT----------ARER 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1377 LEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLqkdveltsqclEEKTMAMDKMEKTKNRLQQELDDLmVDLDHQRQ 1456
Cdd:PRK02224 442 VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERV-----------EELEAELEDLEEEVEEVEERLERA-EDLVEAED 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1457 IVSNLEKKQKKFDQLLAEEKTISAqyaEERDRAEaearekdtkalsmaraleealeakeelerfnkQLRAEMEDLMSSKD 1536
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIE---EKRERAE--------------------------------ELRERAAELEAEAE 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1537 dvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaQFDRDLQARDEQGEEKKRLLVKqvREM 1616
Cdd:PRK02224 555 -------EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE--------RIRTLLAAIADAEDEIERLREK--REA 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1617 EAELEDERKQRTLAVASKKKlemdlnELEGQIEAANkgrdeavkqlrklqaqmkdyqreLEEARASRDEIFTQSKENEKK 1696
Cdd:PRK02224 618 LAELNDERRERLAEKRERKR------ELEAEFDEAR-----------------------IEEAREDKERAEEYLEQVEEK 668
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1697 LKGLEAEILQLQEDHAASERARRHAEQERDELaDEISNSASGKSSLLEEKRRLEA 1751
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEELEELRERR-EALENRVEALEALYDEAEELES 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1151-1750 |
5.22e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1151 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNheaqiqemrqrqataLEELSEQLEQA 1230
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE---------------LPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1231 KRFKSNLEKNKQSLENDNKELscdvKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAErshklqteldnactm 1310
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1311 LEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEvdrntlleqqeeeeearrNLEKQLQMVQSQMFE 1390
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE------------------EKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1391 TKKKLEEDLGSMEGLEEVKRKLQK----DVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1466
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1467 KFD----------QLLAEE--KTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKqLRAEMEDLMSS 1534
Cdd:PRK03918 430 ELKkakgkcpvcgRELTEEhrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1535 KDDVGK-NVHELEKSK---RTLEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqfdrdlqaRDEQGEEKKRLLV 1610
Cdd:PRK03918 509 EEKLKKyNLEELEKKAeeyEKLKEKLIKLKGEIKSLKKELE--------------------------KLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1611 KQVREMEAELED-ERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDeAVKQLRKLQAQMKDYQRELEEARASRDEIFTQ 1689
Cdd:PRK03918 563 KKLDELEEELAElLKELEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1690 SKENEKKL------------KGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLE 1750
Cdd:PRK03918 642 LEELRKELeelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1014-1581 |
5.83e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.31 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKakrkLDAETTDLQDQIVE----- 1088
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1089 --LQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLE----SEKMCRSKAEKLK---RDL 1159
Cdd:PRK02224 275 eeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLRedaDDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1160 SEELEALKTELEDTLDTTAAQQELRSKREQEVAELkkaideetknhEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEK 1239
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEEL-----------EEEIEELRER----FGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1240 NKQSLENDNKELSCDVKTLQQAKTESEHKRKK-------LEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLE 1312
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1313 VAEKKgLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETK 1392
Cdd:PRK02224 500 RAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1393 KKLEEDLGSMEGLEEVkRKLQKDVELTSQCLEEKTmamdkmEKTKNrlQQELDDLMVD-LDHQRQIVSNLEKKqkkFD-- 1469
Cdd:PRK02224 579 SKLAELKERIESLERI-RTLLAAIADAEDEIERLR------EKREA--LAELNDERRErLAEKRERKRELEAE---FDea 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1470 --QLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLmsskDDVGKNVHELEK 1547
Cdd:PRK02224 647 riEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAL----EALYDEAEELES 722
|
570 580 590
....*....|....*....|....*....|....*....
gi 1604804600 1548 SKRTL-----EQQVEEMRTQLEELEDeLQATEDAKLRLE 1581
Cdd:PRK02224 723 MYGDLraelrQRNVETLERMLNETFD-LVYQNDAYSHIE 760
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1053-1227 |
6.22e-13 |
|
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: 70.34 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1053 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQvRELQ 1132
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1133 AhlaeLQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDEETKNHEAQIQEM 1212
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 1604804600 1213 RQRQATALEELSEQL 1227
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
988-1710 |
6.86e-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: 74.23 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 988 KVTAEAKIKKMEEDILLLED----QNSKFLKEKKLLEDRISEMTS---QLTEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1060
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLctpcMPDTYHERKQVLEKELKHLREalqQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1061 EEKTRQE---LEKAKRKLDAETTDLQdqIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAE 1137
Cdd:TIGR00618 269 IEELRAQeavLEETQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1138 LQEDLESEKMCRSKAEKLKRDLSEELEAlkTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQE---MRQ 1214
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdLQG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1215 RQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscdvKTLQQAKTEsehkRKKLEAQLQEFMARATEAERTKGELA 1294
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL----QESAQSLKE----REQQLQTKEQIHLQETRKKAVVLARL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1295 ERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEEtrqklnlstqirqlevdrntlleqqeeeeear 1374
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSE-------------------------------- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1375 RNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQ 1454
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1455 rQIVSNLEKKQKKFDQLLAEEKTISAQYAEE---RDRAEAEAREKDTKALSMARALEEALEAKEELERFN------KQLR 1525
Cdd:TIGR00618 625 -QDLQDVRLHLQQCSQELALKLTALHALQLTltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywkemlAQCQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1526 AEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEK 1605
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1606 KRLLVKQVREMEaelEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLR---KLQAQMKDYQRELEEARAS 1682
Cdd:TIGR00618 784 AAEIQFFNRLRE---EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEeksATLGEITHQLLKYEECSKQ 860
|
730 740 750
....*....|....*....|....*....|.
gi 1604804600 1683 RDEIFTQSK---ENEKKLKGLEAEILQLQED 1710
Cdd:TIGR00618 861 LAQLTQEQAkiiQLSDKLNGINQIKIQFDGD 891
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1028-1776 |
6.93e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1028 SQLTEEEEKAKNLGKVKNKQEMMMVDlEERLKKEEKTRQEleKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEEL 1107
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAE-EARKAEEAKKKAE--DARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1108 -QAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRsKAEKLKRdlseELEALKTELEDTLDTTAAQQELRSK 1186
Cdd:PTZ00121 1164 rKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR-KAEEERK----AEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1187 REqevaELKKAidEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESE 1266
Cdd:PTZ00121 1239 AE----EAKKA--EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1267 HKRKkleaqlqefmarATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKlQDSEELRQEETRQK 1346
Cdd:PTZ00121 1313 EAKK------------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1347 LNlSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDvELTSQCLEEK 1426
Cdd:PTZ00121 1380 AD-AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1427 TMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL----AEEKTISAQYAEERDRAE----AEAREKDT 1498
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaaeAKKKADEAKKAEEAKKADeakkAEEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1499 KALSMARALEEALEAKEELERFNKQLRaEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE----DELQATE 1574
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAE 1616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1575 DAKLRLEvnmQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRtlavasKKKLEMDLNELEgqiEAANKG 1654
Cdd:PTZ00121 1617 EAKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE------AKKAEEDKKKAE---EAKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1655 RDEavkqlRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISN 1734
Cdd:PTZ00121 1685 EDE-----KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1604804600 1735 SASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRK 1776
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
822-1474 |
8.19e-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: 74.23 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 822 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEELQAKDEELvKVKERQLKVENELVEMERKhqqli 901
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERINRARK----- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 902 eeKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAAR 981
Cdd:TIGR00618 292 --AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 982 QKLQldKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKE 1061
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1062 EKTRQ-------ELEKAKRKLDAETTDLQDQIV-----------------ELQAQIEELKFQLTKKEEELQAA------- 1110
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKEQihlqetrkkavvlarllELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1111 --LARSDEETLQKNNALKQVR----ELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1184
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1185 SK-----REQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKelscdvktlQ 1259
Cdd:TIGR00618 608 DMlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS---------R 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1260 QAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLevaekkGLKLAKEVDKLNSKLQDSEELR 1339
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL------GSDLAAREDALNQSLKELMHQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1340 QEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVK-RKLQKDVEL 1418
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQcETLVQEEEQ 832
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1419 TSQCLEEKTmamdkmektknRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE 1474
Cdd:TIGR00618 833 FLSRLEEKS-----------ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
855-1341 |
1.34e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 855 KVKPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQE 934
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 935 LEEILHDLESRVeeeeERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKL----QLDKVTAEAKIKKMEEDILLLEDQNS 1010
Cdd:PRK03918 326 IEERIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEKLEKELEELEKAKE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1011 KFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEektrqelekAKRKLDAETTDLQDQIVELQ 1090
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE---------LLEEYTAELKRIEKELKEIE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1091 AQIEELKFQLTKKEEELqaalarSDEETLQKNNAL-KQVRELQAHLAELQ-EDLEsekmcrsKAEKLKRDLSEELEALKT 1168
Cdd:PRK03918 473 EKERKLRKELRELEKVL------KKESELIKLKELaEQLKELEEKLKKYNlEELE-------KKAEEYEKLKEKLIKLKG 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1169 ELEDTLDTTAAQQELRSKREqevaELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRF----------KSNLE 1238
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdaEKELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1239 KNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFmarateAERTKGELAERSHKLQTELDNACTMLEVAEKKG 1318
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY------SEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
490 500
....*....|....*....|...
gi 1604804600 1319 LKLAKEVDKLNSKLQDSEELRQE 1341
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKE 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1187-1900 |
2.43e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1187 REQEVAELKKAIDEETK-NHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSC--DVKTLQQAKT 1263
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKaeEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1264 ESEHKRKKLEAQLQEFMARATEAERTKgelAERSHKLQTELDNAcTMLEVAEKkglklAKEVDKLNSKLQDSEELRQEET 1343
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAE---DAKRVEIARKAEDA-RKAEEARK-----AEDAKKAEAARKAEEVRKAEEL 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1344 RQklnlSTQIRQLEVDRntlleqqeeEEEARRNLEKQLQMVQSQMFETKKKLEEdlgSMEGLEEVKRKLQKDVELTSQCL 1423
Cdd:PTZ00121 1194 RK----AEDARKAEAAR---------KAEEERKAEEARKAEDAKKAEAVKKAEE---AKKDAEEAKKAEEERNNEEIRKF 1257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1424 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqllAEEKTISAQYAEERDRAEAEAREKDTKALSM 1503
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1504 ARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRtQLEELEDelQATEDAKLRLEVN 1583
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKK--KAEEDKKKADELK 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1584 MQAMKAQFDRDLQARDEQgeekkrllVKQVREMEAELEDERKqrtlAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLR 1663
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEE--------KKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1664 KLQAQMKDYQRELEEARASRDEIftQSKENEKKlkglEAEILQLQEDHAASERARRHAEQERdelADEIsNSASGKSSLL 1743
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEA--KKAAEAKK----KADEAKKAEEAKKADEAKKAEEAKK---ADEA-KKAEEKKKAD 1549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1744 EEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNI--QVDNLNTELAG---ERSAAQKSENARQQMERQNKDLKAKLAE 1818
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMklyEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1819 LEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANsRMKQLK 1898
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELK 1708
|
..
gi 1604804600 1899 RQ 1900
Cdd:PTZ00121 1709 KK 1710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
864-1497 |
2.69e-12 |
|
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: 72.06 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 864 RQEEELQAKDEELVKVKER---QLKVENELVEME-----RKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQEL 935
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKaiqELQFENEKVSLKleeeiQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREET 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 936 EEILHDLESRVEEEEERNQSL--QNEKKKMQSHIQDLEEQLDEEEAARQ----------KLQLDKVTAEAKIKKMEEDIL 1003
Cdd:pfam05483 182 RQVYMDLNNNIEKMILAFEELrvQAENARLEMHFKLKEDHEKIQHLEEEykkeindkekQVSLLLIQITEKENKMKDLTF 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1004 LLEDQNSKF--LKEKKLLED----RISEMTSQLTEEEEKAK-NLGKVKNKQEMMMVDLEERLKK-----EEKTRQ--ELE 1069
Cdd:pfam05483 262 LLEESRDKAnqLEEKTKLQDenlkELIEKKDHLTKELEDIKmSLQRSMSTQKALEEDLQIATKTicqltEEKEAQmeELN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1070 KAK-------RKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDL 1142
Cdd:pfam05483 342 KAKaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1143 ESEKMCRSKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEE 1222
Cdd:pfam05483 422 DEKKQFEKIAEELK-GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1223 LSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQT 1302
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1303 ELDNACTMLEVAEKKGLKLAKEVDKLNSKLqdsEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQ 1382
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNI---EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIID 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1383 MVQSQMfETKKKLEEDLgsmegLEEVKR---------KLQKDVELTSQCLEEKTMAMdkMEKTKNrlqqELDDLMVDLDH 1453
Cdd:pfam05483 658 NYQKEI-EDKKISEEKL-----LEEVEKakaiadeavKLQKEIDKRCQHKIAEMVAL--MEKHKH----QYDKIIEERDS 725
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1604804600 1454 QRQIVSNLEKKQKKFDQLLAEE-KTISAQYAEERDRAEAEAREKD 1497
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKE 770
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
993-1820 |
2.78e-12 |
|
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: 72.39 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 993 AKIKKMEEDILLLEDQNSKFLKEKKLLEdRISEMTSQLTEEE--EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEK 1070
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELE-LKMEKVFQGTDEQlnDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1071 AKRKLDAETTDLQDQIVELQAQIeeLKFQLTKKEEELQAAL---ARSDEETLQKNNALKQVRELQAHLAELQEDLESEkm 1147
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHI--RARDSLIQSLATRLELdgfERGPFSERQIKNFHTLVIERQEDEAKTAAQLCAD-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1148 cRSKAEKLKRDLSEELEALKTELEDTLDT-----TAAQQELRSKReQEVAELKKAIDEETKNHEAQIQEMRQ----RQAT 1218
Cdd:TIGR00606 417 -LQSKERLKQEQADEIRDEKKGLGRTIELkkeilEKKQEELKFVI-KELQQLEGSSDRILELDQELRKAERElskaEKNS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1219 ALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEaQLQEFMARATEA------------ 1286
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDEltsllgyfpnkk 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1287 ---------ERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKlNLSTQIRQLE 1357
Cdd:TIGR00606 574 qledwlhskSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLE-RLKEEIEKSS 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1358 VDRNTLLEQQEEEEEARRNLEKQLQM---VQSQMFETKKKLEE---DLGSM--------EGLEEVKRKLQKDVELTSQCL 1423
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEfisDLQSKlrlapdklKSTESELKKKEKRRDEMLGLA 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1424 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRqivSNLEKKQKKFDQLLAEEKTISAQyaeERDRAEAEAREKDTKALSM 1503
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLLGTIMPEEESAKVC---LTDVTIMERFQMELKDVER 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1504 ARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDElqatedaKLRLEVN 1583
Cdd:TIGR00606 807 KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-------KLQIGTN 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1584 MQamkaqfdrdlqaRDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLR 1663
Cdd:TIGR00606 880 LQ------------RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1664 KLQAQMKDYQRELEEARASRDEIFTQSKENEkklkgLEAEILQLQEdhaaSERARRHAEQERDELADEISNSASGKSSLL 1743
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKETE-----LNTVNAQLEE----CEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1744 EEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELE 1820
Cdd:TIGR00606 1019 DNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
821-1144 |
4.16e-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: 72.01 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 821 FAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTkvkpllQVTRQEEELQAKDEELVKVKERQLKVENELVEmerkhqqL 900
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLSKELTE-------L 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 901 IEEKNILAEQLHAETELFAEAEEmrvrllsRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAA 980
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 981 RQKLQLDKVTAEAKIKKMEEDILLLEDQnskflkekklledrISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1060
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1061 EEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQK-NNALKQVRELQAHLAELQ 1139
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLE 978
|
....*
gi 1604804600 1140 EDLES 1144
Cdd:TIGR02168 979 NKIKE 983
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1055-1755 |
5.46e-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: 71.52 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1055 EERLKKEEKT---RQELEKAKRKLDAEttdlQDQIVELQAQIEELKFQLTKKEEELQAAlarsdEETLQK-NNALKQ--- 1127
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAA-----SDHLNLvQTALRQqek 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1128 VRELQAHLAELQEDLESEKMCRskaeklkrdlsEELEALKTELEDTLdtTAAQQELRSKREQeVAELKKAIDEEtknhea 1207
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVV-----------EEAAEQLAEAEARL--EAAEEEVDSLKSQ-LADYQQALDVQ------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1208 QIQEMRQRQA-TALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEA 1286
Cdd:COG3096 409 QTRAIQYQQAvQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1287 ERtkGELAERSHKLQTELDNACTMLEVAEKKGLKLAkEVDKLNSKLQDSEELRQEETRQ-------KLNLSTQIRQLEVD 1359
Cdd:COG3096 489 ER--SQAWQTARELLRRYRSQQALAQRLQQLRAQLA-ELEQRLRQQQNAERLLEEFCQRigqqldaAEELEELLAELEAQ 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1360 RNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKK-------------LEEDLG-SMEGLEEVKRKLQKDVELtsqcLEE 1425
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdalerLREQSGeALADSQEVTAAMQQLLER----ERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1426 KTMAMDKMEKTKNRLQQELDDLM----------------------------VDLD------------HQRQIVSNLEKKQ 1465
Cdd:COG3096 642 ATVERDELAARKQALESQIERLSqpggaedprllalaerlggvllseiyddVTLEdapyfsalygpaRHAIVVPDLSAVK 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1466 KKFDQL---------------LAEEKTISAQYAEERDRAEAE------------------AREKDTKALSMARALEEALE 1512
Cdd:COG3096 722 EQLAGLedcpedlyliegdpdSFDDSVFDAEELEDAVVVKLSdrqwrysrfpevplfgraAREKRLEELRAERDELAEQY 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1513 AKEELER---------------------FNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQL-------- 1563
Cdd:COG3096 802 AKASFDVqklqrlhqafsqfvgghlavaFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLqllnkllp 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1564 --------------EELEDELQATEDAKL----------RLEVNMQAMK---AQFDRdLQARDEQGEEKKRLLVKQVREM 1616
Cdd:COG3096 882 qanlladetladrlEELREELDAAQEAQAfiqqhgkalaQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFAL 960
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1617 EaeledERKQRTLAVASKKKLEM-----DLNE-LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQS 1690
Cdd:COG3096 961 S-----EVVQRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTL 1035
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1691 KENEKKLKGLEaeilqLQEDHAASERARrhaeQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1755
Cdd:COG3096 1036 QELEQELEELG-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1220-1874 |
8.37e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.43 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1220 LEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHK 1299
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1300 LQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEK 1379
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1380 QLQMVQSQMfETKKKLEEDLgsmEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQivs 1459
Cdd:TIGR04523 202 LLSNLKKKI-QKNKSLESQI---SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1460 NLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEArEKDTKalSMARALEEALEAKEELERFNKQLRAEMEDLMSskdDVG 1539
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-NKELK--SELKNQEKKLEEIQNQISQNNKIISQLNEQIS---QLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1540 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQGEEKKRLLVKQVREMEAE 1619
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDEQIKKLQQEKELLEKE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1620 LEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEavkqlrkLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKG 1699
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-------LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1700 LEAEILQLqedhaaserarrhaEQERDELADEISnsasgksSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNI 1779
Cdd:TIGR04523 501 LNEEKKEL--------------EEKVKDLTKKIS-------SLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1780 --QVDNLNTELagersaaQKSENARQQMERQNKDLKAKLAELEgTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANK 1857
Cdd:TIGR04523 560 ekEIDEKNKEI-------EELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
650
....*....|....*..
gi 1604804600 1858 IVRRTEKKLKEVMMQVE 1874
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVK 648
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1014-1236 |
1.23e-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: 68.64 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1093
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDT 1173
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1174 LdttAAQQELRSKREQEVAELKKAIDEEtknhEAQIQEMrQRQATALEELSEQLEQAKRFKSN 1236
Cdd:COG4942 187 R---AALEALKAERQKLLARLEKELAEL----AAELAEL-QQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
2.05e-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: 60.52 E-value: 2.05e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1604804600 31 TAKRLVWIPSERNGFEAASVREERGDEVVVELaENGKKAVVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1140-1900 |
2.16e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1140 EDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATA 1219
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1220 LEELSEQLEQAKRfksnLEKNKQSLENDNKELSCDVKTLQQAKTE--SEHKRKKLEAQLQEFMARATEAeRTKGELAERS 1297
Cdd:PTZ00121 1171 KAEDAKKAEAARK----AEEVRKAEELRKAEDARKAEAARKAEEErkAEEARKAEDAKKAEAVKKAEEA-KKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1298 HKLQTELD----NACTMLEVAEKKGLKLAKEVDKLNsKLQDSEELRQEETRQKLNlstqirqlEVDRNTLLEQQEEEEEA 1373
Cdd:PTZ00121 1246 EEERNNEEirkfEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKADEAKKAE--------EKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1374 RRNLEKQLQMVQSQMFETKKKLEEdlgsMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDH 1453
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEE----AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1454 QRQIVSNLEKKQKKFDQL--LAEEKTISAQY---AEERDRAEaEAREKDTKALSMARALEEALEAKEELERFNKQLRAEM 1528
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELkkAAAAKKKADEAkkkAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1529 EDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE--DELQATEDAKlrlevnmqamKAQFDRDLQARDEQGEEKK 1606
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAK----------KADEAKKAEEAKKADEAKK 1541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1607 RLLVKQVREMeaeledeRKQRTLAVASKKKlemdlnelegQIEAANKGRDEAVKQLRKLQaqmkdyqrELEEARASRDEI 1686
Cdd:PTZ00121 1542 AEEKKKADEL-------KKAEELKKAEEKK----------KAEEAKKAEEDKNMALRKAE--------EAKKAEEARIEE 1596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1687 FTQSKENEKKLKGLEAEilqlqedhaASERARRHAEQERDElADEISNSASGKSSLLEEKRRLEariaqleeeleeeqgn 1766
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAK---------KAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE---------------- 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1767 mellndRFRKsniqvdnlntelAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLE 1846
Cdd:PTZ00121 1651 ------ELKK------------AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1847 QEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANsRMKQLKRQ 1900
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKE 1765
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1053-1653 |
2.91e-11 |
|
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: 68.61 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1053 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQaalarsdeETLQKNNALKQVRELQ 1132
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR--------EQAELNRLKKKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1133 AHLAELQEDLESEkmcrskAEKLKRDLSEELEALKTELEDtldttaAQQELRSKReQEVAELKKAIDEEtknhEAQIQEM 1212
Cdd:pfam05557 89 NKKLNEKESQLAD------AREVISCLKNELSELRRQIQR------AELELQSTN-SELEELQERLDLL----KAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1213 RQRQATALEELSEQLEQAKRFKsNLEKNKQSLENDNKElscdVKTLqQAKTESEHKRKKLEAQLQEFMARATEAERTKGE 1292
Cdd:pfam05557 152 EQLRQNLEKQQSSLAEAEQRIK-ELEFEIQSQEQDSEI----VKNS-KSELARIPELEKELERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1293 LAERSHKLQTELDNactmLEVAEKKGLKLAKEVDKLNSKLQDSEELRQE---ETRQKLNLSTQIRQLEVDRNTLLEQQEE 1369
Cdd:pfam05557 226 LKEEVEDLKRKLER----EEKYREEAATLELEKEKLEQELQSWVKLAQDtglNLRSPEDLSRRIEQLQQREIVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1370 EEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQcleektmamdkmektknrlqqelddlmv 1449
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTK---------------------------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1450 DLDHQRQIVSNLEKK--QKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQlRAE 1527
Cdd:pfam05557 354 ERDGYRAILESYDKEltMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQ-QES 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1528 MEDLMSSKDDvgknVHELEKSKRTLEQQVEEMRTQLEELEDELqatEDAKLRLEVNMQAMK---------AQFDRDLQAR 1598
Cdd:pfam05557 433 LADPSYSKEE----VDSLRRKLETLELERQRLREQKNELEMEL---ERRCLQGDYDPKKTKvlhlsmnpaAEAYQQRKNQ 505
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1599 DEQGEEKKRLLVKQVREMEAELEDerkQRTLAVASKKKLEMDLNELEGQIEAANK 1653
Cdd:pfam05557 506 LEKLQAEIERLKRLLKKLEDDLEQ---VLRLPETTSTMNFKEVLDLRKELESAEL 557
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1193-1944 |
4.88e-11 |
|
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: 68.17 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1193 ELKKAIDEEtknheAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLEndnkelscdvkTLQQAKTESEhKRKKL 1272
Cdd:TIGR02169 154 ERRKIIDEI-----AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-----------RLRREREKAE-RYQAL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1273 EAQLQEFmaRATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQD-SEELRQEETRQKLNLST 1351
Cdd:TIGR02169 217 LKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1352 QIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVeltsqcleektmamD 1431
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY--------------A 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1432 KMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTisaqyaeERDRAEAEAREKDTKALsmaraleeal 1511
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR-------ELDRLQEELQRLSEELA---------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1512 eakeelerfnkQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF 1591
Cdd:TIGR02169 424 -----------DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1592 DRdLQARDEQGEEKKRLLVKQVREMEAELE------------DERKQRTLAVASKKKLEMDLNELEGQIEAA-------- 1651
Cdd:TIGR02169 493 AE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDDAVAKEAiellkrrk 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1652 ---------NKGRDEAVKQLRKLQAQMKDYQRELEE---------ARASRDEIFTQSKENEKKLKG------LEAEILQ- 1706
Cdd:TIGR02169 572 agratflplNKMRDERRDLSILSEDGVIGFAVDLVEfdpkyepafKYVFGDTLVVEDIEAARRLMGkyrmvtLEGELFEk 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1707 ---LQEDHAASERARRHAEQERDE---LADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQ 1780
Cdd:TIGR02169 652 sgaMTGGSRAPRGGILFSRSEPAElqrLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1781 VDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgTVKSKFKASIAALEAKIL-----QLEDQLEQEAKERAAA 1855
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRI 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1856 NKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTRE 1935
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
....*....
gi 1604804600 1936 VSSLKNRLR 1944
Cdd:TIGR02169 891 RDELEAQLR 899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1272 |
5.01e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 857 KPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERK-------HQQLIEEKNILAEQLHAETEL----FAEAEEMR 925
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleeleerHELYEEAKAKKEELERLKKRLtgltPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 926 VRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEakIKKMEEDILLL 1005
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAE--LKRIEKELKEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1006 EDQNSKFLKEKKLLEDRISEmTSQLTEEEEKAKNLGKVKNKQEmmMVDLEErLKKEEKTRQELEKAKRKLDAETTDLQDQ 1085
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLK--KYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1086 IVELQA---QIEELKFQLTKKEEELQAALARSDEEtlqknnALKQVRELQAHLAELqEDLESEKMCRSKAEKLKRDLSEE 1162
Cdd:PRK03918 548 LEKLEElkkKLAELEKKLDELEEELAELLKELEEL------GFESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1163 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEET-KNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNK 1241
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
410 420 430
....*....|....*....|....*....|.
gi 1604804600 1242 QSLENdNKELSCDVKTLQQAKTESEHKRKKL 1272
Cdd:PRK03918 701 EELEE-REKAKKELEKLEKALERVEELREKV 730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
867-1251 |
1.47e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.58 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 867 EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEK-----NILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHD 941
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 942 LESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1021
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1022 RISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLT 1101
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1102 KKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEK--MCRSKAEKLKRDLSEELEALKTELEDTLDTTAA 1179
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1180 QQELRSKREQEVAELKKAIDEETKnheaQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKEL 1251
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEK----KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1062-1728 |
1.95e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1062 EKTRQELEKAKRKLDAettdLQdQIVELQAQIEELKfqltkkeeeLQAALARSDEETLQKNNALKQVRELQAHLAELQED 1141
Cdd:COG4913 238 ERAHEALEDAREQIEL----LE-PIRELAERYAAAR---------ERLAELEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1142 LESEKMCRSKAEKLKRDLSEELEALK-----------TELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQ 1210
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEaqirgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1211 EMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKT----ESEHKRKKLEAQLQ--------- 1277
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGldeaelpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1278 -EFMARATEAERTKG--ELAERSHKLqteldnacTMLeVAEKKGLKLAKEVDKLNSKL----QDSEELRQEETRQKLNLS 1350
Cdd:COG4913 464 gELIEVRPEEERWRGaiERVLGGFAL--------TLL-VPPEHYAAALRWVNRLHLRGrlvyERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1351 TQIRQLEVDRNTLLEQQEEEEEARRNL-----EKQLQMVQ------------SQMFE--TKKKLEED--LGSmegleEVK 1409
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPraitragqvkgnGTRHEkdDRRRIRSRyvLGF-----DNR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1410 RKLQkdveltsqcleektmamdkmektknRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRA 1489
Cdd:COG4913 610 AKLA-------------------------ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1490 EAEARekdtkaLSmaraleealeakeelerfnkQLRAEMEDLMSSKDDVgknvhelekskRTLEQQVEEMRTQLEELEDE 1569
Cdd:COG4913 665 SAERE------IA--------------------ELEAELERLDASSDDL-----------AALEEQLEELEAELEELEEE 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1570 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAvaskkklemdlNELEGQIE 1649
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR-----------ENLEERID 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1650 AANKGRDEAVKQLRKLqaqMKDYQRELEEARASRD----------EIFTQSKENEkkLKGLEAEILQLQED--------- 1710
Cdd:COG4913 777 ALRARLNRAEEELERA---MRAFNREWPAETADLDadleslpeylALLDRLEEDG--LPEYEERFKELLNEnsiefvadl 851
|
730
....*....|....*...
gi 1604804600 1711 HAASERARRHAEQERDEL 1728
Cdd:COG4913 852 LSKLRRAIREIKERIDPL 869
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
909-1293 |
2.93e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.53 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 909 EQLHAETELFAEAEEMR-------VRLLSRKQELEEILHDLESRVEEEEERNQSLQNEK--KKMQSHIQDLEEQLDEEEA 979
Cdd:pfam17380 234 EKMERRKESFNLAEDVTtmtpeytVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 980 ARQKLQLDKVTAEAKIKKmeEDILLLEDQNSKFLKEKKL----LEDRISEMtsQLTEEEEKAKNLGKVKNKQEMMMvdle 1055
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKREL--ERIRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1056 ERLKKEEKTRQELEKAkRKLDAETTDLQDQIVELQAQIEELKFQltkKEEELQAALARSDEEtlqKNNALKQVRElqahl 1135
Cdd:pfam17380 386 ERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRAE---QEEARQREVRRLEEE---RAREMERVRL----- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1136 AELQEDLESEKMCRSKAEKLKRDLSEELEALKTELedtldttaAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQR 1215
Cdd:pfam17380 454 EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR--------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1216 Q-ATALEELSEQLEQAKRFKSNLEKNKQslendnkelscdvktLQQAKTESEHKRKKLEA--QLQEFMARATEAERTKGE 1292
Cdd:pfam17380 526 QkAIYEEERRREAEEERRKQQEMEERRR---------------IQEQMRKATEERSRLEAmeREREMMRQIVESEKARAE 590
|
.
gi 1604804600 1293 L 1293
Cdd:pfam17380 591 Y 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1053-1288 |
3.48e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1053 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAAlarsdEETLQKNNalKQVRELQ 1132
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-----EAELAELE--KEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1133 AHLAELQEDLesEKMCRSkAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEetknheaqIQEM 1212
Cdd:COG4942 97 AELEAQKEEL--AELLRA-LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--------LAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1213 RQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAER 1288
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
982-1731 |
3.66e-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: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 982 QKLQLDKVTAEAKIK----KMEEDILLLEDQNsKFLKEKKLLEDRISemtSQLTEEEEKAKNLGKVKNKQEMMMVDLEER 1057
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKVS---LKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1058 LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALaRSDEETLQknnalkqvrelqaHLAE 1137
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKL-KEDHEKIQ-------------HLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1138 lqedlESEKMCRSKAEKLKRDLSEelealKTELEDTL-DTTAAQQELRSKREQevaelkkaIDEETKNHEAQIQEMRQRQ 1216
Cdd:pfam05483 230 -----EYKKEINDKEKQVSLLLIQ-----ITEKENKMkDLTFLLEESRDKANQ--------LEEKTKLQDENLKELIEKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1217 atalEELSEQLEQAKRFKSNLEKNKQSLENDnkeLSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAER 1296
Cdd:pfam05483 292 ----DHLTKELEDIKMSLQRSMSTQKALEED---LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1297 SHKLQTELDNACTMLEVAEKKGLKLAKEVDKLnSKLQDSEELRQEETR----QKLNLSTQIRQLEVDRNTLLEQQEEEEE 1372
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVELEELKkilaEDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1373 ARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLE-EVKRKLQKDVELTSQCleektmamDKMEKTKNRLQQELDDLMVDL 1451
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLEL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1452 DHQRQIVSNLEKKQKKfdqLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDL 1531
Cdd:pfam05483 516 KKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1532 MSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVK 1611
Cdd:pfam05483 593 ENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1612 QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRdeiftqsk 1691
Cdd:pfam05483 673 LLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL-------- 744
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1604804600 1692 enEKKLKGLEAEIL----QLQEDHAASERARRHAEQERDELADE 1731
Cdd:pfam05483 745 --EIELSNIKAELLslkkQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1292-1943 |
4.08e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1292 ELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEE 1371
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1372 EARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDL 1451
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1452 DHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLraemedl 1531
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1532 msskDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAqfdRDLQARDEQGEekkrllvK 1611
Cdd:TIGR04523 270 ----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNN-------K 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1612 QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARasrdeifTQSK 1691
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE-------KLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1692 ENEKKLKGLEAEILQLqedhaaserarrhaEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLN 1771
Cdd:TIGR04523 409 QKDEQIKKLQQEKELL--------------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1772 DRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKsKFKASIAALEAKILQLEDQLEqeake 1851
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELN----- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1852 raaaNKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEG 1931
Cdd:TIGR04523 549 ----KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
650
....*....|..
gi 1604804600 1932 LTREVSSLKNRL 1943
Cdd:TIGR04523 625 ENEKLSSIIKNI 636
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1523-1945 |
5.19e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1523 QLRAEMEDLMSSKDDVGKnvheLEKSKRTLEQqVEEMRTQLEELEDELQATEDAKLRLEVnmqAMKAQFDRDLQARDEQG 1602
Cdd:COG4913 229 ALVEHFDDLERAHEALED----AREQIELLEP-IRELAERYAAARERLAELEYLRAALRL---WFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1603 EEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMD-LNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARA 1681
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1682 SRDEIFTQSKENEKKLKGLEAEilqLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELE 1761
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1762 EE-----------------QGNME-LLND----------------------------RFRKSNIQVDNLNTELAGERSAA 1795
Cdd:COG4913 458 AElpfvgelievrpeeerwRGAIErVLGGfaltllvppehyaaalrwvnrlhlrgrlVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1796 QK--------SENARQQMERQNKDLKAKLAE----------LEGTVKSKF---------------------KASIAALEA 1836
Cdd:COG4913 538 GKldfkphpfRAWLEAELGRRFDYVCVDSPEelrrhpraitRAGQVKGNGtrhekddrrrirsryvlgfdnRAKLAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1837 KILQLEDQLEQEAKERAAANKIVRRTEK------KLKEV------MMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEA 1904
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQErrealqRLAEYswdeidVASAEREIAELEAELERLDASSDDLAALEEQLEEL 697
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1604804600 1905 EEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
896-1277 |
6.30e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.37 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 896 KHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEIlhdlESRVEEEEERNQSLQNEKKKMqshiqdleeqld 975
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAIYAEQERM------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 976 eeeAARQKLQLDKVTAEAKIKKMEEdillledqnskflkekklledrisemtsqlTEEEEKAKNLGKVKNKQEMMMvdle 1055
Cdd:pfam17380 343 ---AMERERELERIRQEERKRELER------------------------------IRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1056 ERLKKEEKTRQELEkAKRKLDAETTDLQDQIVELQAQIEELKF--------QLTKKEEELQAALARSDEETLQKNNALKQ 1127
Cdd:pfam17380 386 ERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAeqeearqrEVRRLEEERAREMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1128 VRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEElealktELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEA 1207
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1208 QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLEndnkelscdvktLQQAKTESEHKRKKLEAQLQ 1277
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE------------MMRQIVESEKARAEYEATTP 596
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1001-1485 |
7.65e-10 |
|
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: 63.82 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1001 DILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETT 1080
Cdd:COG5185 135 DELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGN 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1081 DLQDQIVELQAQIEEL------KFQLTKKEEELQAALARSDEETLQKNNALKQVRelqahLAELQEDLESEKMCRSKAEK 1154
Cdd:COG5185 215 LGSESTLLEKAKEIINieealkGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEK-----LGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1155 LKRDLSEELEALKTELEDTLDTTAAQQELRSKR-EQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQaKRF 1233
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEaEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIEN-IVG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1234 KSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLqefmarateaERTKGELAERSHKLQTELDNACTMLEV 1313
Cdd:COG5185 369 EVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATL----------EDTLKAADRQIEELQRQIEQATSSNEE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1314 AEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQirqlevdrntlleqqeeeeEARRNLEKQLQMVQSQMFETKK 1393
Cdd:COG5185 439 VSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVR-------------------SKKEDLNEELTQIESRVSTLKA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1394 KLEEDLGSMEG-LEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL 1472
Cdd:COG5185 500 TLEKLRAKLERqLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLST 579
|
490
....*....|...
gi 1604804600 1473 AEEKTISAQYAEE 1485
Cdd:COG5185 580 IESQQAREDPIPD 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1630-1856 |
1.13e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1630 AVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQE 1709
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1710 DHAASER--ARRHAEQERDELADEISNSASGKSSLLEEKRR--LEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLN 1785
Cdd:COG4942 98 ELEAQKEelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1786 TELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEAKERAAAN 1856
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1083-1307 |
1.58e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1083 QDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEE 1162
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1163 LEALKTELEDTLDttAAQqelRSKREQEVAELKKAIDEETKNHEAQ-IQEMRQRQATALEELSEQLEQAKRFKSNLEKNK 1241
Cdd:COG4942 99 LEAQKEELAELLR--ALY---RLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1242 QSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNA 1307
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1052-1393 |
3.19e-09 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 61.66 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1052 VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQ-AQIEELKFQltkkeeelQAALARSDEETLQKNNALKQVR- 1129
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlAKEEDLKRQ--------NAVLQEAQVELDALQNQLALARa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1130 --ELQAHLAELQEDLESEKMcrskaEKLKRDLSEELEALKTELEDTLDTTAAQQELRskREQEVAELkkaiDEETKNHEA 1207
Cdd:pfam03528 76 emENIKAVATVSENTKQEAI-----DEVKSQWQEEVASLQAIMKETVREYEVQFHRR--LEQERAQW----NQYRESAER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1208 QIQEMRQRQATALEElsEQLE-QAKRFKSNLEKNKQSLENDNKELScdvkTLQQAKTESEHKRKKLEAQLQEFMARATEA 1286
Cdd:pfam03528 145 EIADLRRRLSEGQEE--ENLEdEMKKAQEDAEKLRSVVMPMEKEIA----ALKAKLTEAEDKIKELEASKMKELNHYLEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1287 ERT---------------KGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEEL-RQEETRQKLNLS 1350
Cdd:pfam03528 219 EKScrtdlemyvavlntqKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLlMRDMQRMESVLT 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1604804600 1351 T-QIRQLEVdrntlLEQQEEEEEARRNLEKQLQMVQSQMFETKK 1393
Cdd:pfam03528 299 SeQLRQVEE-----IKKKDQEEHKRARTHKEKETLKSDREHTVS 337
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
861-1478 |
4.82e-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: 61.62 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 861 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQL---IEEKNILAEQLHAE--------TELFAEAEEM----- 924
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLTEEyaelkeelEDLRAELEEVdkefa 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 925 --RVRLLSRKQELEEILHDLESrveeeEERNQS-LQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEED 1001
Cdd:TIGR02169 382 etRDELKDYREKLEKLKREINE-----LKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1002 ILLLEDQNSKFLKEK-------KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRK 1074
Cdd:TIGR02169 457 LEQLAADLSKYEQELydlkeeyDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1075 LD-----AETTDLQDQIVE----LQAQIEELK----------------------------------FQLTKKEEELQAAL 1111
Cdd:TIGR02169 537 YAtaievAAGNRLNNVVVEddavAKEAIELLKrrkagratflplnkmrderrdlsilsedgvigfaVDLVEFDPKYEPAF 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1112 ARSDEETLQKNNaLKQVREL--QAHLAELQEDL--ESEKM-----CRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1182
Cdd:TIGR02169 617 KYVFGDTLVVED-IEAARRLmgKYRMVTLEGELfeKSGAMtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1183 LRSKREQEVAELKKAIDEETKNHEA------QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVK 1256
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1257 TLQQAKT------------ESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKE 1324
Cdd:TIGR02169 776 KLEEALNdlearlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1325 VDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEG 1404
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 1405 LEEVKRKLQKDVeltsqcleEKTMAMDKMEKTKNRLQQELDDL----MVDLDHQRQIVSNLEKKQKKFDQLLAEEKTI 1478
Cdd:TIGR02169 936 IEDPKGEDEEIP--------EEELSLEDVQAELQRVEEEIRALepvnMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1090-1884 |
5.27e-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: 61.52 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1090 QAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTE 1169
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1170 LEDTLDTTA----------AQQELRSKREQE----VAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKS 1235
Cdd:TIGR00618 231 LREALQQTQqshayltqkrEAQEEQLKKQQLlkqlRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1236 NLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQE--FMARATEAERTKGELAERSHKLQTELDNACTMLEV 1313
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1314 AEKKGLKLAKEVDKLNSKL--QDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEarrNLEKQLQMVQSQMFET 1391
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQatIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA---QCEKLEKIHLQESAQS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1392 KKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKtknrlqqELDDLMVDLDHQRQIVSNLEKKQKKFDQL 1471
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI-------HPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1472 LAEEKTISAQYAEERDRA---EAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHElEKS 1548
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRaslKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA-LLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1549 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQamkaqfdrdlqardeqgEEKKRLLVKQVREMEAELEDERKQRT 1628
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT-----------------QERVREHALSIRVLPKELLASRQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1629 LAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSkenEKKLKGLEAEILQLQ 1708
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS---LKELMHQARTVLKAR 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1709 E-DHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNL--- 1784
Cdd:TIGR00618 760 TeAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRlee 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1785 NTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLeqeakeraAANKIVRRTEK 1864
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEI--------TLYANVRLANQ 911
|
810 820
....*....|....*....|
gi 1604804600 1865 KLKEVMMQVEDERRHADQYK 1884
Cdd:TIGR00618 912 SEGRFHGRYADSHVNARKYQ 931
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1650-1880 |
7.38e-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: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1650 AANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELa 1729
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1730 deisnsasgKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQN 1809
Cdd:COG4942 96 ---------RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1810 KDLKAKLAELEGTVKS--KFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHA 1880
Cdd:COG4942 167 AELEAERAELEALLAEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1034-1483 |
9.41e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1034 EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALAR 1113
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1114 SDEETLQK--NNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEV 1191
Cdd:COG4717 132 QELEALEAelAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1192 AELKKAIDEETKNHEAQIQEMRQRQATalEELSEQLEQAKR----------FKSNLEKNKQSLENDNKELSCDVKTLQQA 1261
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEA--AALEERLKEARLllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1262 KTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQE 1341
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1342 ETRQKLNLSTQIRQLEVdrntlLEQQEEEEEARRNLEKQLQMVQSQMfETKKKLEEDLGSMEGLEEVKRKLQKdvelTSQ 1421
Cdd:COG4717 370 QEIAALLAEAGVEDEEE-----LRAALEQAEEYQELKEELEELEEQL-EELLGELEELLEALDEEELEEELEE----LEE 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1422 CLEEKTMAMDKMEKTKNRLQQELDDLMVDldhqrqivSNLEKKQKKFDQLLAEEKTISAQYA 1483
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEED--------GELAELLQELEELKAELRELAEEWA 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1522-1714 |
1.02e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1522 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ 1601
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1602 GEEKKRLLV------------------------KQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDE 1657
Cdd:COG4942 117 GRQPPLALLlspedfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1658 AVKQLRKLQAQMKDYQRELEEARASRDEIftqskenEKKLKGLEAEILQLQEDHAAS 1714
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
866-1184 |
1.32e-08 |
|
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: 60.47 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 866 EEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEM----RVRLLSRK--------Q 933
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsRIPEIQAElskleeevS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 934 ELEEILHDLESRVeeeeernqslqnekkkmqshiqdleeqldeeeaarQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFL 1013
Cdd:TIGR02169 809 RIEARLREIEQKL-----------------------------------NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 KEKKLLEDRISEMTSQLTEEEEKAKnlgkvknkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1093
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALR--------------DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EELKFQLTKKEEELqAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKA-----EKLKR--DLSEELEAL 1166
Cdd:TIGR02169 920 SELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAiqeyeEVLKRldELKEKRAKL 998
|
330
....*....|....*...
gi 1604804600 1167 KTELEDTLDTTAAQQELR 1184
Cdd:TIGR02169 999 EEERKAILERIEEYEKKK 1016
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1374-1702 |
1.49e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1374 RRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCL-EEKTMAMDKmEKTKNRLQQelddlmvdld 1452
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYaEQERMAMER-ERELERIRQ---------- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1453 hqrqivsnlEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLM 1532
Cdd:pfam17380 356 ---------EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1533 SSKDDVGKnvhelEKSKRTLEQQVEEM-RTQLEELEDELQATedaKLRL-EVNMQAMKAQFDRDLQARDEQGEEKKRLLV 1610
Cdd:pfam17380 427 AEQEEARQ-----REVRRLEEERAREMeRVRLEEQERQQQVE---RLRQqEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1611 KQVRE-MEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMK--DYQRELEEARASRDEIF 1687
Cdd:pfam17380 499 KELEErKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMM 578
|
330
....*....|....*
gi 1604804600 1688 TQSKENEKKLKGLEA 1702
Cdd:pfam17380 579 RQIVESEKARAEYEA 593
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1051-1753 |
1.50e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1051 MVDLEERLKKEEKT---RQELEKAKRKLDAEttdlQDQIVELQAQIEELKFQLTKKEEELQAALARsdeetLQK-NNAL- 1125
Cdd:PRK04863 275 MRHANERRVHLEEAlelRRELYTSRRQLAAE----QYRLVEMARELAELNEAESDLEQDYQAASDH-----LNLvQTALr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1126 --KQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEA-------LKTELEDTLDTTAAQQELRSKREQEVAELKK 1196
Cdd:PRK04863 346 qqEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAaeeevdeLKSQLADYQQALDVQQTRAIQYQQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1197 A------IDEETKNHEAQIQEMR---QRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEH 1267
Cdd:PRK04863 426 AkqlcglPDLTADNAEDWLEEFQakeQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1268 KRKKLEA-QLQEFMARATEAERTKGE-------LAERSHKLQTELDNActmlEVAEKKGLKLAKEVDKLNSKLQDSEELR 1339
Cdd:PRK04863 506 REQRHLAeQLQQLRMRLSELEQRLRQqqraerlLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1340 QEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQL---QMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDV 1416
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFedsQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1417 ELTSQcleEKTMAMDKMEKTKNRLQQEL-----DDLMVD--------LDHQRQ--IVSNLEKKQkkfDQLLAEEKTISAQ 1481
Cdd:PRK04863 662 ERLSQ---PGGSEDPRLNALAERFGGVLlseiyDDVSLEdapyfsalYGPARHaiVVPDLSDAA---EQLAGLEDCPEDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1482 Y---------------AEERDRAEA---------------------EAREKDTKAL-----SMARALEEALEAKEELERF 1520
Cdd:PRK04863 736 YliegdpdsfddsvfsVEELEKAVVvkiadrqwrysrfpevplfgrAAREKRIEQLraereELAERYATLSFDVQKLQRL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1521 NKQLR----------------AEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQL--------------------- 1563
Cdd:PRK04863 816 HQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladetladr 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1564 -EELEDELQATEDAKL-------------RLEVNMQAMKAQFDRdLQARDEQGEEKKRLL------VKQVREMEAELEDE 1623
Cdd:PRK04863 896 vEEIREQLDEAEEAKRfvqqhgnalaqlePIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAkqqafaLTEVVQRRAHFSYE 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1624 RKQRTLAVASkkklemDLNE-LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLkglea 1702
Cdd:PRK04863 975 DAAEMLAKNS------DLNEkLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL----- 1043
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1703 EILQLQEDHAASERARRHaeqeRDELADEISNSASGKSSLLEEKRRLEARI 1753
Cdd:PRK04863 1044 QDLGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
861-1611 |
1.83e-08 |
|
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: 59.75 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 861 QVTRQEEELQAKDEELVKVKERQLKVEN-ELVEMERKHQQLIEEKNILAEQLHA--------ETELFAEAEEMRvRLLSR 931
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANsELTEARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQNK-RLWDR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 932 KQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDeeeaarqklqldkvtaeAKIKKMEEDILLLEDQNSK 1011
Cdd:pfam15921 407 DTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQM-----------------AAIQGKNESLEKVSSLTAQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1012 FLKEKKLLEDRISEMTSQLTEEEEKAKNLGKvknkqemMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ------DQ 1085
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSD-------LTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1086 IVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKM--CRSKAEKLKRDLS-EE 1162
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLelQEFKILKDKKDAKiRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1163 LEALKT--ELEDTLDTTAAQQELRS------KREQEVAELKKA---IDEETKNHEAQIQEMRQRqATALEELSEQLE-QA 1230
Cdd:pfam15921 623 LEARVSdlELEKVKLVNAGSERLRAvkdikqERDQLLNEVKTSrneLNSLSEDYEVLKRNFRNK-SEEMETTTNKLKmQL 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1231 KRFKSNLEKNKQSLENDNKELSCDVKT---LQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNA 1307
Cdd:pfam15921 702 KSAQSELEQTRNTLKSMEGSDGHAMKVamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1308 CT-------MLEVAEKKGLKLAKEV-------DKLNSKLQDSEEL----RQEETRQKLNLSTQIRQLE---VDRNTLLEQ 1366
Cdd:pfam15921 782 ATeknkmagELEVLRSQERRLKEKVanmevalDKASLQFAECQDIiqrqEQESVRLKLQHTLDVKELQgpgYTSNSSMKP 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1367 QEEEEEARRNLEKQLQMVQSQM-FETKKKLEEDLGSMEGLEEVKRKLQkdvELTSQCLEEKTMAMDKME-KTKNRLQQEL 1444
Cdd:pfam15921 862 RLLQPASFTRTHSNVPSSQSTAsFLSHHSRKTNALKEDPTRDLKQLLQ---ELRSVINEEPTVQLSKAEdKGRAPSLGAL 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1445 DDLMVDLDHQRQIVSNLEKKQKKFdqLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQL 1524
Cdd:pfam15921 939 DDRVRDCIIESSLRSDICHSSSNS--LQTEGSKSSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPK 1016
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1525 RAEMEDLMSS--KDDVG--------KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdRD 1594
Cdd:pfam15921 1017 KSPVHSLLTSsaEGSIGsssqyrsaKTIHSPDSVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMI-RN 1095
|
810
....*....|....*..
gi 1604804600 1595 LQARDEQGEEKKRLLVK 1611
Cdd:pfam15921 1096 QEKRIQKVKDQEKMLLK 1112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1124-1337 |
1.87e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1124 ALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETK 1203
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1204 NHEAQIQEMRQR--------QATALEEL--SEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLE 1273
Cdd:COG4942 98 ELEAQKEELAELlralyrlgRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1274 AQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEE 1337
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1066-1309 |
1.90e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1066 QELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEetlqknnALKQVRELQAHLAELQEDLESe 1145
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-------LQAEIAEAEAEIEERREELGE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1146 kmcRSKAEKLKRDLSEELEALK--TELEDTLDTTAAQQELRSKREQEVAELKKAIdEETKNHEAQIQEMRQRQATALEEL 1223
Cdd:COG3883 91 ---RARALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1224 SEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTE 1303
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
....*.
gi 1604804600 1304 LDNACT 1309
Cdd:COG3883 247 AGAGAA 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1671-1945 |
2.09e-08 |
|
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: 59.70 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1671 DYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSasgKSSLLEEKRRLE 1750
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE---KEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1751 ARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSaaqksenarqqmERQNKdLKAKLAELEgtvkskfkAS 1830
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLR-VKEKIGELE--------AE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1831 IAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR 1910
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270
....*....|....*....|....*....|....*
gi 1604804600 1911 ANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
868-1285 |
2.17e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.35 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 868 ELQAKDEELvkvKERQLKVENELVEMERKHQQLIEEKNILAEQLHAET---ELFAEAEEMRVRLLSRKQELeeilHDLES 944
Cdd:pfam05483 385 ELQKKSSEL---EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKiaeELKGKEQELIFLLQAREKEI----HDLEI 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 945 RVEEEEERNQSLQNEKKKMQSHIQDLeeqldeeeaarqklqldkvtaeaKIKKMEedillLEDQNSKFLKEKKLLEDRIS 1024
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDLKTELEKE-----------------------KLKNIE-----LTAHCDKLLLENKELTQEAS 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1025 EMTSQLTEEEEKAKNlgkVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKE 1104
Cdd:pfam05483 510 DMTLELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1105 EELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1184
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1185 SKREQ--------------EVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKN----KQSLEN 1246
Cdd:pfam05483 667 KISEEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEqssaKAALEI 746
|
410 420 430
....*....|....*....|....*....|....*....
gi 1604804600 1247 DNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATE 1285
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1255-1725 |
2.19e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1255 VKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQD 1334
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1335 SEELRQ-EETRQKLN-LSTQIRQLEvdrntlleqqeEEEEARRNLEKQLQMVQSQMFETKKKLEEDLgsmeglEEVKRKL 1412
Cdd:COG4717 128 LPLYQElEALEAELAeLPERLEELE-----------ERLEELRELEEELEELEAELAELQEELEELL------EQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1413 QKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDH--QRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAE 1490
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1491 AEAREKDTKALSMA----------RALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMR 1560
Cdd:COG4717 271 LILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1561 TQLEELEDELQ--ATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLvKQVREMEAELEDERK--QRTLAVASKKK 1636
Cdd:COG4717 351 ELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGelEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1637 LEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDY--QRELEEARASRDEIftqskenEKKLKGLEAEILQLQEDHAAS 1714
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL-------KAELRELAEEWAALKLALELL 502
|
490
....*....|.
gi 1604804600 1715 ERARRHAEQER 1725
Cdd:COG4717 503 EEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
993-1398 |
2.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 993 AKIKKMEEDILLLEDQNSKFLKekklLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMmVDLEERLKKEEKTRQELEKAK 1072
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1073 RKLDAETTDLQdQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQK-NNALKQVRELQAHLAELQEDLEsekmcrsk 1151
Cdd:COG4717 146 ERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELE-------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1152 aeklkrDLSEELEALKTELEDTLDTTAAQQELRSKREQE---------------------------------VAELKKAI 1198
Cdd:COG4717 217 ------EAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1199 DEETKNHEAQIQEMRQRQATALEELSEQLEQaKRFKSNLEKNKQSLENDNKELSCDVKTLQQA-----KTESEHKRKKLE 1273
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEEL-EELLAALGLPPDLSPEELLELLDRIEELQELlreaeELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1274 AQLQEFMARAT---------------EAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKlaKEVDKLNSKLQDSEEL 1338
Cdd:COG4717 370 QEIAALLAEAGvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEE 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1339 RQEETRQKLNLSTQIRQLEVDRN--TLLEQQEEEEEARRNLEKQ---LQMVQSQMFETKKKLEED 1398
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEwaaLKLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1083-1307 |
2.94e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1083 QDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLEsekmcrskaeklkrDLSEE 1162
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1163 LEALKTELEDTLdtTAAQQELRSKREQEVAELKKAIDEETKNHEAqIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQ 1242
Cdd:COG3883 81 IEERREELGERA--RALYRSGGSVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1243 SLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNA 1307
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1119-1776 |
3.51e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1119 LQKNNALKQVRELQAHLAEL---QEDLEsekmcrsKAEKlKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1195
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLeraHEALE-------DARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1196 kaiDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKE-LSCDVKTLQQAKTESEHKRKKLEA 1274
Cdd:COG4913 290 ---LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1275 QLQEFmarATEAERTKGELAERSHKLQTELDnactmlevaekkglKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIR 1354
Cdd:COG4913 367 LLAAL---GLPLPASAEEFAALRAEAAALLE--------------ALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1355 QLEVDRNTLleqQEEEEEARRNLEKQLQMVQSQM------FETKKKLEEDLGSMEG-LEEVKRKLQKDVELTSQcleekt 1427
Cdd:COG4913 430 SLERRKSNI---PARLLALRDALAEALGLDEAELpfvgelIEVRPEEERWRGAIERvLGGFALTLLVPPEHYAA------ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1428 mAMDKMEKTKNRLQqelddlmVDLDHQRQIVSNLEKKQKKFDQLLAEEKT--------ISAQYAEERDRAEAEarekDTK 1499
Cdd:COG4913 501 -ALRWVNRLHLRGR-------LVYERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAELGRRFDYVCVD----SPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1500 ALSMARaleealeakeelerfnkqlRAEMEDLMSSKddvGKNVHELEKSKRTLEQQV--EEMRTQLEELEDELQATEDAK 1577
Cdd:COG4913 569 ELRRHP-------------------RAITRAGQVKG---NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEEL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1578 LRLEVNMQAMKAQFDRDlqardeqgeEKKRLLVKQVREMEAELEDerkqrtlaVASkkkLEMDLNELEGQIEAANKGRDE 1657
Cdd:COG4913 627 AEAEERLEALEAELDAL---------QERREALQRLAEYSWDEID--------VAS---AEREIAELEAELERLDASSDD 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1658 avkqLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHaasERARRHAEQERDELADEISNSAS 1737
Cdd:COG4913 687 ----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAAL 759
|
650 660 670
....*....|....*....|....*....|....*....
gi 1604804600 1738 GKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRK 1776
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1054-1496 |
3.74e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1054 LEERLKKEektRQELEKAKRKLDaetTDLQDQIVELQAQIEELKfqltKKEEELQAALARSDEETLQKNNALKQVRELQA 1133
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1134 HLAELqEDLESEKMCRSKAEKLKRDLSEELEALKtELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMR 1213
Cdd:COG4717 117 ELEKL-EKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1214 QRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscdvktlqQAKTESEHKRKKLEAQLQEFMARATEAERTkGEL 1293
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLLIAAALLALL-GLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1294 AERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNT----------L 1363
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLspeellelldR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1364 LEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQcLEEKTMAMDKMEKTKNRLQQE 1443
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1444 LDDLMVDLDHQrQIVSNLEKKQKKFDQLLAEEKTISAQYAE-ERDRAEAEAREK 1496
Cdd:COG4717 425 LDEEELEEELE-ELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQE 477
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1154-1921 |
4.20e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.90 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1154 KLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAiDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRF 1233
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1234 KSnLEKNKQSLENDNKELSCDVKTLQQAKTEsehkrkkleaQLQEFMARATEAERTKGELAERSHKlQTELDNACTMLEV 1313
Cdd:TIGR00606 272 KA-LKSRKKQMEKDNSELELKMEKVFQGTDE----------QLNDLYHNHQRTVREKERELVDCQR-ELEKLNKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1314 AEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKK 1393
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1394 KLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK--FDQL 1471
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNslTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1472 LAEEKTISAQYAE--ERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSK 1549
Cdd:TIGR00606 500 KKEVKSLQNEKADldRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1550 RTLEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQgeekkrllvkqvremEAELEDerkqRTL 1629
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ---------------LSSYED----KLF 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1630 AVASKKKLEMDLNELEGQIEAANKgrdeavkQLRKLQAQMKDYQRELEEARASR-------DEIFTQSKENEKKLKGLEA 1702
Cdd:TIGR00606 630 DVCGSQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQS 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1703 EILQLQEDHAASERARRHAEQERDEL-------ADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFR 1775
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1776 KSNI-QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASiaaleAKILQLEDQLEQEAKERAA 1854
Cdd:TIGR00606 783 SAKVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEL-----DTVVSKIELNRKLIQDQQE 857
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1855 ANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRE 1921
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1005-1231 |
4.64e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1005 LEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLgkvknKQEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQD 1084
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELE-------SQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1085 QIVELQAQIEELKFQLTKKEEELQAALARSDEETLqknnaLKQVRELQAHLAELQEDLESE----KMCRSKAEKLKRDLS 1160
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL-----RAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1161 EELEALKTELEDTLDTTAAQ-QELRskreQEVAELKKAIDEETKNhEAQIQEMRQRQATA---LEELSEQLEQAK 1231
Cdd:COG3206 309 QEAQRILASLEAELEALQAReASLQ----AQLAQLEARLAELPEL-EAELRRLEREVEVArelYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1054-1600 |
5.55e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1054 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQ--------IEELKFQLTKKEEELQAALARSD--EETLQK-- 1121
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRArlEALLAAlg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1122 ---NNALKQVRELQAHLAELQEDLESEkmcRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAI 1198
Cdd:COG4913 373 lplPASAEEFAALRAEAAALLEALEEE---LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1199 DEETKNHEAQIQ------EMRQRQA---TALEEL-----------SEQLEQAKRFksnLEKNKQSLENDNKELSCDVKTL 1258
Cdd:COG4913 450 AEALGLDEAELPfvgeliEVRPEEErwrGAIERVlggfaltllvpPEHYAAALRW---VNRLHLRGRLVYERVRTGLPDP 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1259 QQAKTES----------EHK-RKKLEAQLQEFMARA---------------TEAERTKGELAERSHKLQTELD------- 1305
Cdd:COG4913 527 ERPRLDPdslagkldfkPHPfRAWLEAELGRRFDYVcvdspeelrrhpraiTRAGQVKGNGTRHEKDDRRRIRsryvlgf 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1306 NACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTlleqqEEEEEARRNLEKQLQmvq 1385
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----ASAEREIAELEAELE--- 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1386 sqmfetkkKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK- 1464
Cdd:COG4913 679 --------RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAl 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1465 -QKKFDQLLAE--EKTISAQYAEERDRAEAEAREKDTKALSMARaleealeakeeleRFNKQLRAEMEDLMSSKDDVGkn 1541
Cdd:COG4913 751 lEERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMR-------------AFNREWPAETADLDADLESLP-- 815
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1542 vhelekskrtleqQVEEMRTQLEelEDEL-QATEDAKLRLEVNMQAMKAQFDRDL-QARDE 1600
Cdd:COG4913 816 -------------EYLALLDRLE--EDGLpEYEERFKELLNENSIEFVADLLSKLrRAIRE 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1373-1626 |
5.72e-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: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1373 ARRNLEKQLQMVQSQMFETKKKLEEdlgsmegLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLmvdld 1452
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1453 hqrqivsnlekkQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLM 1532
Cdd:COG4942 89 ------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1533 SSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLvKQ 1612
Cdd:COG4942 157 ADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-AL 228
|
250
....*....|....
gi 1604804600 1613 VREMEAELEDERKQ 1626
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1438-1945 |
8.25e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1438 NRLQQELDDL------MVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAqyaeERDRAEAEAREKDTKALSMARAleeal 1511
Cdd:COG4913 228 DALVEHFDDLeraheaLEDAREQIELLEPIRELAERYAAARERLAELEY----LRAALRLWFAQRRLELLEAELE----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1512 eakeelerfnkQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQ-LEELEDELQATEDAKLRLEVNMQAMKAQ 1590
Cdd:COG4913 299 -----------ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1591 FdRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQrtlavaskkkLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMK 1670
Cdd:COG4913 368 L-AALGLPLPASAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1671 DYQRELEEARasrDEIFTQSKENEKKLKGLeAEILQLQEDHA----ASER------------------ARRHAEQERDEL 1728
Cdd:COG4913 437 NIPARLLALR---DALAEALGLDEAELPFV-GELIEVRPEEErwrgAIERvlggfaltllvppehyaaALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1729 ----------ADEISNSASGKSSLLEE--------KRRLEARIAQLEEELE--------------EEQGNMELLNDRFRK 1776
Cdd:COG4913 513 rlvyervrtgLPDPERPRLDPDSLAGKldfkphpfRAWLEAELGRRFDYVCvdspeelrrhpraiTRAGQVKGNGTRHEK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1777 --------------SNI-QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKF-KASIAALEAKILQ 1840
Cdd:COG4913 593 ddrrrirsryvlgfDNRaKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1841 LEDQLEQEAkeraAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRR---- 1916
Cdd:COG4913 673 LEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelr 748
|
570 580 590
....*....|....*....|....*....|....*.
gi 1604804600 1917 -----KLQRELDDATEA--SEGLTREVSSLKNRLRR 1945
Cdd:COG4913 749 alleeRFAAALGDAVERelRENLEERIDALRARLNR 784
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1521-1945 |
9.72e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1521 NKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFD-RDLQARD 1599
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1600 EQGEEKkrllVKQVREMEAELED-ERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEE 1678
Cdd:COG4717 149 EELEER----LEELRELEEELEElEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1679 ARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDE-----LADEISNSASGKSSLLEEKRRLEARI 1753
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1754 AQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKakLAELEGTVKSKFKASIAA 1833
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1834 LEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVmmqvedERRHADQYKEQMEKansRMKQLKRQLEEAEEEATRANA 1913
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGEL------EELLEALDEEELEE---ELEELEEELEELEEELEELRE 453
|
410 420 430
....*....|....*....|....*....|....
gi 1604804600 1914 TRRKLQRELDDATEASE--GLTREVSSLKNRLRR 1945
Cdd:COG4717 454 ELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
864-1447 |
1.12e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.16 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 864 RQEEELQAKDEELVKVKER---QLKVENELVEMERKHQQLIEEKNILAEQLHAETelFAEAEEMRVRLLSRKQELEEILH 940
Cdd:pfam12128 287 ELNQLLRTLDDQWKEKRDElngELSAADAAVAKDRSELEALEDQHGAFLDADIET--AAADQEQLPSWQSELENLEERLK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 941 DLESRVEEEEERNQSLqnEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDI-LLLEDQNSKFLKEKKLL 1019
Cdd:pfam12128 365 ALTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1020 EDRISEMTSQL---TEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD---QIVELQAQI 1093
Cdd:pfam12128 443 KSRLGELKLRLnqaTATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSAL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EELKFQLTKKEEEL--------------------QAALARSD----------------------EETLQKNNALKQVREL 1131
Cdd:pfam12128 523 DELELQLFPQAGTLlhflrkeapdweqsigkvisPELLHRTDldpevwdgsvggelnlygvkldLKRIDVPEWAASEEEL 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1132 QAHLAELQEDLESEK-----------MCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDE 1200
Cdd:pfam12128 603 RERLDKAEEALQSARekqaaaeeqlvQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1201 ETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKsnleknkqslendnkelscdvktlQQAKTESEHKRKKLEAQLQEfm 1280
Cdd:pfam12128 683 RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK------------------------QAYWQVVEGALDAQLALLKA-- 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1281 arATEAERTkgELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETR-----------QKLNL 1349
Cdd:pfam12128 737 --AIAARRS--GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRL 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1350 STQIRQLEVD----RNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVK-----RKLQKDVELTS 1420
Cdd:pfam12128 813 ATQLSNIERAiselQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERL 892
|
650 660
....*....|....*....|....*..
gi 1604804600 1421 QCLEEktmAMDKMEKTKNRLQQELDDL 1447
Cdd:pfam12128 893 AQLED---LKLKRDYLSESVKKYVEHF 916
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
824-1447 |
1.13e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.36 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 824 KQQQLSALKVLQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERK---HQQL 900
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 901 IEEKNILAEQLHAETELFAEAEEMrvrllsrkqelEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAA 980
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEM-----------EQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 981 RQKLQLDKV--TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNkQEMMMVDLEERL 1058
Cdd:TIGR00606 570 PNKKQLEDWlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEEI 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1059 KKEEKTRQELE----------------------------KAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAA 1110
Cdd:TIGR00606 649 EKSSKQRAMLAgatavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1111 LARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRS---KR 1187
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKI 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1188 EQEVAELKKAIDEETKNheaQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEH 1267
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQ---QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1268 KRKKLEAQLQEFMARATEAERTKGE---LAERSHKLQTE----LDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQ 1340
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1341 EETRQklnlstQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQsQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTS 1420
Cdd:TIGR00606 966 DGKDD------YLKQKETELNTVNAQLEECEKHQEKINEDMRLMR-QDIDTQKIQERWLQDNLTLRKRENELKEVEEELK 1038
|
650 660
....*....|....*....|....*...
gi 1604804600 1421 QCLEE-KTMAMDKMEKTKNRLQQELDDL 1447
Cdd:TIGR00606 1039 QHLKEmGQMQVLQMKQEHQKLEENIDLI 1066
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1082-1868 |
1.21e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1082 LQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVREL-QAHLAELQE-DLESEKMCRSKAEKLK--R 1157
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEEIQenK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1158 DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQI---QEMRQRQATALEELSEQLEQAKRFK 1234
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMIlafEELRVQAENARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1235 SNLEKNKQSLENDNKElscDVKTLQQAKTESEHKRKKLEAQLQEfmarateaERTKGELAERSHKLQTEldnacTMLEVA 1314
Cdd:pfam05483 225 QHLEEEYKKEINDKEK---QVSLLLIQITEKENKMKDLTFLLEE--------SRDKANQLEEKTKLQDE-----NLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1315 EKKGlKLAKEVDKLNSKLQDSEElRQEETRQKLNLSTQ-IRQLEVDRNTLLEQQEEEEEARrnlekqlQMVQSQMFETKK 1393
Cdd:pfam05483 289 EKKD-HLTKELEDIKMSLQRSMS-TQKALEEDLQIATKtICQLTEEKEAQMEELNKAKAAH-------SFVVTEFEATTC 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1394 KLEEDLGSMEGLEEvkrKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLA 1473
Cdd:pfam05483 360 SLEELLRTEQQRLE---KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1474 EEKTISAQYaeerdraeaEAREKDTKALSMarALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLE 1553
Cdd:pfam05483 437 KEQELIFLL---------QAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1554 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfDRDLQARDEqgeekkrllVKQVREMEAELEDERKQRTlavas 1633
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDE---------LESVREEFIQKGDEVKCKL----- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1634 kKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAA 1713
Cdd:pfam05483 569 -DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1714 serARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNME--------LLNDRFRKSNIQVDNLN 1785
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvaLMEKHKHQYDKIIEERD 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1786 TELAGERSAAQKSENARQQMERQNKDLKAKLaelegtvkskfkasiaaleakiLQLEDQLEQEAKERAAANKIVRRTEKK 1865
Cdd:pfam05483 725 SELGLYKNKEQEQSSAKAALEIELSNIKAEL----------------------LSLKKQLEIEKEEKEKLKMEAKENTAI 782
|
...
gi 1604804600 1866 LKE 1868
Cdd:pfam05483 783 LKD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1075-1303 |
1.27e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1075 LDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETL--QKNNALKQVRELQAHLAELQEDLESEkmcRSKA 1152
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEA---EARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1153 EKLKRDLSEELEALKTELEDtldttAAQQELRSKREQEVAELKKAIDEETKNHEaQIQEMRQRQATALEELSEQLEQAKr 1232
Cdd:COG3206 243 AALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHP-DVIALRAQIAALRAQLQQEAQRIL- 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1233 fksnleknkQSLENDNKELSCDVKTLQQAKTESEHKRKKL---EAQLQEFMARATEAERTKGELAERSHKLQTE 1303
Cdd:COG3206 316 ---------ASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1644-1896 |
1.28e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1644 LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFT--QSKENEKKLKGLEAEILQLQEDHAASERARRHA 1721
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1722 EQERDELADEISN--SASGKSSLLEEKRRLEARIAQleeeleeeqgnmelLNDRFRKSNIQVDNLNTELAgersaaqkse 1799
Cdd:COG3206 246 RAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE--------------LSARYTPNHPDVIALRAQIA---------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1800 narqqmerqnkDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIvrrtEKKLKEVMMQVEDERRH 1879
Cdd:COG3206 302 -----------ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVAREL 366
|
250
....*....|....*..
gi 1604804600 1880 ADQYKEQMEKANSRMKQ 1896
Cdd:COG3206 367 YESLLQRLEEARLAEAL 383
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1284 |
1.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 851 RLFTKVKPLLQVTRQEEELQAKDEELvKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLS 930
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 931 RKQELEEILHDLEsrveeeEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQldkvTAEAKIKKMEEDILLLEDQNS 1010
Cdd:COG4717 168 LEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELE----EAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1011 KFLKEKKLLEDR--------ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQElEKAKRKLDAETTDL 1082
Cdd:COG4717 238 AAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK-EAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1083 QDQivELQAQIEELKFQLTKKEEELQAALARsdeetlqknnaLKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEE 1162
Cdd:COG4717 317 EEE--ELEELLAALGLPPDLSPEELLELLDR-----------IEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1163 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQ 1242
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1604804600 1243 SLENDNkelscdvkTLQQAKTESEHKRKKLEAQLQEFMARAT 1284
Cdd:COG4717 464 QLEEDG--------ELAELLQELEELKAELRELAEEWAALKL 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1522-1755 |
1.45e-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: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1522 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdrdlqardeq 1601
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1602 gEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAankgrdeavkqlrkLQAQMKDYQRELEEARA 1681
Cdd:COG4942 100 -EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--------------RREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1682 SRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1755
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1708-1946 |
1.46e-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: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1708 QEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTE 1787
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1788 LAGERSAAQKSENARQQMERQNKdLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLK 1867
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1868 EVMMQVEDERRhadQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRRG 1946
Cdd:COG4942 178 ALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1065-1727 |
1.57e-07 |
|
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: 56.68 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1065 RQELEKAKRKLDAETTDLQDQIVELQA-QIEELKfqltKKEEELqaalaRSDEETlqknnALKQVRELQAHLAELQEDLE 1143
Cdd:pfam07111 43 GQGPGRRGRSLELEGSQALSQQAELISrQLQELR----RLEEEV-----RLLRET-----SLQQKMRLEAQAMELDALAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1144 SEKMCRSKAEKLKRDLSEElEALKTELEDtldttAAQQELrskreQEVAELkkaideetknHEAQIQEMRQRQATALEEL 1223
Cdd:pfam07111 109 AEKAGQAEAEGLRAALAGA-EMVRKNLEE-----GSQREL-----EEIQRL----------HQEQLSSLTQAHEEALSSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1224 SEQLEqakrfksNLEKNKQSLENDNkelSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAErshklQTE 1303
Cdd:pfam07111 168 TSKAE-------GLEKSLNSLETKR---AGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGE-----QVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1304 LDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETrQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRN---LEKQ 1380
Cdd:pfam07111 233 PEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRV-QSLTHMLALQEEELTRKIQPSDSLEPEFPKKCrslLNRW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1381 LQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVelTSQCLEEKTmamdkmektknrLQQELDDLMVDLDHQRQIVSN 1460
Cdd:pfam07111 312 REKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQV--TSQSQEQAI------------LQRALQDKAAEVEVERMSAKG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1461 LEKKQKKFDQLLAEEKTISAQYAEE-RDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRA--EMEDLMSSKDD 1537
Cdd:pfam07111 378 LQMELSRAQEARRRQQQQTASAEEQlKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKGLMARKVA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1538 VGKNVHELEKSKRTLEQQVEEMRTQLEELEDElqatedaKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREME 1617
Cdd:pfam07111 458 LAQLRQESCPPPPPAPPVDADLSLELEQLREE-------RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1618 AELedERKQRTLAVASkKKLEMDLNELEGQIEAANKGRDEAVKQLR---------------KLQAQMKDYQRELEEARAS 1682
Cdd:pfam07111 531 QEL--QRAQESLASVG-QQLEVARQGQQESTEEAASLRQELTQQQEiygqalqekvaevetRLREQLSDTKRRLNEARRE 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1683 RDEIF----------TQSKENEKKLKGLEAEilqlQEDHAASERARRHAEQERDE 1727
Cdd:pfam07111 608 QAKAVvslrqiqhraTQEKERNQELRRLQDE----ARKEEGQRLARRVQELERDK 658
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1189-1634 |
1.75e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1189 QEVAELKKAIDEEtKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLENDnKELSCDVKTLQQAKTESEHK 1268
Cdd:COG4717 71 KELKELEEELKEA-EEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1269 RKKLEaQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLK-LAKEVDKLNSKLQDSEELRQEETRQKL 1347
Cdd:COG4717 145 PERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1348 NLSTQIRQLEVDRNTLleqqeeEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEV-----------KRKLQKDV 1416
Cdd:COG4717 224 ELEEELEQLENELEAA------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1417 ELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREK 1496
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1497 DTKA------LSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKnvHELEKSKRTLEQQVEEMRTQLEELEDEL 1570
Cdd:COG4717 378 EAGVedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 1571 QATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKK----RLLVKQVREMEAELEDERKQRTLAVASK 1634
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELEELKAELRELAEEwaalKLALELLEEAREEYREERLPPVLERASE 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1176-1407 |
1.92e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1176 TTAAQQELRSKREQEVAELKKAIdEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLEndnkelscdv 1255
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEI-AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1256 KTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDS 1335
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1336 EELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEE 1407
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
922-1504 |
2.04e-07 |
|
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: 56.37 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 922 EEMRVRLLSRKQELEeilhdlesrveeeeERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKlqldkVTAEAKIKKMEed 1001
Cdd:pfam10174 140 EEMELRIETQKQTLG--------------ARDESIKKLLEMLQSKGLPKKSGEEDWERTRRI-----AEAEMQLGHLE-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1002 iLLLEDQNSKFLKEKKLLEDRisemtSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEktrQELEKAKRKLDAETTD 1081
Cdd:pfam10174 199 -VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1082 LQDQIVELQA----------QIEELKFQLTKKEEELQAALARSDE------------ETLQKNNALKQVRE--LQAHLAE 1137
Cdd:pfam10174 270 REEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1138 LQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAqqelrskREQEVAELKKAID---EETKNHEAQIQEMRQ 1214
Cdd:pfam10174 350 LRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGLKE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1215 RQA----------TALEELSEQLEQAKRFKSNLEKNKqslENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARAT 1284
Cdd:pfam10174 423 RVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1285 EAERTKGELAERSHKLQTELDNactmLEVAEKKGLKlakEVDKLNSKLQDSEELrQEETRQKLNLSTQIRQLEVDRNTLL 1364
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKS----LEIAVEQKKE---ECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQEVARYK 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1365 EQQEEEEEARRNLEKQLQMVQSQMFETKKKLE--EDLGSMEGLEEVKRKLQKDvelTSQCLEEKTMAM-------DKMEK 1435
Cdd:pfam10174 572 EESGKAQAEVERLLGILREVENEKNDKDKKIAelESLTLRQMKEQNKKVANIK---HGQQEMKKKGAQlleearrREDNL 648
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1436 TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMA 1504
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1062-1232 |
2.11e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1062 EKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELK--FQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQ 1139
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1140 EDLES--EKMCRSKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELRSKREQeVAELKKAIDEETKNHEAQIQEMRQRQ 1216
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQ-IAALRAQLQQEAQRILASLEAELEAL 325
|
170
....*....|....*.
gi 1604804600 1217 ATALEELSEQLEQAKR 1232
Cdd:COG3206 326 QAREASLQAQLAQLEA 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
784-1312 |
2.35e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 784 FFRTGVLahleEERDL--KITDIIIYFQSVCRgylARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWW 850
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 851 RLFTKVKpLLQ--VTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQL-IEEKNILAEQLhaetelfAEAEEMRVR 927
Cdd:COG4913 285 FAQRRLE-LLEaeLEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREI-------ERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 928 LLSRKQELEEILHDLESRVEEEEernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLED 1007
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1008 QNSKFLKEkklLEDRISEMTSQLTEEEEKAKNLG---KVKNKQEM---------------MMVDlEERLKK------EEK 1063
Cdd:COG4913 434 RKSNIPAR---LLALRDALAEALGLDEAELPFVGeliEVRPEEERwrgaiervlggfaltLLVP-PEHYAAalrwvnRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1064 TRQELekakRKLDAETTDLQDQIVELQAQ--IEELKFQLTKKEEELQAALARS-------DEETL--------------- 1119
Cdd:COG4913 510 LRGRL----VYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRfdyvcvdSPEELrrhpraitragqvkg 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1120 -----QKN-------------NALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELE---DTLDTTA 1178
Cdd:COG4913 586 ngtrhEKDdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1179 AQQELRSKrEQEVAELKKAIDEetknhEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTL 1258
Cdd:COG4913 666 AEREIAEL-EAELERLDASSDD-----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1259 qqAKTESEHKRKKLEAQLQEFMARATEAERTKgELAERSHKLQTELDNACTMLE 1312
Cdd:COG4913 740 --EDLARLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNRAEEELE 790
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
875-1446 |
3.10e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 875 ELVKVKERQLKVENELVEMERKHQqliEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQ 954
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK---RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 955 SLqneKKKMQSHIQDLEEQLDEEEAARQ-KLQLDKVTAEAKIKKMEEDILLLEDQNSK--FLKEKKLLEDRISEMtSQLT 1031
Cdd:pfam05557 80 LK---KKYLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQRAELELQSTNSELeeLQERLDLLKAKASEA-EQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1032 EEEEKAKNLGKVKNKQemmMVDLEERLKKEEKTRQELEKAKRKLdAETTDLQDqivELQAQIEELKFQLTKKEEELqaaL 1111
Cdd:pfam05557 156 QNLEKQQSSLAEAEQR---IKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEK---ELERLREHNKHLNENIENKL---L 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1112 ARSDEETLQKNnaLKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEEL---EALKTELEDTLDTTAAQQELRSKRE 1188
Cdd:pfam05557 226 LKEEVEDLKRK--LEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1189 QEVAELKKAIDE---ETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKN----KQSLENDNKELSCDVKTLQQA 1261
Cdd:pfam05557 304 SSARQLEKARREleqELAQYLKKIEDLNKK----LKRHKALVRRLQRRVLLLTKErdgyRAILESYDKELTMSNYSPQLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1262 K--TESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKlaKEVDKLNSKLQDSEELR 1339
Cdd:pfam05557 380 EriEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELER 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1340 QEETRQKLNLSTQIRQLEVDRNTLLEQQeeeeearrnleKQLQMVQSQMFETKKKLEEDLGSM----EGLEEVKRKLQKD 1415
Cdd:pfam05557 458 QRLREQKNELEMELERRCLQGDYDPKKT-----------KVLHLSMNPAAEAYQQRKNQLEKLqaeiERLKRLLKKLEDD 526
|
570 580 590
....*....|....*....|....*....|.
gi 1604804600 1416 VElTSQCLEEKTMAMDkmEKTKNRLQQELDD 1446
Cdd:pfam05557 527 LE-QVLRLPETTSTMN--FKEVLDLRKELES 554
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1523-1855 |
3.20e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 55.07 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1523 QLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFDRDLQARDEQG 1602
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1603 EEKKRLLVK---QVREMEAELEDERKQ-RTLAVASK------KKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDY 1672
Cdd:pfam19220 107 EELRIELRDktaQAEALERQLAAETEQnRALEEENKalreeaQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1673 QRELEEARASRDEIFTQSKENEKKLKGLEAeilQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEAR 1752
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEG---QLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1753 IAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQ-----------NKDLKAKLAELEG 1821
Cdd:pfam19220 264 LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraeleeraemlTKALAAKDAALER 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1604804600 1822 -------------TVKSKFKASIAALEAKILQLEDQLEQEAKERAAA 1855
Cdd:pfam19220 344 aeeriaslsdriaELTKRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
914-1490 |
3.30e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 914 ETELFAEAEEMrvrllsrkQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEeaaRQKLQLDKVTAEA 993
Cdd:COG4913 220 EPDTFEAADAL--------VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE---YLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 994 KIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTE-EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAK 1072
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1073 RKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARsdeetlqknnALKQVRELQAHLAELQEDLESEKMCRS-- 1150
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE----------AEAALRDLRRELRELEAEIASLERRKSni 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1151 --KAEKLKRDLSEELEALKTEL-----------EDTLDTTAAQQELRSKR------EQEVAELKKAIDE----------- 1200
Cdd:COG4913 439 paRLLALRDALAEALGLDEAELpfvgelievrpEEERWRGAIERVLGGFAltllvpPEHYAAALRWVNRlhlrgrlvyer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1201 ----------------------ETKNHEAQ---IQEMRQRQATALEELSEQLEQAKR-------FKSNL---EKNKQS-- 1243
Cdd:COG4913 519 vrtglpdperprldpdslagklDFKPHPFRawlEAELGRRFDYVCVDSPEELRRHPRaitragqVKGNGtrhEKDDRRri 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1244 -----LENDNKELscdVKTLQQaktesehKRKKLEAQLQEFMARATEAERTKGELAERSHKLQ-------TELDNACTML 1311
Cdd:COG4913 599 rsryvLGFDNRAK---LAALEA-------ELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVASAER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1312 EVAEKKGLKLA-----KEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQS 1386
Cdd:COG4913 669 EIAELEAELERldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1387 QMFEtkKKLEEDLGSmEGLEEVKRKLQKDVE-LTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLD--------HQRQI 1457
Cdd:COG4913 749 ALLE--ERFAAALGD-AVERELRENLEERIDaLRARLNRAEEELERAMRAFNREWPAETADLDADLEslpeylalLDRLE 825
|
650 660 670
....*....|....*....|....*....|....*...
gi 1604804600 1458 VSNLEKKQKKFDQLLAEEKT-----ISAQYAEERDRAE 1490
Cdd:COG4913 826 EDGLPEYEERFKELLNENSIefvadLLSKLRRAIREIK 863
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1409-1696 |
5.93e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1409 KRKLQKDVeltsqcLEEKTMA-MDKMEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQL 1471
Cdd:PHA02562 152 RRKLVEDL------LDISVLSeMDKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1472 LAEEKTISAQYAEERDRAEAEAREKDTKALSMaraleealeakeelerfnKQLRAEMEDLMSSKDDVGKNVHELEKSKR- 1550
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSAAL------------------NKLNTAAAKIKSKIEQFQKVIKMYEKGGVc 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1551 -TLEQQVEEMRTQLEELEDelqatedaklrlevNMQAMKAQFDRDLQARDEqgeekkrllvkqvremEAELEDErkqrtL 1629
Cdd:PHA02562 288 pTCTQQISEGPDRITKIKD--------------KLKELQHSLEKLDTAIDE----------------LEEIMDE-----F 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1630 AVASKKKLEM--DLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKK 1696
Cdd:PHA02562 333 NEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1638-1868 |
7.63e-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: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1638 EMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEdhAASERA 1717
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE--ELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1718 RrhAEQERDELADEISN--SASGKSSLLEekrRLEAriaqleeeleeeqgnMELLNDRFRKSNIQVDNLNTELAGERSAA 1795
Cdd:COG3883 93 R--ALYRSGGSVSYLDVllGSESFSDFLD---RLSA---------------LSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1796 qksENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKE 1868
Cdd:COG3883 153 ---EAKLAELEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
995-1222 |
8.34e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.52 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 995 IKKMEEDILLLE-------DQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQE 1067
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE-EQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1068 LEKA-KRKLDAETTDLQDQIVELQAQIEELKFQLTKkeeelqaaLARSDEE--TLQKNNAL--KQVRELQAHLAELQEDL 1142
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIE--------VAETEERvfKLEKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1143 esekmcrSKAEKLKRD-LSEELEalktELEDTLDTTAAQQELRSKREQEVAELKKAIDE-ETKNHEAQIQ-------EMR 1213
Cdd:PLN02939 288 -------SKLSPLQYDcWWEKVE----NLQDLLDRATNQVEKAALVLDQNQDLRDKVDKlEASLKEANVSkfssykvELL 356
|
....*....
gi 1604804600 1214 QRQATALEE 1222
Cdd:PLN02939 357 QQKLKLLEE 365
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1031-1243 |
9.99e-07 |
|
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: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1031 TEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAA 1110
Cdd:COG3883 16 PQIQAKQKELSELQAELE----AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1111 L------------------ARSDEETLQKNNALKQVRELQAHLAELQEDLesekmcRSKAEKLKrdlsEELEALKTELED 1172
Cdd:COG3883 92 AralyrsggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKAD------KAELEAKK----AELEAKLAELEA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1173 TLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQS 1243
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1586-1732 |
1.01e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1586 AMKAQFDR--DLQARDEQGEEKKRLLV---KQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVK 1660
Cdd:COG1579 1 AMPEDLRAllDLQELDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1661 QLRKLQA--QMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEI 1732
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1264-1939 |
1.02e-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: 54.07 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1264 ESEHKRKKLEAQLQEFMA-RATEAERTKGE-LAERSHKLQTELDNACTM------LEVAEKKGLKLAKEVDK-LNSKL-- 1332
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIQAiAGIMKIRPEFTkLQQEFNTLESAELRLSHLhfgyksDETLIASRQEERQETSAeLNQLLrt 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1333 ------QDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLE 1406
Cdd:pfam12128 295 lddqwkEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVT 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1407 E--------VKRKLQKDVELTSQCLE--------EKTMAMDKMEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFD 1469
Cdd:pfam12128 375 AkynrrrskIKEQNNRDIAGIKDKLAkireardrQLAVAEDDLQALESELREQLEAGKLEFnEEEYRLKSRLGELKLRLN 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1470 QLLAEEKTISAQyaEERDRAEAEAREKDTKAlsmaraleealeakeelerfnkqlRAEMEDLMSSKDDVGKNVHELEKSK 1549
Cdd:pfam12128 455 QATATPELLLQL--ENFDERIERAREEQEAA------------------------NAEVERLQSELRQARKRRDQASEAL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1550 RTLEQQVEEMRTQLEELEDELQA----------TEDAKLRLEVNMQAMKAQFDR-DLQARDEQGEEKKRLLVKQVRemea 1618
Cdd:pfam12128 509 RQASRRLEERQSALDELELQLFPqagtllhflrKEAPDWEQSIGKVISPELLHRtDLDPEVWDGSVGGELNLYGVK---- 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1619 eLEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASrdeiFTQSKENEKKLK 1698
Cdd:pfam12128 585 -LDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLF 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1699 G-LEAEILQLQEdhaASERARRHAEQERDELADEISNSASGKSSLLEEKRR--LEARIAQLeeeleeeQGNMELLNDRfr 1775
Cdd:pfam12128 660 DeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL-- 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1776 ksNIQVDNLNTELAGERSAAQKSENA-RQQMERqnkDLKAKlaELEGTVKSKFKASIAALEAKIlqledqlEQEAKERAA 1854
Cdd:pfam12128 728 --DAQLALLKAAIAARRSGAKAELKAlETWYKR---DLASL--GVDPDVIAKLKREIRTLERKI-------ERIAVRRQE 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1855 ankiVRRTEKKLKEVMMQvederrHADQYKEQMEKANSRMK----QLKRQLEEAEEEATRANATRRKLQRELDDATEASE 1930
Cdd:pfam12128 794 ----VLRYFDWYQETWLQ------RRPRLATQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
....*....
gi 1604804600 1931 GLTREVSSL 1939
Cdd:pfam12128 864 GLRCEMSKL 872
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
862-1502 |
1.09e-06 |
|
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: 53.99 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 862 VTRQEEELQAKDEELVKVKE----RQLKVENELVEMErkhQQLIEEKNILAEQLHAETELfAEAEEMRVRLLSRKQ-ELE 936
Cdd:pfam07111 68 ISRQLQELRRLEEEVRLLREtslqQKMRLEAQAMELD---ALAVAEKAGQAEAEGLRAAL-AGAEMVRKNLEEGSQrELE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 937 EIlhdlesrveeeeernQSLQNEK--KKMQSHiqdleeQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQnskflK 1014
Cdd:pfam07111 144 EI---------------QRLHQEQlsSLTQAH------EEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----K 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1015 EKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQemmmVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIE 1094
Cdd:pfam07111 198 EAELLRKQLSKTQEELEAQVTLVESLRKYVGEQ----VPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1095 ELKFQLTKKEEELQAALARSD----EETLQKNNALKQVRELQAHLaelqedlesekMCRSKAEKLK-RDLSEELEalkte 1169
Cdd:pfam07111 274 SLTHMLALQEEELTRKIQPSDslepEFPKKCRSLLNRWREKVFAL-----------MVQLKAQDLEhRDSVKQLR----- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1170 ledtlDTTAAQQELRSKREQEVAELKKAIDEETKnhEAQIQEMrqrqatALEELSEQLEQAKRFKSNLEKNKQSLENDNK 1249
Cdd:pfam07111 338 -----GQVAELQEQVTSQSQEQAILQRALQDKAA--EVEVERM------SAKGLQMELSRAQEARRRQQQQTASAEEQLK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1250 ELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERT----KGELAERSHKLQTELDnACTMLEVAEKKGLKLAKEV 1325
Cdd:pfam07111 405 FVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhtiKGLMARKVALAQLRQE-SCPPPPPAPPVDADLSLEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1326 dklnsklqdsEELRQEETR--QKLNLSTQIRQLEVDRNTLLEQQEEEEEAR--RNLEKQLQMVQSQMFETKKKLEEDL-G 1400
Cdd:pfam07111 484 ----------EQLREERNRldAELQLSAHLIQQEVGRAREQGEAERQQLSEvaQQLEQELQRAQESLASVGQQLEVARqG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1401 SMEGLEE---VKRKLQKDVELTSQCLEEktmamdKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKt 1477
Cdd:pfam07111 554 QQESTEEaasLRQELTQQQEIYGQALQE------KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK- 626
|
650 660
....*....|....*....|....*
gi 1604804600 1478 isaQYAEERDRAEAEAREKDTKALS 1502
Cdd:pfam07111 627 ---ERNQELRRLQDEARKEEGQRLA 648
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1169-1860 |
1.29e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1169 ELEDTLDTTAAQqelRSKREQEVAELKKAidEETKNHEAQIQEMRQRQATALEELSEQLeqaKRFKSNLEKNKQSLENDN 1248
Cdd:PRK01156 139 EMDSLISGDPAQ---RKKILDEILEINSL--ERNYDKLKDVIDMLRAEISNIDYLEEKL---KSSNLELENIKKQIADDE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1249 KELSCDVKTLQQAKTESEHKRKK---LEAQLQEFMARATEAERTKGELAERSHKLQTEldnactmlevaEKKGLKLAKEV 1325
Cdd:PRK01156 211 KSHSITLKEIERLSIEYNNAMDDynnLKSALNELSSLEDMKNRYESEIKTAESDLSME-----------LEKNNYYKELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1326 DKLNSKLQDSEELRQEETRQKLNLSTQIRQLEvdrntlleqqeeeeEARRNLEKQLQMVQSQMfetkKKLEEdlgsmegl 1405
Cdd:PRK01156 280 ERHMKIINDPVYKNRNYINDYFKYKNDIENKK--------------QILSNIDAEINKYHAII----KKLSV-------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1406 eevkrkLQKDVEltsqcleektmAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEE 1485
Cdd:PRK01156 334 ------LQKDYN-----------DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1486 RDRAEAEAREkdtkalsmaraleealeakeelerfnkqLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEE 1565
Cdd:PRK01156 397 LKIQEIDPDA----------------------------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEM 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1566 LEDE---------LQATEDAKLRLEVNMQAMKAQFD-----RDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAV 1631
Cdd:PRK01156 449 LNGQsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKireieIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESAR 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1632 ASKKKLEMDLNELEGQIEAANKGRDEAVK-QLRKLQAQMKDYQR--------ELEEARASRDEIFTQSKENEKKLKGLEA 1702
Cdd:PRK01156 529 ADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNalavisliDIETNRSRSNEIKKQLNDLESRLQEIEI 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1703 EIlqlQEDHAASERARRHAEQErdeladeiSNSASGKSSLLEEKRRLEARIAQLEeeleeeqgnmellnDRFRKSNIQVD 1782
Cdd:PRK01156 609 GF---PDDKSYIDKSIREIENE--------ANNLNNKYNEIQENKILIEKLRGKI--------------DNYKKQIAEID 663
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 1783 NLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSkFKASIAALEAKILQLEDQLEQEAKERAAANKIVR 1860
Cdd:PRK01156 664 SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI-LRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1373-1901 |
1.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1373 ARRNLEKQLQMVQ--SQMFETKKKLEEDLGSMEGLEEVKRKLqkDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVD 1450
Cdd:COG4913 240 AHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1451 LDHQRQIVSNLEKK--QKKFDQLlaeektisAQYAEERDRAEAEAREKDTKAlsmaraleealeakeelERFNKQLRAEM 1528
Cdd:COG4913 318 LDALREELDELEAQirGNGGDRL--------EQLEREIERLERELEERERRR-----------------ARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1529 EDLMSSKDDVGKNV--------------HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRD 1594
Cdd:COG4913 373 LPLPASAEEFAALRaeaaallealeeelEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1595 LQARDEQ-----------GEEKK--------------RLLV-----KQVREMEAELEDERKQRTLAVASKKKLEMDLNEL 1644
Cdd:COG4913 453 LGLDEAElpfvgelievrPEEERwrgaiervlggfalTLLVppehyAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1645 EGQIE-----AANKGRDEAVKQLRKL--------QAQMKDYQREL---------EEARASRDEIFTQSK-----ENEKKL 1697
Cdd:COG4913 533 PDSLAgkldfKPHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAItragqvkgnGTRHEKDDRRRIRSRyvlgfDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1698 KGLEAEILQLQEDHAASERARRHAEQERDEladeisnsasgksslLEEKRRLEARIAQleeeleeeqgnmellndrFRKS 1777
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDA---------------LQERREALQRLAE------------------YSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1778 NIQVDNLNTELA---GERSAAQKSENARQQMERQNKDLKAKLAELEGTVKsKFKASIAALEAKILQLEDQLEQEAKERAA 1854
Cdd:COG4913 660 EIDVASAEREIAeleAELERLDASSDDLAALEEQLEELEAELEELEEELD-ELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1855 ANKIVR-----RTEKKLKEVMMQvEDERRHADQYKEQMEKANSRMKQLKRQL 1901
Cdd:COG4913 739 AEDLARlelraLLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1700-1942 |
1.40e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1700 LEAEILQLQEDHAASERARRHAEQERDELAdeisnsasgkssLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKsnI 1779
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQ--R 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1780 QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAaankiv 1859
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRA------ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1860 rRTEKKLKEVMMQVEDErrhADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDateasegLTREVSSL 1939
Cdd:COG4913 363 -RLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIASL 431
|
...
gi 1604804600 1940 KNR 1942
Cdd:COG4913 432 ERR 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1120-1346 |
1.69e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1120 QKNNALKQVRELQAHLAELQEDLESekmcrskaeklkrdLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID 1199
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA--------------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1200 EETKNHEAQIQEMRQ--RQATALEEL--SEQLEQakrFKSNLEKNKQSLENDNKELscdvKTLQQAKTESEHKRKKLEAQ 1275
Cdd:COG3883 83 ERREELGERARALYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1276 LQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQK 1346
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1014-1418 |
2.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAettdlQDQIVELQAQI 1093
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEK-----LLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EELKFQLTKKEEELQAALARSDEEtlqkNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLK-RDLSEELEALKTELED 1172
Cdd:COG4717 135 EALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1173 TLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEK-----------NK 1241
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllalLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1242 QSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKL 1321
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1322 AKEVDKLNSKLQDSEELRQ--EETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEA--RRNLEKQLQMVQSQMFETKKKLEE 1397
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEE 450
|
410 420
....*....|....*....|.
gi 1604804600 1398 DLGSMEGLEEVKRKLQKDVEL 1418
Cdd:COG4717 451 LREELAELEAELEQLEEDGEL 471
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1544-1704 |
2.23e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1544 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQGEEKKrllVKQVREMEAELEDE 1623
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN---NKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1624 RKQRtlavaskKKLEMDLNELEGQIEAANKgrdeavkQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAE 1703
Cdd:COG1579 102 KRRI-------SDLEDEILELMERIEELEE-------ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
.
gi 1604804600 1704 I 1704
Cdd:COG1579 168 L 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1393-1868 |
3.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1393 KKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDhQRQIVSNLEKKQKKFDQLL 1472
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1473 AEEKTIsAQYAEERDRAEAEAREKDTKAlsmaraleealeaKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTL 1552
Cdd:COG4717 153 ERLEEL-RELEEELEELEAELAELQEEL-------------EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1553 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKR-------------LLVKQVREMEAE 1619
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1620 LEDERKQRTLAVASKKKLEMdlNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIftqskenekKLKG 1699
Cdd:COG4717 299 SLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL---------QLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1700 LEAEILQL-QEDHAASERARRHAEQERDELADeisnsasgkssLLEEKRRLEARIAQLEEELEEEQGNMELlndrfrksn 1778
Cdd:COG4717 368 LEQEIAALlAEAGVEDEEELRAALEQAEEYQE-----------LKEELEELEEQLEELLGELEELLEALDE--------- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1779 iqvDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGtvkskfKASIAALEAKILQLEDQLEQEAKERAAAN-- 1856
Cdd:COG4717 428 ---EELEEELEELEEELEELEEELEELREELAELEAELEQLEE------DGELAELLQELEELKAELRELAEEWAALKla 498
|
490
....*....|...
gi 1604804600 1857 -KIVRRTEKKLKE 1868
Cdd:COG4717 499 lELLEEAREEYRE 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1535-1755 |
4.50e-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: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1535 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA----------TEDAKLRLEvNMQAMKAQFdRDLQARDEQGEE 1604
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQ-QLSELESQL-AEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1605 KKRLLVKQVREMEAELEDERKQRTLAvaskkKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQREL-EEARASR 1683
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1684 DEIFTQSKENEKKLKGLEAEILQLQEDHAA-SERARRHAEQERD-ELADEISNsasgksSLLeeKRRLEARIAQ 1755
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYE------SLL--QRLEEARLAE 381
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1603-1752 |
4.55e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1603 EEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIE--------AANKGRD----EAVKQLRKLQAQMK 1670
Cdd:COG1842 22 EDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEAQAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1671 DYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLqedhAASERARRHAEQERDELADEISNSASGKSSLLEEK-RRL 1749
Cdd:COG1842 102 ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL----KARAKAAKAQEKVNEALSGIDSDDATSALERMEEKiEEM 177
|
...
gi 1604804600 1750 EAR 1752
Cdd:COG1842 178 EAR 180
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1480-1852 |
6.38e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1480 AQYAEERDRaEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1559
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1560 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKqVREMEAELederkqRTLAvaskKKLEM 1639
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK-LQQTEEEL------RSLS----KEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1640 DLNELEGQIEAANKGRDEAVKQLRKL-QAQMKDYQRE--LEEARASRDEIFTqskeNEKKLKGLEAEILQL--QEDHAAS 1714
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNA----SERKVEGLGEELSSMaaQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1715 E--RARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGER 1792
Cdd:pfam07888 273 ElhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1793 --SAAQKSENARQQMErqnkdLKAKLAELEGTvKSKFKASIAALEAKILQLEDQLEQEAKER 1852
Cdd:pfam07888 353 dcNRVQLSESRRELQE-----LKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1373-1755 |
6.81e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1373 ARRNLEKQLQMvQSQMFETKKKLEEdlgSMEGLEEVKRKLQKDVEltsqclEEKTMAMDkMEKTKNRLQQelddLMVDLD 1452
Cdd:PRK04863 281 RRVHLEEALEL-RRELYTSRRQLAA---EQYRLVEMARELAELNE------AESDLEQD-YQAASDHLNL----VQTALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1453 HQRQI---VSNLEKKQKKfdqlLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEME 1529
Cdd:PRK04863 346 QQEKIeryQADLEELEER----LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1530 DLMSSKDDVGKNVHELEKskrtLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFDRDLQARDEQGEEKKRLL 1609
Cdd:PRK04863 422 ALERAKQLCGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIAGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1610 VKQV-REMeaeLEDERKQRTLAvASKKKLEMDLNELEGQIE---AANKGRDEAVKQLRK---LQAQMKDYQRELEEARAS 1682
Cdd:PRK04863 494 AWDVaREL---LRRLREQRHLA-EQLQQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKnldDEDELEQLQEELEARLES 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1683 RDEIFTQSKEN----EKKLKGLEAEILQL----QEDHAASERARRHAEQERDELADE------ISNSASGKSSLLEEKRR 1748
Cdd:PRK04863 570 LSESVSEARERrmalRQQLEQLQARIQRLaaraPAWLAAQDALARLREQSGEEFEDSqdvteyMQQLLERERELTVERDE 649
|
....*..
gi 1604804600 1749 LEARIAQ 1755
Cdd:PRK04863 650 LAARKQA 656
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1642-1945 |
7.12e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1642 NELEGQIEAANKGRDeavkqlrkLQAQMKDYQRELEEARASRDEIFTQSKENE---KKLKGLEAEILQLQEDHAASERAr 1718
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1719 rhaeqerdelADEISNSASGKSSLleekRRLEARIAQLEEELEEEQGNmelLNDrfrkSNIQVDNLNTelAGERSAAQKS 1798
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQND---LAE----YNSQLVSLQT--QPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1799 ENAR--QQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKIL----------QLEDqLEQEAKERAAANkiVRRTEKKL 1866
Cdd:PRK11281 167 ANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDlqrkslegntQLQD-LLQKQRDYLTAR--IQRLEHQL 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1867 KEVMMQVEDERRhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANatrRKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:PRK11281 244 QLLQEAINSKRL--TLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLDR 317
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1019-1174 |
8.59e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1019 LEDRISEMTSQLTEEEEKAKnlGKVKNKQEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQDQIVELQAQIEELKF 1098
Cdd:COG2433 378 IEEALEELIEKELPEEEPEA--EREKEHEERELTEEEEEIRRLEEQVERLE-------AEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1099 QLTKKEEELQAALARSDEetlqknnalkqVRELQAHLAELQEDLESEkmcRSKAEKLKRDLSEELEALKTELEDTL 1174
Cdd:COG2433 449 ELSEARSEERREIRKDRE-----------ISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
899-1280 |
8.83e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 899 QLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEE 978
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 979 AARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLgkvknkqEMMMVDLEERL 1058
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1059 KKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQieelkfqltkkeeelqaaLARSDEETLQKNNALKQVRELQAHLAEL 1138
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK------------------LTTAHRKEAENEALLEELRSLQERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1139 QEdlesekmcrsKAEKLKRDLSE---------------ELEALKTELEdTLDTTAAQQELRSKREQEVAELKKAIDEETK 1203
Cdd:pfam07888 250 ER----------KVEGLGEELSSmaaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1204 NHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHkrkkLEAQLQEFM 1280
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQ----LQAEKQELL 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1522-1738 |
1.11e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1522 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ 1601
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1602 GEEKKRL-----------LVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMK 1670
Cdd:COG3883 99 GGSVSYLdvllgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 1671 DYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASG 1738
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
892-1317 |
1.21e-05 |
|
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: 50.07 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 892 EMERKHQQLIEEKNILAEQLHAETELFAEAEEM--------RVRLLSRKQ--ELEEILHDLESRVEEEEERNQSLQNEKK 961
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGddsgtpggKKYLLLQKQleQLQEENFRLETARDDYRIKCEELEKEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 962 KMQSHIQdleeqldeeeaarqklQLDKVTAEAKIKKMEEDILLLEDQNSKFLKE-----KKLLEDrISEMTSQLTEEEEk 1036
Cdd:pfam05622 98 ELQHRNE----------------ELTSLAEEAQALKDEMDILRESSDKVKKLEAtvetyKKKLED-LGDLRRQVKLLEE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1037 aKNLGKVKNKqemmmVDLEERLKKEEKTRQELEKAKRKLdaetTDLQDQIVELQAQIEELKFQLTKKEEELqAALARSDE 1116
Cdd:pfam05622 160 -RNAEYMQRT-----LQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKL-EALQKEKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1117 ETLQKNNALKQVRElQAHLAELQED-LESEKMCRSKAEKLKRDLSEELeaLKTELEDTLdttaaqqeLRSKREQEVAELK 1195
Cdd:pfam05622 229 RLIIERDTLRETNE-ELRCAQLQQAeLSQADALLSPSSDPGDNLAAEI--MPAEIREKL--------IRLQHENKMLRLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1196 KAIDEETKnheaqiqemrqrqataLEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTE-------SEHK 1268
Cdd:pfam05622 298 QEGSYRER----------------LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEqgskaedSSLL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1604804600 1269 RKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKK 1317
Cdd:pfam05622 362 KQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRK 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
943-1133 |
1.22e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 943 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDIlllEDQNSKFLKEKKLLEDR 1022
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1023 ISEM---------TSQLTEEE------EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIV 1087
Cdd:COG3883 92 ARALyrsggsvsyLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1604804600 1088 ELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQA 1133
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
672-696 |
1.30e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.30e-05
10 20
....*....|....*....|....*
gi 1604804600 672 YKESLTKLMATLRNTNPNFVRCIIP 696
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
990-1195 |
1.31e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 990 TAEAKIK--KMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEErLKKEEKTRQE 1067
Cdd:COG3206 193 EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1068 LEKAKRKLDAETTDLQD---QIVELQAQIEELKFQLtKKEEELQAALARSDEETLQknnalKQVRELQAHLAELQEDLES 1144
Cdd:COG3206 272 LAELEAELAELSARYTPnhpDVIALRAQIAALRAQL-QQEAQRILASLEAELEALQ-----AREASLQAQLAQLEARLAE 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1145 EKMCRSKAEKLKRDlseeLEALKTELEDTLdttAAQQELRSKREQEVAELK 1195
Cdd:COG3206 346 LPELEAELRRLERE----VEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
861-1340 |
1.35e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 861 QVTRQEEELQAKDEELVKVKERqlkveneLVEMERKHQQLieekNILAEQLHAETELFAEAEEmRVRLLSRKQELEE--- 937
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEA----EQLRQNLEKQQSSLAEAEQ-RIKELEFEIQSQEqds 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 938 -ILHDLESRVeeeeERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQlDKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1016
Cdd:pfam05557 187 eIVKNSKSEL----ARIPELEKELERLREHNKHLNENIENKLLLKEEVE-DLKRKLEREEKYREEAATLELEKEKLEQEL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1017 KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMM---VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1093
Cdd:pfam05557 262 QSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKeenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EEL---KFQLTKKEEELQAALARSDEETLQKN---NALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALK 1167
Cdd:pfam05557 342 RRLqrrVLLLTKERDGYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1168 TELedTLDTTAAQQELRSKREQEVAELKKAIDEetknHEAQIQEMRQRQatalEELSEQLEqakrfksnleknKQSLEND 1247
Cdd:pfam05557 422 REL--QALRQQESLADPSYSKEEVDSLRRKLET----LELERQRLREQK----NELEMELE------------RRCLQGD 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1248 NKELSCDVKTLQQAKT-ESEHKRKKLEAQLQEfmaratEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVD 1326
Cdd:pfam05557 480 YDPKKTKVLHLSMNPAaEAYQQRKNQLEKLQA------EIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
490
....*....|....
gi 1604804600 1327 KLNSKLQDSEELRQ 1340
Cdd:pfam05557 554 SAELKNQRLKEVFQ 567
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1315-1940 |
1.43e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1315 EKKGLKLAKEVDKLNSKLQDSEELRQEETRQKL---NLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQM--- 1388
Cdd:PRK01156 165 ERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLeleNIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALnel 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1389 ---FETKKKLEEDLGSMEGleEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMvDLDHQRQIVSNLEKKQ 1465
Cdd:PRK01156 245 sslEDMKNRYESEIKTAES--DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1466 KKFDQL---LAEEKTISAQYAEERDRAEaearEKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNV 1542
Cdd:PRK01156 322 NKYHAIikkLSVLQKDYNDYIKKKSRYD----DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1543 HELEKSKRTLEQQVEEMRTQLEELEDE---LQATEDA----KLRLEVNMQAMKAQFDRDLQARDeQGEEKKRLLVKQVRE 1615
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKvssLNQRIRAlrenLDELSRNMEMLNGQSVCPVCGTT-LGEEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1616 meaelederkqrtlavaSKKKLEMDLNELEGQIEAAnkgrDEAVKQLRKLQAQMKdyQRELEEARASrdeiftqskenEK 1695
Cdd:PRK01156 477 -----------------KKSRLEEKIREIEIEVKDI----DEKIVDLKKRKEYLE--SEEINKSINE-----------YN 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1696 KLKGLEAEIlqlqEDHAASERARRHAEQERDELADEIsnsasgKSSLLEEkrrLEARiaqleeeleeeqgNMELLNDRFR 1775
Cdd:PRK01156 523 KIESARADL----EDIKIKINELKDKHDKYEEIKNRY------KSLKLED---LDSK-------------RTSWLNALAV 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1776 KSNIQVDNLNTElagersaaqksenaRQQMERQNKDLKAKLAELEGT---VKSKFKASIAALEAKILQLEDQLeQEAKER 1852
Cdd:PRK01156 577 ISLIDIETNRSR--------------SNEIKKQLNDLESRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NEIQEN 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1853 AAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGL 1932
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
....*...
gi 1604804600 1933 TREVSSLK 1940
Cdd:PRK01156 722 NETLESMK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
902-1117 |
1.57e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 902 EEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDE--EEA 979
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 980 ARQKLQLDKVTAEA-KIKKMEEDILLLEDQN-SKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEER 1057
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1058 LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfqltKKEEELQAALARSDEE 1117
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAE 235
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
934-1424 |
2.10e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 934 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaarQKLQLDKVTAEA-------KIKKMEEDILLLE 1006
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---------QINDLEDVADKAisnddpeEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1007 DQNSKFLKEKKLLEDRISEMTSQLTE-EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD------AET 1079
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIEKDKTSlEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDeikeksPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1080 TDLQDQIVELQAQIEEL--------KFQLTKK-----------------------------EEELQAALARSDEET---- 1118
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMETFnishdddkDHHIISKkhdenisdirekslkiiedfseesdindiKKELQKNLLDAQKHNsdin 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1119 ------------LQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEE--LEALKTELEDTLD--------- 1175
Cdd:TIGR01612 1343 lylneianiyniLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDinLEECKSKIESTLDdkdidecik 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1176 -TTAAQQELRSKREQEVAELKKAID------------EETKNHEAQIQEMRQRQATA-----LEELSEQLEQAKRFKSNL 1237
Cdd:TIGR01612 1423 kIKELKNHILSEESNIDTYFKNADEnnenvlllfkniEMADNKSQHILKIKKDNATNdhdfnINELKEHIDKSKGCKDEA 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1238 EKNKQSLEND---------------NKELSCDVKT-LQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQ 1301
Cdd:TIGR01612 1503 DKNAKAIEKNkelfeqykkdvtellNKYSALAIKNkFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIE 1582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1302 TELDN----------ACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLS-TQIRQLEVDRNTLLEQQEEE 1370
Cdd:TIGR01612 1583 DDAAKndksnkaaidIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQdTELKENGDNLNSLQEFLESL 1662
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1371 EEARRNLE---KQLQMVQSQMFETKKKLEE-----DLGSMEGLEEVKRKLQKDVELTSQCLE 1424
Cdd:TIGR01612 1663 KDQKKNIEdkkKELDELDSEIEKIEIDVDQhkknyEIGIIEKIKEIAIANKEEIESIKELIE 1724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
867-1099 |
2.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 867 EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRV 946
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 947 EEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLdkvtAEAKIKKMEEDillLEDQNSKFLKEK-KLLEDRISE 1025
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEELRKE---LEELEKKYSEEEyEELREEYLE 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1026 MTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLdAETTDLQDQIVELQAQIEELKFQ 1099
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL-ERVEELREKVKKYKALLKERALS 743
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1544-1822 |
2.16e-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: 49.74 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1544 ELEKSKRTLEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARdeQGEEKKRLL-----------V 1610
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELerirqeeiameI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1611 KQVREME--------------AELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQREL 1676
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1677 EEARASRDEIFTQsKENEKKLKGLEAEILQlQEDHAASERARRHAEQERDEladeisnsasGKSSLLEEKRR---LEARI 1753
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEK-RDRKRAEEQRRKILEKELEE----------RKQAMIEEERKrklLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1754 AQLEEELEEEQGNMELLNDRFRKSNI----QVDNLNTELAGERSAAQKSENARQQMeRQNKDLKAKLAELEGT 1822
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
983-1710 |
2.77e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 983 KLQLDKVTAeaKIKKMEEDILLLEDQNSKFLKEKklLEDRISEMTSQLTEE--EEKAKNLGKVKNKQEmmmvDLEERLKK 1060
Cdd:TIGR01612 702 KSKIDKEYD--KIQNMETATVELHLSNIENKKNE--LLDIIVEIKKHIHGEinKDLNKILEDFKNKEK----ELSNKIND 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1061 EEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfQLTKKEEELQAALARSDEETLQKNNALKQVRElqAHLAELQE 1140
Cdd:TIGR01612 774 YAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAK-QNYDKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1141 DLESEKMCRSKAEKLKRDLSEELEALKTELEDtldttaaqqELRSKREQEVAELKKAIDEETKNHEAQIQEMrqrqaTAL 1220
Cdd:TIGR01612 851 FINFENNCKEKIDSEHEQFAELTNKIKAEISD---------DKLNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTL 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1221 EELSEQLEQAKRFKSNLEK--NKQSLENDnkELSCDVKTLQQAKTESEHKRKKLEAQLQEfmarateaertkgelaersh 1298
Cdd:TIGR01612 917 KKVDEYIKICENTKESIEKfhNKQNILKE--ILNKNIDTIKESNLIEKSYKDKFDNTLID-------------------- 974
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1299 kLQTELDNACTMLEvaekkglklakevdkLNSKLQDSEELRQEETRQKLNLSTQirqlevDRNTLLEQQEEEEEARRNLE 1378
Cdd:TIGR01612 975 -KINELDKAFKDAS---------------LNDYEAKNNELIKYFNDLKANLGKN------KENMLYHQFDEKEKATNDIE 1032
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1379 KQLQMVQSQMFETKKKLEEDLGSMegLEEVKRKLQKDVE-LTSQCLEEKTMAMDKMEKTKNRLqqelddlmvdldhqrqi 1457
Cdd:TIGR01612 1033 QKIEDANKNIPNIEIAIHTSIYNI--IDEIEKEIGKNIElLNKEILEEAEINITNFNEIKEKL----------------- 1093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1458 vsnlekKQKKFDQLLAEEktiSAQYAEERDRAEAEAREKDTKalsmaraleealeakeelerfnkqlraemedlmsskdd 1537
Cdd:TIGR01612 1094 ------KHYNFDDFGKEE---NIKYADEINKIKDDIKNLDQK-------------------------------------- 1126
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1538 VGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQARDEQGEekkrlLVKQVR 1614
Cdd:TIGR01612 1127 IDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIA 1200
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1615 EMEAELEDERKQRTLAVA---------------SKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMkDYQRELEEA 1679
Cdd:TIGR01612 1201 EIEKDKTSLEEVKGINLSygknlgklflekideEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETF 1279
|
730 740 750
....*....|....*....|....*....|....
gi 1604804600 1680 RASRDEI---FTQSKENEKKLKGLEAEILQLQED 1710
Cdd:TIGR01612 1280 NISHDDDkdhHIISKKHDENISDIREKSLKIIED 1313
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1082-1751 |
3.39e-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: 49.05 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1082 LQDQIVELQAQIEELKFQLTKKEEELQAALAR-----SDEetLQKNNALKqvRELQAHLAELQEDLesekmcrskaeklk 1156
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSiktfwSPE--LKKERALR--KEEAARISVLKEQY-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1157 RDLSEELEALKTELEDTLDTTAAQQELRSKREQEV------AELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQa 1230
Cdd:pfam10174 63 RVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1231 krFKSNLEKNKQSLENDNKELSCDVKTLQ-----QAKTESEHKRKK----LEAQLQEFMARATEAERTKGELAERSHK-- 1299
Cdd:pfam10174 142 --MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREELHRrn 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1300 -----------LQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEEtrqklnlstqIRQLEVDRN------- 1361
Cdd:pfam10174 220 qlqpdpaktkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEE----------IKQMEVYKShskfmkn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1362 ---TLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKN 1438
Cdd:pfam10174 290 kidQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1439 RLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAK 1514
Cdd:pfam10174 370 DLTEEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1515 EELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ------ATEDAKLR-LEVNMQAM 1587
Cdd:pfam10174 450 RIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1588 KAQFDRdLQARD------EQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKL-------EMDLNELEGQIEAANKG 1654
Cdd:pfam10174 530 KEECSK-LENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLlgilrevENEKNDKDKKIAELESL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1655 RDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKlkglEAEILQLQEDHAASERARrhaeQERDELADEISn 1734
Cdd:pfam10174 609 TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTR----QELDATKARLS- 679
|
730
....*....|....*..
gi 1604804600 1735 saSGKSSLLEEKRRLEA 1751
Cdd:pfam10174 680 --STQQSLAEKDGHLTN 694
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1035-1146 |
4.01e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1035 EKAK-NLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLtkkEEELQAALA- 1112
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKe 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1604804600 1113 ------------RSDEETLQKNNALKQVRELQAHLAELQEDLESEK 1146
Cdd:PRK00409 582 akkeadeiikelRQLQKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
860-1117 |
4.19e-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: 48.58 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 860 LQVTRQE------EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETElfAEAEEMRVRLLSRKQ 933
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA--REMERVRLEEQERQQ 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 934 ELEEILHDLESRveeeeernqslqnekkkmqshiqdleeqldeeeaARQKLQLDKvtaeakikkMEEDILLLEDQNskfl 1013
Cdd:pfam17380 461 QVERLRQQEEER----------------------------------KRKKLELEK---------EKRDRKRAEEQR---- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 keKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaettDLQDQIveLQAQI 1093
Cdd:pfam17380 494 --RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM--RKATE 563
|
250 260
....*....|....*....|....
gi 1604804600 1094 EELKFQLTKKEEELQAALARSDEE 1117
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVESEKA 587
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
817-1232 |
4.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 817 ARKAFAKKQQQLSALKVLQRNCAAYLK-----LRHWQWWRLFTKVKPLL-QVTRQEEELQAKDEELVKVKERQLKVENEL 890
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEkleklLQLLPLYQELEALEAELaELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 891 VEMERKHQQLIEEKNILAEQlhAETELFAEAEEMRVRLLSRKQELEEI---LHDLESRVEEEEERNQSLQNEKKKMQSHI 967
Cdd:COG4717 173 AELQEELEELLEQLSLATEE--ELQDLAEELEELQQRLAELEEELEEAqeeLEELEEELEQLENELEAAALEERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 968 QDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEdqNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVknkq 1047
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALL--FLLLAREKASLGKEAEELQALPALEELEEEELEEL---- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1048 emmmvdLEERLKKEEKTRQELEKAKRKLdAETTDLQDQIVELQAQIEeLKFQLTKKEEELQAALARSDEETLQKNNALKQ 1127
Cdd:COG4717 325 ------LAALGLPPDLSPEELLELLDRI-EELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1128 VRELQAHLAELQEDLES------EKMCRSKAEKLK---RDLSEELEALKTELEDTLdttaaqqelrskreQEVAELKKAI 1198
Cdd:COG4717 397 YQELKEELEELEEQLEEllgeleELLEALDEEELEeelEELEEELEELEEELEELR--------------EELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....
gi 1604804600 1199 DEETKNHEaqIQEMRQRQATALEELSEQLEQAKR 1232
Cdd:COG4717 463 EQLEEDGE--LAELLQELEELKAELRELAEEWAA 494
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1005-1857 |
4.25e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1005 LEDQNSKFLKEKKLledrISEMTSQLTEEEEKAKNLGKVKNKQEMmmvdLEERLKKEEKTRQELEKAKRKLDAETTDLQD 1084
Cdd:TIGR01612 885 LNDYEKKFNDSKSL----INEINKSIEEEYQNINTLKKVDEYIKI----CENTKESIEKFHNKQNILKEILNKNIDTIKE 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1085 QIVELQAQIEELKFQLTKKEEELQAA---LARSDEETlqKNNALKQ-VRELQAHLAELQEDL------ESEKMCRS---K 1151
Cdd:TIGR01612 957 SNLIEKSYKDKFDNTLIDKINELDKAfkdASLNDYEA--KNNELIKyFNDLKANLGKNKENMlyhqfdEKEKATNDieqK 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1152 AEKLKRDLSEELEALKTELEDTLDttaaqqelrskreqevaELKKAIDEETKNHEAQIQEMRQRQATALEELSEQL---- 1227
Cdd:TIGR01612 1035 IEDANKNIPNIEIAIHTSIYNIID-----------------EIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLkhyn 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1228 ------EQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQefmarateaertkgelaershKLQ 1301
Cdd:TIGR01612 1098 fddfgkEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIN---------------------DLE 1156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1302 TELDNACTMLEVAEkkglkLAKEVDKLNSKLqDSEELRQEETRQKLNlstQIRQLEVDRNTLLEQQEEEEEARRNLEKql 1381
Cdd:TIGR01612 1157 DVADKAISNDDPEE-----IEKKIENIVTKI-DKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGK-- 1225
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1382 qMVQSQMFETKKKLEEDLGSMEG----LEEVKRKLQK-DVELTSQCLEEKTMAMDKMEKTKNRlqqelDDLMVDLDHQRQ 1456
Cdd:TIGR01612 1226 -LFLEKIDEEKKKSEHMIKAMEAyiedLDEIKEKSPEiENEMGIEMDIKAEMETFNISHDDDK-----DHHIISKKHDEN 1299
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1457 IvSNLEKKQKKFDQLLAEEKTISAQYAE-ERDRAEAEAREKDTKalsmarALEEALEAKEELERFN--KQLRAEMEDLMS 1533
Cdd:TIGR01612 1300 I-SDIREKSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDIN------LYLNEIANIYNILKLNkiKKIIDEVKEYTK 1372
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1534 SKDDVGKNVH-ELEKSKrTLEQQVEEmRTQLEELEDELQATEDAK---------LRLEVNMQAMKAQFDRDLQARDEQGE 1603
Cdd:TIGR01612 1373 EIEENNKNIKdELDKSE-KLIKKIKD-DINLEECKSKIESTLDDKdidecikkiKELKNHILSEESNIDTYFKNADENNE 1450
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1604 EKKrLLVKQVremeaELEDERKQRTLAVA---SKKKLEMDLNELEGQIEAANKGRDEA---VKQLRKLQAQMKDYQRELE 1677
Cdd:TIGR01612 1451 NVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVT 1524
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1678 E------ARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEA 1751
Cdd:TIGR01612 1525 EllnkysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEN 1604
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1752 ------RIAQLEEELEEEQGNMELLNDRFrkSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgTVKS 1825
Cdd:TIGR01612 1605 fenkflKISDIKKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD-ELDS 1681
|
890 900 910
....*....|....*....|....*....|..
gi 1604804600 1826 KFKASIAALEAKILQLEDQLEQEAKERAAANK 1857
Cdd:TIGR01612 1682 EIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1780-1927 |
4.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1780 QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTvkskfkASIAALEAKILQLEDQLEQEAKERAAANKIV 1859
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1860 RRTEKKLKEVMMQVEDE-RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRK---LQRELDDATE 1927
Cdd:COG3206 294 IALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1480-1945 |
4.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1480 AQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEdlmsskddvgknvhELEKSKRTLEQQVEEM 1559
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1560 RTQLEELEDELQATEDAKLRLEVNMQamKAQFDRDLQARDEQGEEKKRLLvKQVREMEAELEDERKQRTlavaskKKLEM 1639
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELE-EELEELEAELAELQEELE------ELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1640 DLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARR 1719
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1720 HAEQERDE-----LADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSA 1794
Cdd:COG4717 266 GSLLSLILtiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1795 AQKSENARQQMERQNKDLkaKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVE 1874
Cdd:COG4717 346 IEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1875 DERRhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKL--QRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:COG4717 424 ALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1307-1530 |
4.90e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1307 ACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQS 1386
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1387 QMFETKKKLEEDLGSmegLEEVKRKLQK-------DVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVS 1459
Cdd:COG4942 91 EIAELRAELEAQKEE---LAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1460 NLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMED 1530
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1136-1447 |
4.96e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1136 AELQEDLESEKMCRSKAEKLKR--DLSEELEALKTELEDTLDTTAAQQelrsKREQEVAELKKAID---EETKNHEAQIQ 1210
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALNKqkLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQLAqapAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1211 EMRQRQATALEELSEQLEQAkRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEA---QLQEFMARATEAE 1287
Cdd:PRK11281 105 ALKDDNDEETRETLSTLSLR-QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAnsqRLQQIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1288 RTKGEL-AERSHKLQTELD--NACTMLEVAEKKGlklakevdklNSKLQDSEELRQEEtrqklnLSTQIRQLEVDRNTLl 1364
Cdd:PRK11281 184 VGGKALrPSQRVLLQAEQAllNAQNDLQRKSLEG----------NTQLQDLLQKQRDY------LTARIQRLEHQLQLL- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1365 eqqeEEEEARRNL---EKQLQMVQSQmfetkkkleEDLGSMEGLEEVKRKLQKDVELtSQCLEEKTMAMDKMEKTKNRLQ 1441
Cdd:PRK11281 247 ----QEAINSKRLtlsEKTVQEAQSQ---------DEAARIQANPLVAQELEINLQL-SQRLLKATEKLNTLTQQNLRVK 312
|
....*.
gi 1604804600 1442 QELDDL 1447
Cdd:PRK11281 313 NWLDRL 318
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
877-1642 |
6.15e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 877 VKVKERQLKVENELVEMERKHQQLIEEKNILAEQLhAETELFAEAEEMRVR---LLSRKQELEEILHD--------LESR 945
Cdd:TIGR01612 605 LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQVPEHLKNKdkiYSTIKSELSKIYEDdidalyneLSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 946 VEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarqklqlDKVTaeAKIKKMEEDILLLEDQNSKFLKEKklLEDRISE 1025
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKI-------------------DKEY--DKIQNMETATVELHLSNIENKKNE--LLDIIVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1026 MTSQLTEE--EEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfQLTKK 1103
Cdd:TIGR01612 741 IKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAK-QNYDK 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1104 EEELQAALARSDEETLQKNNALKQVRElqAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDtldttaaqqEL 1183
Cdd:TIGR01612 816 SKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD---------DK 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1184 RSKREQEVAELKKAIDEETKNHEAQIQEMrqrqaTALEELSEQLEQAKRFKSNLEK--NKQSLENDnkELSCDVKTLQQA 1261
Cdd:TIGR01612 885 LNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTLKKVDEYIKICENTKESIEKfhNKQNILKE--ILNKNIDTIKES 957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1262 KTESEHKRKKLEAQLQEfmarateaertkgelaershkLQTELDNACTMLEvaekkglklakevdkLNSKLQDSEELRQE 1341
Cdd:TIGR01612 958 NLIEKSYKDKFDNTLID---------------------KINELDKAFKDAS---------------LNDYEAKNNELIKY 1001
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1342 ETRQKLNLSTQirqlevDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMegLEEVKRKLQKDVE-LTS 1420
Cdd:TIGR01612 1002 FNDLKANLGKN------KENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNI--IDEIEKEIGKNIElLNK 1073
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1421 QCLEEKTMAMDKMEKTKNRLqqelddlmvdldhqrqivsnlekKQKKFDQLLAEEktiSAQYAEERDRAEAEAREKDTKa 1500
Cdd:TIGR01612 1074 EILEEAEINITNFNEIKEKL-----------------------KHYNFDDFGKEE---NIKYADEINKIKDDIKNLDQK- 1126
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1501 lsMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDV--GKNVHELEKSKRTLEQQVEEMRTQLEELE---DELQATED 1575
Cdd:TIGR01612 1127 --IDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIENIVTKIDKKKNIYDEIKkllNEIAEIEK 1204
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1576 AKLRLEvNMQAMKAQFDRDLQARD-EQGEEKKRLLVKQVREMEAELE--DERKQRTLAVASKKKLEMDLN 1642
Cdd:TIGR01612 1205 DKTSLE-EVKGINLSYGKNLGKLFlEKIDEEKKKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIK 1273
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1205-1497 |
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 1604804600 1205 HEAQIQEmRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKtlQQAKTESEHKRKKLEaqlqefmaRAT 1284
Cdd:pfam17380 280 HQKAVSE-RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQERMAME--------RER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1285 EAERTKGELAERshklqteldnactmlEVAEKKGLKLAKEVDKLNS--KLQDSEELRQEETRQKLNLSTQIRQLEVDRNT 1362
Cdd:pfam17380 349 ELERIRQEERKR---------------ELERIRQEEIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1363 LLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEedlgsMEGLEEVKRKLQKDVELTSQCLEE---KTMAMDKMEKTKNR 1439
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERARE-----MERVRLEEQERQQQVERLRQQEEErkrKKLELEKEKRDRKR 488
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1440 LQQELDDLM-VDLDHQRQIVSNLEKKQKKFDQLLAEEKTisAQYAEERDRAEAEAREKD 1497
Cdd:pfam17380 489 AEEQRRKILeKELEERKQAMIEEERKRKLLEKEMEERQK--AIYEEERRREAEEERRKQ 545
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1127-1717 |
6.74e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1127 QVRELQAHLAELQEDLES----EKMCRSKAEKLKRDLS--EELEALKTELEDTLDTTAAQQ-ELRSKREQEVAELKKaID 1199
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQqqraERLLAEFCKRLGKNLDdeDELEQLQEELEARLESLSESVsEARERRMALRQQLEQ-LQ 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1200 EETKNHEAQIQEMRQRQAtALEELSEQLEQAkrfksnlEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEF 1279
Cdd:PRK04863 593 ARIQRLAARAPAWLAAQD-ALARLREQSGEE-------FEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1280 MARAT-EAERTKGeLAER-SHKLQTELDNACTMLEVAEKKGL------------------KLAKE-------------VD 1326
Cdd:PRK04863 665 SQPGGsEDPRLNA-LAERfGGVLLSEIYDDVSLEDAPYFSALygparhaivvpdlsdaaeQLAGLedcpedlyliegdPD 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1327 KLNSKLQDSEELRQEETRQklnlsTQIRQLEVDRntLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLgsmegle 1406
Cdd:PRK04863 744 SFDDSVFSVEELEKAVVVK-----IADRQWRYSR--FPEVPLFGRAAREKRIEQLRAEREELAERYATLSFDV------- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1407 evkRKLQKDVELTSQCL---------EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKT 1477
Cdd:PRK04863 810 ---QKLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1478 IsaqyAEER--DRAEaEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLmsskDDVGKNVHELEKSKRTLEQQ 1555
Cdd:PRK04863 887 L----ADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF----EQLKQDYQQAQQTQRDAKQQ 957
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1556 ------VEEMRTQL------EELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDEQGEEKKRLLVK------QVREME 1617
Cdd:PRK04863 958 afalteVVQRRAHFsyedaaEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQLAQYNQVLASlkssydAKRQML 1036
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1618 AELEDERKQRTL---------AVASKKKLEMDLNELEGQIEAANKGR-------DEAVKQLRKLQAQMKDYQRELEEARA 1681
Cdd:PRK04863 1037 QELKQELQDLGVpadsgaeerARARRDELHARLSANRSRRNQLEKQLtfceaemDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
650 660 670
....*....|....*....|....*....|....*...
gi 1604804600 1682 SRDEIFTQSKEN--EKKLKGLEAEILQLQEDHAASERA 1717
Cdd:PRK04863 1117 GWCAVLRLVKDNgvERRLHRRELAYLSADELRSMSDKA 1154
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1600-1754 |
7.51e-05 |
|
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: 46.21 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1600 EQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIE--------AANKGRD----EAVKQLRKLQA 1667
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaALTKGNEelarEALAEKKSLEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1668 QMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEdHAASERARRHAEQERDELadeisnSASGKSSLLEekr 1747
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKA-RLKAAKAQEAVQTSLGSL------STSSATDSFE--- 167
|
....*..
gi 1604804600 1748 RLEARIA 1754
Cdd:pfam04012 168 RIEEKIE 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
974-1117 |
8.56e-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: 46.07 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 974 LDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKaknLGKVKNKQEMMmvD 1053
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEYE--A 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1054 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEE 1117
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
912-1133 |
1.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 912 HAETELFAEAEEMRvRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLDKVTA 991
Cdd:COG3883 13 FADPQIQAKQKELS-ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 992 EAKIKKMEE-------------------DILLLEDQNSKFLKEKKLLeDRISEMTSQLTEEEEKAKNlgKVKNKQEmmmv 1052
Cdd:COG3883 78 EAEIEERREelgeraralyrsggsvsylDVLLGSESFSDFLDRLSAL-SKIADADADLLEELKADKA--ELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1053 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQ 1132
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
.
gi 1604804600 1133 A 1133
Cdd:COG3883 231 A 231
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1053-1296 |
1.10e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1053 DLEERLK-KEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKnnalkqvREL 1131
Cdd:pfam00038 29 LLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1132 QAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTEledtldttaaqqelrskREQEVAELKKAIDEETKNHE---AQ 1208
Cdd:pfam00038 102 ENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVEmdaAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1209 IQEMrqrqATALEELSEQLE-QAKRFKSNLEKNKQS-LENDNKELSCDVKTLQQAKTE-SEHKR--KKLEAQLQEFMARA 1283
Cdd:pfam00038 165 KLDL----TSALAEIRAQYEeIAAKNREEAEEWYQSkLEELQQAAARNGDALRSAKEEiTELRRtiQSLEIELQSLKKQK 240
|
250
....*....|...
gi 1604804600 1284 TEAERTKGELAER 1296
Cdd:pfam00038 241 ASLERQLAETEER 253
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1657-1871 |
1.15e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1657 EAVKQLRKLQAQMKDYQRELEEARASRDEIftqskeNEKKLKglEAEILQLQEdhaasERAR-RHAEQERDELA---DEI 1732
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEEL------EAAALQ--PGEEEELEE-----ERRRlSNAEKLREALQealEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1733 SNSASGKSSLLEE-KRRLEaRIAQleeeleeEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQME-RQN- 1809
Cdd:COG0497 236 SGGEGGALDLLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEeRLAl 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1810 -------------------KDLKAKLAELEGtvkskFKASIAALEAKILQLEDQLEQEAKE-----RAAANKIVRRTEKK 1865
Cdd:COG0497 308 lrrlarkygvtveellayaEELRAELAELEN-----SDERLEELEAELAEAEAELLEAAEKlsaarKKAAKKLEKAVTAE 382
|
....*.
gi 1604804600 1866 LKEVMM 1871
Cdd:COG0497 383 LADLGM 388
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1093-1238 |
1.17e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1093 IEELKFQLTKKEEELqaalarsdEETLQKNNALKqvRELQAHLAELQEDLEsekmcrsKAEKLKRDLSEELEALKTELED 1172
Cdd:PRK00409 504 IEEAKKLIGEDKEKL--------NELIASLEELE--RELEQKAEEAEALLK-------EAEKLKEELEEKKEKLQEEEDK 566
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 1173 TLdttaaqQELRSKREQEVAELKKAIDE------------ETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLE 1238
Cdd:PRK00409 567 LL------EEAEKEAQQAIKEAKKEADEiikelrqlqkggYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
864-1252 |
1.26e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 864 RQEEELQAKDEELVKVKERQLKVENELVEMERKHQQL------IEEKNILAEQLHAETE-LFAEAEEMRVRLLSRKQELE 936
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksIESLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 937 EILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDillledqnskFLKEK 1016
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINH----------YNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1017 KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVD-LEERLKKEEKTRQELEKAKRKLdAETTDLQDQIVELQAQIEE 1095
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKS 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1096 LKFQL--TKKEEELQAALARS--DEETLQK--NNALKQVRELQAHLAELQEDLESEKmcrSKAEKLKRDLSEELEALKTE 1169
Cdd:PRK01156 558 LKLEDldSKRTSWLNALAVISliDIETNRSrsNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1170 LEDTLDTTAAQQELRSKRE---QEVAElKKAIDEETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLEN 1246
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDnykKQIAE-IDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRARLESTIEILRT 709
|
....*.
gi 1604804600 1247 DNKELS 1252
Cdd:PRK01156 710 RINELS 715
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
866-1200 |
1.39e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.77 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 866 EEELQAKDEELVKVkerqLKVENELVEMERKHQQLIEE-KNILAE---QLHAETELFAEAEEmrvrllsrkqELEEILHD 941
Cdd:pfam06160 92 EELLDDIEEDIKQI----LEELDELLESEEKNREEVEElKDKYRElrkTLLANRFSYGPAID----------ELEKQLAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 942 LESRVEEEEERNQSLQNEK-----KKMQSHIQDLEEQLDEEEAARQKL------QLDKVtaEAKIKKMEEDILLLEDQNs 1010
Cdd:pfam06160 158 IEEEFSQFEELTESGDYLEarevlEKLEEETDALEELMEDIPPLYEELktelpdQLEEL--KEGYREMEEEGYALEHLN- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1011 kFLKEKKLLEDRISEMTSQL--TEEEEKAKNLGKVKNKQEMMMVDLEerlkKEEKTRQELEKAKRKLDAETTDLQDQIVE 1088
Cdd:pfam06160 235 -VDKEIQQLEEQLEENLALLenLELDEAEEALEEIEERIDQLYDLLE----KEVDAKKYVEKNLPEIEDYLEHAEEQNKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1089 LQAQIEELK--FQLTKKEEELQAALArsdeetlqknnalKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEAL 1166
Cdd:pfam06160 310 LKEELERVQqsYTLNENELERVRGLE-------------KQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEI 376
|
330 340 350
....*....|....*....|....*....|....
gi 1604804600 1167 KTELEDTLDTTAAQQELRSKREQEVAELKKAIDE 1200
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDELEAREKLDEFKLELRE 410
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1320-1940 |
1.40e-04 |
|
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: 47.02 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1320 KLAKEVDKLNS-KLQDSEELRQEETRQKLNlstqirqlevdrntlleqqeeeeeaRRNLEKQLQMVQSQMFETKKKleeD 1398
Cdd:pfam05483 82 KLYKEAEKIKKwKVSIEAELKQKENKLQEN-------------------------RKIIEAQRKAIQELQFENEKV---S 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1399 LGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDhqrqIVSNLEKKQKKFDQL--LAEEK 1476
Cdd:pfam05483 134 LKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMD----LNNNIEKMILAFEELrvQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1477 TISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKqlraeMEDLMSSKDDVGKNVHELEKSKRTLEQQV 1556
Cdd:pfam05483 210 RLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK-----MKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1557 EEMRTQLEELEDELqatEDAKLRLEVNMQAMKAqFDRDLQArdeqgeeKKRLLVKQVREMEAELEDERKQRTLAVASKKK 1636
Cdd:pfam05483 285 KELIEKKDHLTKEL---EDIKMSLQRSMSTQKA-LEEDLQI-------ATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1637 LEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEAR-----------------ASRDEIFTQSKENEK---K 1696
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeveleelkkilAEDEKLLDEKKQFEKiaeE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1697 LKGLEAEILQLQEDHaaserarrhaEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRK 1776
Cdd:pfam05483 434 LKGKEQELIFLLQAR----------EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1777 SNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEG---TVKSKFKASIAALEAKILQLEDQLEQEAKERA 1853
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDeleSVREEFIQKGDEVKCKLDKSEENARSIEYEVL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1854 AANKIVRRTEKKLKEVMMQVEDERRHADQYKEQ----MEKANSRMKQLKRQLEEAEEEATRANATRRKL-------QREL 1922
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalKKKGSAENKQLNAYEIKVNKLELELASAKQKFeeiidnyQKEI 663
|
650
....*....|....*...
gi 1604804600 1923 DDATEASEGLTREVSSLK 1940
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAK 681
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1315-1898 |
1.92e-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: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1315 EKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEvdrntlleqqEEEEEARRNLEKQLQMVQSQ---MFET 1391
Cdd:pfam05557 19 KQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLE----------KREAEAEEALREQAELNRLKkkyLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1392 KKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL 1471
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1472 LAEEKTISAQYAEERDRAEaEAREKDTKALSMARALEEAleakeelerfnKQLRAEMEDLMSSKDDVGKNVHELEKSKRT 1551
Cdd:pfam05557 169 EQRIKELEFEIQSQEQDSE-IVKNSKSELARIPELEKEL-----------ERLREHNKHLNENIENKLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1552 LEQQvEEMRTQLEELEDELQATEdAKLRLEVNMQAMKAQFDR---DLQARDEQGEEKKRLLVKQVREMEAELEDERKQRT 1628
Cdd:pfam05557 237 LERE-EKYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1629 LavaskkkLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARA---SRDEIFTQSKENEKKLKGLEAEIL 1705
Cdd:pfam05557 315 E-------LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1706 QLQEDHAASERARRHAEQERDELadeisnsASGKSSLLEEKRRLEARIAQleeeleeeqgnmELLNDRfRKSNIQVDNLN 1785
Cdd:pfam05557 388 MTQKMQAHNEEMEAQLSVAEEEL-------GGYKQQAQTLERELQALRQQ------------ESLADP-SYSKEEVDSLR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1786 TELagersaaQKSENARQQMERQNKDLKAKLA--ELEGTVK-SKFK----ASIAALEAKiLQLEDQLEQEAKERAAANKI 1858
Cdd:pfam05557 448 RKL-------ETLELERQRLREQKNELEMELErrCLQGDYDpKKTKvlhlSMNPAAEAY-QQRKNQLEKLQAEIERLKRL 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1604804600 1859 VRRTEKKLKEV----MMQVEDERRHADQYKEQMEKANSRMKQLK 1898
Cdd:pfam05557 520 LKKLEDDLEQVlrlpETTSTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
990-1228 |
2.00e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.29 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 990 TAEAKIKKMEEDILLLEDQNSKFLKEKKL-LEDRISEMTSQLTEEEEK--------------AKNLGKVKNKQEMMMVDL 1054
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEEEAAPPLLDaAPETPPKLPEHLDNVEEKvekaqslaklvdqyKELVASERIVFQQELVSI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1055 EERLKKEEKTRQELEKAKrkLDAETTDLQDQIVELQAQIEELKfqlTKKEEELQAALARSDEEtlQKNNALKQVRELQAH 1134
Cdd:pfam09731 267 FPDIIPVLKEDNLLSNDD--LNSLIAHAHREIDQLSKKLAELK---KREEKHIERALEKQKEE--LDKLAEELSARLEEV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1135 LA--ELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDEETKNHEAQIQEM 1212
Cdd:pfam09731 340 RAadEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNEL 418
|
250
....*....|....*.
gi 1604804600 1213 rqrqATALEELSEQLE 1228
Cdd:pfam09731 419 ----LANLKGLEKATS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1522-1934 |
2.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1522 KQLRAEMEDLMSSKDDVGK--NVHELEKSKRTLEQQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMKAQFDRDLQ 1596
Cdd:COG4717 105 EELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1597 ARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRD-EAVKQLRKLQAQMKDYQRE 1675
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1676 LEEARASRDEI-----------FTQSKENEKKLKGLEAEILQLQEDHAASERarrhAEQERDELADEISNSASGKSSLLE 1744
Cdd:COG4717 265 GGSLLSLILTIagvlflvlgllALLFLLLAREKASLGKEAEELQALPALEEL----EEEELEELLAALGLPPDLSPEELL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1745 EKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNkDLKAKLAELEGTVK 1824
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE-ELEEQLEELLGELE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1825 SKFKA-SIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEE 1903
Cdd:COG4717 420 ELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
410 420 430
....*....|....*....|....*....|.
gi 1604804600 1904 AEEEATRANATRRKLQRELDDATEASEGLTR 1934
Cdd:COG4717 500 ELLEEAREEYREERLPPVLERASEYFSRLTD 530
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1632-1836 |
2.25e-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: 45.44 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1632 ASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQ--SKENEKKLKGLEAEILQLQE 1709
Cdd:cd22656 114 EAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKEIKDLQKELEKLNE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1710 DHAASerarrhAEQERDELADEISNsasgksslLEEKRRLEARIaqleeeleeeQGNMELLNDrfrksniQVDNLNTELA 1789
Cdd:cd22656 194 EYAAK------LKAKIDELKALIAD--------DEAKLAAALRL----------IADLTAADT-------DLDNLLALIG 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1604804600 1790 GERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEA 1836
Cdd:cd22656 243 PAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1465-1733 |
2.38e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1465 QKKFDQLLAEEKTISAQyaeERDRAEAEAREKDTKALSMARALEEALEAKEELERfnKQLRAEMEDLMSSKDDVGKNVHE 1544
Cdd:TIGR00606 172 KQKFDEIFSATRYIKAL---ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1545 LEKSKRTLeQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDER 1624
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1625 KQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLK--GLEA 1702
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVieRQED 405
|
250 260 270
....*....|....*....|....*....|.
gi 1604804600 1703 EILQLQEDHAASERARRHAEQERDELADEIS 1733
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
855-1175 |
2.54e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 855 KVKPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLH-AETELFAEAEEMRVRLLSRKQ 933
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 934 ELEEIlhdlesrveeeeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDqnskfL 1013
Cdd:PTZ00121 1676 KAEEA---------------KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE-----A 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEkTRQELEKAKRKLDAETTDLQDQIVELQAQI 1093
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-LDEEDEKRRMEVDKKIKDIFDNFANIIEGG 1814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1094 EELKFQLTKKEEELQAALarsDEETLQKNNALKQVRELQAHL----AELQEDLESEKMCRSKAEKLKRDLSEELEALKTE 1169
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAI---KEVADSKNMQLEEADAFEKHKfnknNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
....*.
gi 1604804600 1170 LEDTLD 1175
Cdd:PTZ00121 1892 KIDKDD 1897
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1037-1283 |
2.98e-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: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1037 AKNLGKVKNKQEMMMVDLEERLKkEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQaalarsde 1116
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLA-DATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTE-------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1117 etlqknnalKQVRELQAHLAELQEDLESEkmcrskaekLKRDLSEELEALKTELEDtldttaAQQELRSKREQEVAELKK 1196
Cdd:cd22656 153 ---------KDQTALETLEKALKDLLTDE---------GGAIARKEIKDLQKELEK------LNEEYAAKLKAKIDELKA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1197 AI--DEETKNHEAQIQEMRQRQATALEELSEQLEQAKR-----------FKSNLEKNKQSLENDNKELSCDVKTLQQAKt 1263
Cdd:cd22656 209 LIadDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPaleklqgawqaIATDLDSLKDLLEDDISKIPAAILAKLELE- 287
|
250 260
....*....|....*....|
gi 1604804600 1264 ESEHKRKKLEAQLQEFMARA 1283
Cdd:cd22656 288 KAIEKWNELAEKADKFRQNA 307
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1018-1199 |
3.00e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 43.79 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1018 LLEDRISEMTSQLTEEEEKAKNLGK-VKNKQEMMMVDLEERLKKE-----EKTRQELEKAKRKLDAETTDLQDQiveLQA 1091
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQeLVDRLEKETEALRERLQKDleevrAKLEPYLEELQAKLGQNVEELRQR---LEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1092 QIEELKFQLTKKEEELQAALARSDEETlqKNNALKQVRELQAHLAELQEDLesekmcRSKAEKLKRDLSEELEALKTELE 1171
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLAPYGEEL--RERLEQNVDALRARLAPYAEEL------RQKLAERLEELKESLAPYAEEVQ 149
|
170 180
....*....|....*....|....*...
gi 1604804600 1172 DTLDTTAaqQELRSKREQEVAELKKAID 1199
Cdd:pfam01442 150 AQLSQRL--QELREKLEPQAEDLREKLD 175
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1155-1325 |
3.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1155 LKRDLSEELEALKTELEDTLDttAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFK 1234
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1235 SNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMA-RATEA---------ERTKGELAERSHKLQTEl 1304
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEEAkeillekveEEARHEAAVLIKEIEEE- 181
|
170 180
....*....|....*....|.
gi 1604804600 1305 dnactmlevAEKKGLKLAKEV 1325
Cdd:PRK12704 182 ---------AKEEADKKAKEI 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1612-1802 |
4.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1612 QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSK 1691
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1692 ENEKKLKGLEA--------------------------EILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEE 1745
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1746 KRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENAR 1802
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1099-1361 |
4.46e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1099 QLTKKEEELQAALARSDEETlqknnalkqVRELQAHLAELQEDLESEKmcRSKA--------EKLKRDLSEELEALKTEL 1170
Cdd:PRK10929 27 QITQELEQAKAAKTPAQAEI---------VEALQSALNWLEERKGSLE--RAKQyqqvidnfPKLSAELRQQLNNERDEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1171 EdTLDTTAAQQELrskrEQEVAELKKAIDEETknHEAQIQEMRQRQ-ATALEELSEQLEQAKRFKSNLEKNKQSLENDNK 1249
Cdd:PRK10929 96 R-SVPPNMSTDAL----EQEILQVSSQLLEKS--RQAQQEQDRAREiSDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1250 ELSCDVKTLQQAKTeSEHKRKKLEAQLQEFMAR-ATEAERTKGELAERSHklqTELDnactmlevAEKKGLKlakevDKL 1328
Cdd:PRK10929 169 PLAQAQLTALQAES-AALKALVDELELAQLSANnRQELARLRSELAKKRS---QQLD--------AYLQALR-----NQL 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1604804600 1329 NSKLQDSEELRQEETR----QKLNLSTQI-RQLEVDRN 1361
Cdd:PRK10929 232 NSQRQREAERALESTEllaeQSGDLPKSIvAQFKINRE 269
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1046 |
4.60e-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: 44.75 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 861 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAE----------AEEMRV---- 926
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrQPPLALllsp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 927 ----RLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDI 1002
Cdd:COG4942 129 edflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1604804600 1003 LLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNK 1046
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
859-1317 |
4.72e-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: 45.21 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 859 LLQVTRQEEELQAKDEELVKVKERQLKVENEL-----------VEMERKHQQLIEEKNILAEqlhAETELFAEA------ 921
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAgtllhf 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 922 --------EEMRVRLLSRKQELEEILHdlESRVEEEEERNQSLQNEKKKMQS-HIQDLEEQLDEEEAARQKLQLDKVTAE 992
Cdd:pfam12128 540 lrkeapdwEQSIGKVISPELLHRTDLD--PEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 993 AKIKKMEEDILLLEDQnskflkekklLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVD----LEERLKKEEKTRQEL 1068
Cdd:pfam12128 618 EKQAAAEEQLVQANGE----------LEKASREETFARTALKNARLDLRRLFDEKQSEKDKknkaLAERKDSANERLNSL 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1069 EKAKRKLDaetTDLQDQIVELQAQIEELKFQLTKK----EEELQAALARSDEETLQKNNALKqvrelqAHLAELQEDLES 1144
Cdd:pfam12128 688 EAQLKQLD---KKHQAWLEEQKEQKREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKR 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1145 EKMCRSKAEKLKRDLSEELEALKTELEDTldttaaqqelrSKREQEVAELKKAIDE----ETKNHEAQIQEMRQRQATAL 1220
Cdd:pfam12128 759 DLASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQ 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1221 EELSEQLEQAKRFKSNLEKNKQSLENdnkelscdvktlQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKL 1300
Cdd:pfam12128 828 QQLARLIADTKLRRAKLEMERKASEK------------QQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQL 895
|
490
....*....|....*..
gi 1604804600 1301 QTELDNACTMLEVAEKK 1317
Cdd:pfam12128 896 EDLKLKRDYLSESVKKY 912
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1081-1701 |
5.21e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1081 DLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLS 1160
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1161 EELEALK--TELEDTLDTTAAQQELRSKRE-QEVAELKKAID---EETKNHEAQIQ--EMRQRQATALEELSEQLEQAKR 1232
Cdd:PRK01156 267 MELEKNNyyKELEERHMKIINDPVYKNRNYiNDYFKYKNDIEnkkQILSNIDAEINkyHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1233 FKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDnactmle 1312
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ------- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1313 vaekkglKLAKEVDKLNSKLqDSEELRQEETRQKLNLSTQIRQLEVDRNTLleqqeeeeearrnLEKQLQMVQSQMFETK 1392
Cdd:PRK01156 420 -------DISSKVSSLNQRI-RALRENLDELSRNMEMLNGQSVCPVCGTTL-------------GEEKSNHIINHYNEKK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1393 KKLEEDLGSMEglEEVKRKLQKDVELTSQcleEKTMAMDKMEKTKNRLQQeLDDLMVDLDHQRQIVSNLEKKQKKFDQLL 1472
Cdd:PRK01156 479 SRLEEKIREIE--IEVKDIDEKIVDLKKR---KEYLESEEINKSINEYNK-IESARADLEDIKIKINELKDKHDKYEEIK 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1473 AEEKTISAQYAEERdraeaeaREKDTKALSMARAleealeakeelerfnkqlrAEMEDLMSSKDDVGKNVHELEKSKRTL 1552
Cdd:PRK01156 553 NRYKSLKLEDLDSK-------RTSWLNALAVISL-------------------IDIETNRSRSNEIKKQLNDLESRLQEI 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1553 EQQVEEMRT----QLEELEDELQATEDAKLRLEVNMQAMkaqfdrdlqardeqgeEKKRLLVKQVREMEAELEDERKQRT 1628
Cdd:PRK01156 607 EIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILI----------------EKLRGKIDNYKKQIAEIDSIIPDLK 670
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1629 LAVASKKKLEMDLNELEGQIEAANKGRDEavkqLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLE 1701
Cdd:PRK01156 671 EITSRINDIEDNLKKSRKALDDAKANRAR----LESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLK 739
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1033-1305 |
5.42e-04 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 44.19 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1033 EEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfqltkkeEELQAALA 1112
Cdd:pfam09311 15 QEQEAETRDQVKKLQEMLR-QANDQLEKTMKDKKELEDKMNQLSEETSNQVSTLAKRNQKSETLL-------DELQQAFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1113 RSDEETLQKNNALKQVRELQA-HLAELQEDLESEKMCRSKAEKLKR-------DLSEELEALKTEL-EDTLDTTAAQQEL 1183
Cdd:pfam09311 87 QAKRNFQDQLAVLMDSREQVSdELVRLQKDNESLQGKHSLHVSLQQaekfdmpDTVQELQELVLKYrEELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1184 RSKREQEVAELKKAIDEEtKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKT 1263
Cdd:pfam09311 167 EEKLKAEILFLKEQIQAE-QCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQLEDLQTTKG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1604804600 1264 EsehkrkkLEAQLQEFMARATEAERTKGELAERSHKLQTELD 1305
Cdd:pfam09311 246 S-------LETQLKKETNEKAAVEQLVFEEKNKAQRLQTELD 280
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1675-1892 |
5.83e-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: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1675 ELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISnsasgksslleekrRLEARIA 1754
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1755 QLeeeleeeqgnMELLNDRFR---KSNIQVDNLN--------TELAGERSAAQKSENARQQMERQNKDLKAKLAELegtv 1823
Cdd:COG3883 83 ER----------REELGERARalyRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAK---- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804600 1824 KSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANS 1892
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1279-1505 |
6.33e-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: 44.37 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1279 FMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEV 1358
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1359 DRNTLleqQEEEEEARRNLEKQLQMVQSQMFETKKKLeedLGSMEGLEEVKRKLQKDVELTSQCLEEktmaMDKMEKTKN 1438
Cdd:COG4942 91 EIAEL---RAELEAQKEELAELLRALYRLGRQPPLAL---LLSPEDFLDAVRRLQYLKYLAPARREQ----AEELRADLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1439 RLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMAR 1505
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1592-1933 |
6.50e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1592 DRDLQARDEQGEEKKRLLVKQVR--EMEAELED-ERKQRTL----------------AVASKKKLEM---DLNELEGQIE 1649
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRlvEMARELEElSARESDLeqdyqaasdhlnlvqtALRQQEKIERyqeDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1650 AANKGRDEAVKQLRKLQAQmkdyqreLEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARR-------HAE 1722
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcglpdlTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1723 QERDELADEISNSASGKSSLLEEKRRLeaRIAQLEEeleeeqgnmellnDRFRKSNIQVdnlnTELAGERSAAQKSENAR 1802
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQKL--SVADAAR-------------RQFEKAYELV----CKIAGEVERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1803 QQMeRQNKDLKAKLAELEgtvkskfkasiaALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMmQVEDERRHADQ 1882
Cdd:COG3096 499 ELL-RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEELLAELEA 564
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1883 YKEQMEkansrmkqlkrqleeaeEEATRANATRRKLQRELDDATEASEGLT 1933
Cdd:COG3096 565 QLEELE-----------------EQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1016-1167 |
7.35e-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: 43.85 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1016 KKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD----AETTDLQDQIVELQA 1091
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1092 QIEELKFQLTKKEEELQAAlarsdEETLQKNNALKQvrELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALK 1167
Cdd:smart00787 219 EIMIKVKKLEELEEELQEL-----ESKIEDLTNKKS--ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1058-1324 |
7.52e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1058 LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALArsDEETLQKNNAlkqvrELQAHLAE 1137
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVR--EKTSLSASVA-----SLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1138 LQE--DLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ-----------EVAELKKAIDEETKN 1204
Cdd:pfam15905 134 LTRvnELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQvtqknlehskgKVAQLEEKLVSTEKE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1205 HEAQIQEMrQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFmarAT 1284
Cdd:pfam15905 214 KIEEKSET-EKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL---ES 289
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1604804600 1285 EAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKE 1324
Cdd:pfam15905 290 EKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1498-1671 |
7.60e-04 |
|
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: 44.63 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1498 TKALSMARALEEALEAKEELERFNKQ-----LRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1572
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQREeeleeLQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1573 TEDAKLRL---EVNMQAMKAQFD---RDLQARDEQGEEKKRLLVKQVRemeaELEDERKQRTLavASKKKLE--MDLNEL 1644
Cdd:pfam05667 389 KKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYR----ALKEAKSNKED--ESQRKLEeiKELREK 462
|
170 180
....*....|....*....|....*..
gi 1604804600 1645 EGQIEAANKGRDEAVKQlrkLQAQMKD 1671
Cdd:pfam05667 463 IKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1415-1634 |
7.62e-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: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1415 DVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERDRAEAEA 1493
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1494 REKDT----KALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1569
Cdd:COG3883 97 RSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804600 1570 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASK 1634
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1084-1329 |
7.77e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1084 DQIV---ELQAQIEELKFQLTKKEeelQAALARSDEETLQKNNA-LKQVRELQ-AHLAELQEDLES-EKMCRSKAEKLKR 1157
Cdd:NF012221 1532 DNVVatsESSQQADAVSKHAKQDD---AAQNALADKERAEADRQrLEQEKQQQlAAISGSQSQLEStDQNALETNGQAQR 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1158 D-LSEELEALKTELE------DTLDTTAAQQELRSK--REQEVAELKKAIDEE---TKNH-EAQIQEMRQRQATALEELS 1224
Cdd:NF012221 1609 DaILEESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1225 EQLEQAKRFKSNLEKNKQSLENDnkelscdvktLQQAKTESEhkRKKLEAQLQEfmARATEAErTKGELAERSHKLQTEL 1304
Cdd:NF012221 1689 DAVAKSEAGVAQGEQNQANAEQD----------IDDAKADAE--KRKDDALAKQ--NEAQQAE-SDANAAANDAQSRGEQ 1753
|
250 260
....*....|....*....|....*....
gi 1604804600 1305 DNACTMLEV----AEKKGLKLaKEVDKLN 1329
Cdd:NF012221 1754 DASAAENKAnqaqADAKGAKQ-DESDKPN 1781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
855-1255 |
8.18e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 855 KVKPLLQVTRQEEELQA---KDEELVKVKERQLKVENELVEMERKHQ----QLIEEKNILAEQLHAETELFAEAEEMRVR 927
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMalrKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 928 LLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQshiqdleEQLDEEEAARQKLQLDKVTAEAKiKKMEEDILLLED 1007
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-------EAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAE 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1008 QNSKFLKEKKLLEDRISEMTSQLTEEEEKaknlgkvKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDqiv 1087
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEED-------KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--- 1783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1088 ELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQahLAELQEDLESEKMCRSKAEKLKRDLSEElEALK 1167
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME--DSAIKEVADSKNMQLEEADAFEKHKFNK-NNEN 1860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1168 TELEDTLDTTAAQQELRSKREQEVAELK--KAIDEETKNHEAQIQEMRQRQAtalEELSEQLEQAKRFKSNLEKNKQSLE 1245
Cdd:PTZ00121 1861 GEDGNKEADFNKEKDLKEDDEEEIEEADeiEKIDKDDIEREIPNNNMAGKNN---DIIDDKLDKDEYIKRDAEETREEII 1937
|
410
....*....|
gi 1604804600 1246 NDNKELSCDV 1255
Cdd:PTZ00121 1938 KISKKDMCIN 1947
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1078-1224 |
8.26e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1078 ETTDLQDQIVELQAQIEELKFQLTKKE---EELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEK 1154
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 1155 L-------KRDLsEELEALKTELEDTLDTTAAQQE-LRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELS 1224
Cdd:pfam00529 132 LapiggisRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
932-1125 |
8.29e-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: 42.99 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 932 KQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQ--N 1009
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1010 SKFLKEKKLLEDRISEMTSQLTEEEEKAKNLgkvknkqemmMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVEL 1089
Cdd:COG1579 85 VRNNKEYEALQKEIESLKRRISDLEDEILEL----------MERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1604804600 1090 QAQIEELKFQLTKKEEELQAALARSDEETLQKNNAL 1125
Cdd:COG1579 155 EAELEELEAEREELAAKIPPELLALYERIRKRKNGL 190
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
993-1229 |
8.31e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 993 AKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTS-QLTEEEEkaknlgkvknkqemmmVDLEE---RLKKEEKTRQEL 1068
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELEAaALQPGEE----------------EELEEerrRLSNAEKLREAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1069 EKAKRKLDAETTDLQDQIVELQAQIEELkfqlTKKEEELQAALARSDEetlqknnALKQVRELQAHLAELQEDLES---- 1144
Cdd:COG0497 229 QEALEALSGGEGGALDLLGQALRALERL----AEYDPSLAELAERLES-------ALIELEEAASELRRYLDSLEFdper 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1145 -----EKMcrSKAEKLKR---DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETknheAQIQEMRQRQ 1216
Cdd:COG0497 298 leeveERL--ALLRRLARkygVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----EKLSAARKKA 371
|
250
....*....|....
gi 1604804600 1217 ATALEE-LSEQLEQ 1229
Cdd:COG0497 372 AKKLEKaVTAELAD 385
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1061-1338 |
8.80e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1061 EEKTRQELEKAKRKLDAETTD------LQDQIVELQAQIEE-----------LKFQLTKKEEELQAALARSD--EETLQK 1121
Cdd:PLN03229 457 ELALNEMIEKLKKEIDLEYTEaviamgLQERLENLREEFSKansqdqlmhpvLMEKIEKLKDEFNKRLSRAPnyLSLKYK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1122 NNALKQVRELQAhlaelqedlESEKmcRSKAEKLKR-------------DLSEELEALKTELEDTLDTTAAqqELRSKRE 1188
Cdd:PLN03229 537 LDMLNEFSRAKA---------LSEK--KSKAEKLKAeinkkfkevmdrpEIKEKMEALKAEVASSGASSGD--ELDDDLK 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1189 QEVAELKKAIDEET----KNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQ--------SLENDNKELSCDV- 1255
Cdd:PLN03229 604 EKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKiervirssDLKSKIELLKLEVa 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1256 KTLQQAKTESEHKRKKLEAQLQEFMARATEAErtkgELAERSHKLQTELDNActmLEVAEKKGLKLAKEVDKLNSKLQDS 1335
Cdd:PLN03229 684 KASKTPDVTEKEKIEALEQQIKQKIAEALNSS----ELKEKFEELEAELAAA---RETAAESNGSLKNDDDKEEDSKEDG 756
|
...
gi 1604804600 1336 EEL 1338
Cdd:PLN03229 757 SRV 759
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1610-1899 |
9.37e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1610 VKQVREMEAELEDERKQRTLAVASKKKLEMDLNE----LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDE 1685
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEelkeLAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1686 IFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNsasgksslLEEKRRLEARIAQLEEELEEEQG 1765
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLS--------PEEEKELVEKIKELEKELEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1766 NMELlndrfrksNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKsKFKASIAALEAKILQLEDQL 1845
Cdd:COG1340 155 ALEK--------NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1846 EQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQyKEQMEKANSRMKQLKR 1899
Cdd:COG1340 226 DELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1411-1891 |
9.61e-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: 44.19 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1411 KLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAE 1490
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1491 AEARekdtkalsmaraleealeakeeLERFNKQLRAEMEDLMSSkddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1570
Cdd:TIGR00618 254 EQLK----------------------KQQLLKQLRARIEELRAQ-----EAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1571 QATEDAKLRLEVNMQAM-KAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKK---LEMDLNELEG 1646
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtLTQHIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1647 QIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERD 1726
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1727 ELADEISNSASGKSSLLEEKRRLEARIAqleeELEEEQGNMELLNDRFRKSNIQVDNLNtELAGERSAAQKSENARQQME 1806
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPARQDID-NPGPLTRRMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1807 RQNKDLKAKLAELegtvkskfKASIAALEAKILQLEDQLEQEAKER----AAANKIVRRTEKKLKEVMMQVEDERRHADQ 1882
Cdd:TIGR00618 542 TSEEDVYHQLTSE--------RKQRASLKEQMQEIQQSFSILTQCDnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
....*....
gi 1604804600 1883 YKEQMEKAN 1891
Cdd:TIGR00618 614 QHALLRKLQ 622
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1007-1797 |
9.76e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1007 DQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKqemMMVDLEERLKKeeKTRQELE--------------KAK 1072
Cdd:TIGR01612 486 DENSKQDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNI---IGFDIDQNIKA--KLYKEIEaglkesyelaknwkKLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1073 RKLDAETTDLQDQIVELQAQIEELKFQLTKKEEE------LQAALARSDEETLQKNNALKQVRELQ-------AHLAELQ 1139
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinkLKLELKEKIKNISDKNEYIKKAIDLKkiiennnAYIDELA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1140 --------EDLES-EKMCRSKAEKLKRDLSEELEALKTEL-----EDTLDTT---AAQQELRSKREQEVAELKKAIDEET 1202
Cdd:TIGR01612 641 kispyqvpEHLKNkDKIYSTIKSELSKIYEDDIDALYNELssivkENAIDNTedkAKLDDLKSKIDKEYDKIQNMETATV 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1203 KNHEAQIQEMRQRQATALEELSEQLEqaKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLeAQLQEFMAR 1282
Cdd:TIGR01612 721 ELHLSNIENKKNELLDIIVEIKKHIH--GEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKI-SEIKNHYND 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1283 ATEAERTKGELAERSHKLQTELDNACTMLE------VAEKKGLK--LAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIR 1354
Cdd:TIGR01612 798 QINIDNIKDEDAKQNYDKSKEYIKTISIKEdeifkiINEMKFMKddFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIK 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1355 QlEVDRNTLleqqeeeeearRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLqKDVELTSQCLEEktmAMDKME 1434
Cdd:TIGR01612 878 A-EISDDKL-----------NDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEK---FHNKQN 941
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1435 KTKNRLQQELDDLmvdldhqrQIVSNLEKKQK-KFDQLLAEEKTISAQYAEERDRAEAEAREKD-TKALSMARALEEALE 1512
Cdd:TIGR01612 942 ILKEILNKNIDTI--------KESNLIEKSYKdKFDNTLIDKINELDKAFKDASLNDYEAKNNElIKYFNDLKANLGKNK 1013
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1513 AKEELERFNKQLRAeMEDLMSSKDDVGKNVHELEKSKRT------------LEQQVEEMRTQ-LEELE------------ 1567
Cdd:TIGR01612 1014 ENMLYHQFDEKEKA-TNDIEQKIEDANKNIPNIEIAIHTsiyniideiekeIGKNIELLNKEiLEEAEinitnfneikek 1092
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1568 ------DELQATEDAKLRLEVN-----MQAMKAQFDRDLQARdeqgEEKKRLLVKQVREMEAELEDERK--QRTLAVASK 1634
Cdd:TIGR01612 1093 lkhynfDDFGKEENIKYADEINkikddIKNLDQKIDHHIKAL----EEIKKKSENYIDEIKAQINDLEDvaDKAISNDDP 1168
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1635 KKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDyQRELEEARA-------SRDEIFTQSKENEKK-----LKGLEA 1702
Cdd:TIGR01612 1169 EEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEVKGinlsygkNLGKLFLEKIDEEKKksehmIKAMEA 1247
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1703 EILQLQEDHAASERARRHAEQERDELAD----EISNSASGKSSLLEEKrrleariaQLEEELEEEQGNMELLNDRFRKSN 1778
Cdd:TIGR01612 1248 YIEDLDEIKEKSPEIENEMGIEMDIKAEmetfNISHDDDKDHHIISKK--------HDENISDIREKSLKIIEDFSEESD 1319
|
890
....*....|....*....
gi 1604804600 1779 IqvDNLNTELAGERSAAQK 1797
Cdd:TIGR01612 1320 I--NDIKKELQKNLLDAQK 1336
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
996-1302 |
1.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 996 KKMEEDILLLedqnSKFLKEKKLLEDRISEMTSQLTEeeekaknlgkvknkQEMMMVDLEERLKKEEKTRQELEKakrKL 1075
Cdd:PHA02562 153 RKLVEDLLDI----SVLSEMDKLNKDKIRELNQQIQT--------------LDMKIDHIQQQIKTYNKNIEEQRK---KN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1076 DAETTDLQDQIVELQAQIEELKFQLtkkeEELQAALARSDEETLQKNNALKQVRELQAhlaelqeDLESEKMCRSKAEKL 1155
Cdd:PHA02562 212 GENIARKQNKYDELVEEAKTIKAEI----EELTDELLNLVMDIEDPSAALNKLNTAAA-------KIKSKIEQFQKVIKM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1156 KRDlSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDEETKnheaQIQEMRQRqataLEELSEQLEQAKRFKS 1235
Cdd:PHA02562 281 YEK-GGVCPTCTQQISEG-------PDRITKIKDKLKELQHSLEKLDT----AIDELEEI----MDEFNEQSKKLLELKN 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1236 NLEKNKQSLENDNKElscdVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQT 1302
Cdd:PHA02562 345 KISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1544-1945 |
1.01e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1544 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmQAMKAQFDRDLQARDEQGEEKKRLL--VKQVREMEAELE 1621
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRarIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1622 DERKQRTLAVASKKKLEMD--LNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQR-ELEEARASRDEIFTQSKENEKKLK 1698
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIkaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqQSSIEEQRRLLQTLHSQEIHIRDA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1699 GLEAEILQLQEDHAASERARRHAEQERDELADEISNSASgksSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSN 1778
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC---KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1779 IQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgtVKSKFKASIAALEAKILQLEDQLEQEAKERA----- 1853
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE--QIHLQETRKKAVVLARLLELQEEPCPLCGSCihpnp 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1854 ----------------AANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQleeaeeeATRANATRRK 1917
Cdd:TIGR00618 516 arqdidnpgpltrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPN 588
|
410 420
....*....|....*....|....*...
gi 1604804600 1918 LQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1019-1103 |
1.11e-03 |
|
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467481 [Multi-domain] Cd Length: 103 Bit Score: 40.22 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1019 LEDRISEMTSQLTEEEEKAKNLGKVKNkqEMMMVDLEERLK----------KEEKTRQELEKAKRKLDAETTDLQDQIVE 1088
Cdd:cd23165 11 LNARLHELKEELKAKKKELENLEDASD--ELELADDDEPVPykigevfvhlSLEEAQERLEKAKEELEEEIEKLEEEIDE 88
|
90
....*....|....*
gi 1604804600 1089 LQAQIEELKFQLTKK 1103
Cdd:cd23165 89 IEEEMKELKVQLYAK 103
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1584-1963 |
1.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1584 MQAMKAQFDRDLQARDEQ----GEEKKRLLVKQVREMEAELEDERKQrtlaVASKKKLEMDLNELEGQIEAANKGRDEAV 1659
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1660 KQLRKLQaQMKDYQRELEEARASRDEIftqsKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGK 1739
Cdd:COG4717 116 EELEKLE-KLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1740 ----SSLLEEKRRLEARIAQLEEELEEEQGNMELLNDrfrksniQVDNLNTELAGERSAAQKSENARQQM---------- 1805
Cdd:COG4717 191 eeelQDLAEELEELQQRLAELEEELEEAQEELEELEE-------ELEQLENELEAAALEERLKEARLLLLiaaallallg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1806 --------ERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDER 1877
Cdd:COG4717 264 lggsllslILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1878 RHADQYKEQMEKANSRMKQLKRQLEEAEEEA--TRANATRRKLQRELDDATEASEGLTREVSSLKNRLRRGGPVSSFSSS 1955
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
....*...
gi 1604804600 1956 RSGRRNLN 1963
Cdd:COG4717 424 ALDEEELE 431
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1696-1855 |
1.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1696 KLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLndrfr 1775
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1776 KSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEG---TVKSKFKASIAALEAKILQLEDQLEQEAKER 1852
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAelaELEAELEEKKAELDEELAELEAELEELEAER 165
|
...
gi 1604804600 1853 AAA 1855
Cdd:COG1579 166 EEL 168
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1565-1866 |
1.31e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1565 ELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQGEEKKrllvkqvremeaelEDERKQRTLAVASKkklemdLNEL 1644
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAA--------------EARAAKDKDAVAAA------LARV 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1645 EGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKlkgleAEILqlqedhAASERAR-RHAEQ 1723
Cdd:PRK05035 496 KAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKK-----AAVA------AAIARAKaKKAAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1724 ErDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDrfRKSNIqvdnlntELAGERSAAQKSenARQ 1803
Cdd:PRK05035 565 Q-AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP--KKAAV-------AAAIARAKAKKA--EQQ 632
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804600 1804 QMERQNKDLKAKLAELEGTVkSKFKASIAALEAKilQLEDQLEQEAKERAAANKIVRRTEKKL 1866
Cdd:PRK05035 633 ANAEPEEPVDPRKAAVAAAI-ARAKARKAAQQQA--NAEPEEAEDPKKAAVAAAIARAKAKKA 692
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1235-1497 |
1.35e-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: 43.26 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1235 SNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNActmleVA 1314
Cdd:pfam15905 41 LNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAA-----VR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1315 EKKGLKLAKEV-DKLNSKLQDSEELRQ----EETRQKlNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMF 1389
Cdd:pfam15905 116 EKTSLSASVASlEKQLLELTRVNELLKakfsEDGTQK-KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1390 ETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFD 1469
Cdd:pfam15905 195 HSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
|
250 260
....*....|....*....|....*...
gi 1604804600 1470 QLLAEEKTISAQYAEERDRAEAEAREKD 1497
Cdd:pfam15905 275 KQIKDLNEKCKLLESEKEELLREYEEKE 302
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1543-1939 |
1.42e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1543 HELEKSKRTL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQfdRDLQARDEQGEEkkrlLVKQ 1612
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQ--EKIERYQEDLEE----LTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1613 VREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDeaVKQLRKLQAQMKdyQRELEEARA-------SRDE 1685
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALD--VQQTRAIQYQQA--VQALEKARAlcglpdlTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1686 IFTQSKENEKKLKGLEAEILQLQEDHAASERARR---HAEQERDELADEISNSASGKS--SLLEEKRRLEARIAQleeel 1760
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTarELLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1761 eeeqgnmellndrfrksniqVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgtvkskfkasiaALEAKILQ 1840
Cdd:COG3096 514 --------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1841 LEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKeqmeKANSRMKQLKRQLEEAEEEATRANATR----- 1915
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMqqlle 637
|
410 420
....*....|....*....|....*.
gi 1604804600 1916 --RKLQRELDDATEASEGLTREVSSL 1939
Cdd:COG3096 638 reREATVERDELAARKQALESQIERL 663
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1006-1202 |
1.44e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1006 EDQNSKFLKEKKLLEdRISEMTSQLTEEEEKAKnlGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1085
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1086 IVELQAQIEELK----FQL----------------TKKEEELQAALARSD----------------------------EE 1117
Cdd:PRK05771 116 IKELEQEIERLEpwgnFDLdlslllgfkyvsvfvgTVPEDKLEELKLESDvenveyistdkgyvyvvvvvlkelsdevEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1118 TLQKNNALKQVRELQAHLAELQEDLESEKmcrSKAEKLKRDLSEELEALKTELEDTLdtTAAQQELRSKREQEVAELKKA 1197
Cdd:PRK05771 196 ELKKLGFERLELEEEGTPSELIREIKEEL---EEIEKERESLLEELKELAKKYLEEL--LALYEYLEIELERAEALSKFL 270
|
....*
gi 1604804600 1198 IDEET 1202
Cdd:PRK05771 271 KTDKT 275
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
874-1363 |
1.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 874 EELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAeteLFAEAEEMRVRLLSRKQE-LEEILHDLESRVEEEEER 952
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQRRLELLEAELEeLRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 953 NQSLQNEKKKMQSHIQDLEEQLDeeeaarQKLQLDKVTAEAKIKKMEEDILLLEDQ----NSKFLKEKKLLEDRISEMTS 1028
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1029 QLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVE-LQAQIEELKF-----QLTK 1102
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFvgeliEVRP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1103 KEEELQAA-------LARS---DEETLQKnnALKQVRELQA----HLAELQEDLESEKMCR----SKAEKLKRDLSEELE 1164
Cdd:COG4913 472 EEERWRGAiervlggFALTllvPPEHYAA--ALRWVNRLHLrgrlVYERVRTGLPDPERPRldpdSLAGKLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1165 ALKTEL-----------EDTLDTTA-------------------AQQELRSKR-------------EQEVAELKKAI--- 1198
Cdd:COG4913 550 WLEAELgrrfdyvcvdsPEELRRHPraitragqvkgngtrhekdDRRRIRSRYvlgfdnraklaalEAELAELEEELaea 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1199 DEETKNHEAQIQEMRQRQAT--ALEELSEQ---LEQAKRFKSNLEKNKQSLENDNKELscdvKTLQQaktesehKRKKLE 1273
Cdd:COG4913 630 EERLEALEAELDALQERREAlqRLAEYSWDeidVASAEREIAELEAELERLDASSDDL----AALEE-------QLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1274 AQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEvdKLNSKLQdseELRQEETRQKL--NLST 1351
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFA---AALGDAVERELreNLEE 773
|
570
....*....|..
gi 1604804600 1352 QIRQLEVDRNTL 1363
Cdd:COG4913 774 RIDALRARLNRA 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1435-1681 |
1.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1435 KTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERD-RAEAEAREKDTKALSmARALEEALE 1512
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRIRAlEQELAALEAELAELE-KEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1513 AKEELERFNKQLRA--------EMEDLMSSKDdvgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnm 1584
Cdd:COG4942 99 LEAQKEELAELLRAlyrlgrqpPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1585 qamkaqfdrdlqardeqgEEKKRLlvkqvREMEAELEDERKQRTLAVASKKKLemdLNELEGQIEAANKGRDEAVKQLRK 1664
Cdd:COG4942 171 ------------------AERAEL-----EALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*..
gi 1604804600 1665 LQAQMKDYQRELEEARA 1681
Cdd:COG4942 225 LEALIARLEAEAAAAAE 241
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1544-1729 |
1.47e-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: 42.91 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1544 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqaRDEQGEEKKRLLVKQVREMEAELEDE 1623
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1624 RKQRTLAVASKKKLEmdlnelegqiEAANKGRDEAVKqlrKLQAQMKdyqRELEEARASRDEIFTQSKENEKKLKGLEAE 1703
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 1604804600 1704 ILQLQEDHAASERARRHAEQERDELA 1729
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1074-1237 |
1.53e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1074 KLDAETTDLQDQIVELQAQIEELKfqLTKKEEELQAALARSDE--ETLQ-----KNNALKQVRELQAHLAELQEdleSEK 1146
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQlyDILErevkaRKYVEKNSDTLPDFLEHAKE---QNK 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1147 MCRSKAEKLK-------------RDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHE---AQIQ 1210
Cdd:PRK04778 328 ELKEEIDRVKqsytlneselesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEklsEMLQ 407
|
170 180 190
....*....|....*....|....*....|..
gi 1604804600 1211 EMRQRQATA---LEELSEQLEQAKRF--KSNL 1237
Cdd:PRK04778 408 GLRKDELEArekLERYRNKLHEIKRYleKSNL 439
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1658-1945 |
1.54e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1658 AVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAE---QERDELADEISN 1734
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1735 SASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNiqvdnlntelagersAAQKSENARQQMERQNKDLKA 1814
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---------------ELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1815 KLAELEGTvKSKFKASIAALEAKILQLEDQLEQeakeraaankiVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANsRM 1894
Cdd:PRK03918 308 ELREIEKR-LSRLEEEINGIEERIKELEEKEER-----------LEELKKKLKELEKRLEELEERHELYEEAKAKKE-EL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1895 KQLKRQLeeaeeeatrANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:PRK03918 375 ERLKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1488-1945 |
1.57e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1488 RAEAEAREKDTKALSmaraleealeakeelerfnkqLRAEmedLMSSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELE 1567
Cdd:PRK04863 276 RHANERRVHLEEALE---------------------LRRE---LYTSRR-------QLAAEQYRLVEMARELAELNEAES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1568 DELQATEDAKLRLEVNMQAMKAQ-----FDRDLQARDEQGEEKkrllvKQVREMEAELEDERkqrtlavaskkklemdln 1642
Cdd:PRK04863 325 DLEQDYQAASDHLNLVQTALRQQekierYQADLEELEERLEEQ-----NEVVEEADEQQEEN------------------ 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1643 elEGQIEAANKGRDEavkqlrkLQAQMKDYQRELEEA--RASRDEIFTQSKENEKKLKGLEA-EILQLQEDHAASERARR 1719
Cdd:PRK04863 382 --EARAEAAEEEVDE-------LKSQLADYQQALDVQqtRAIQYQQAVQALERAKQLCGLPDlTADNAEDWLEEFQAKEQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1720 HAEQERDELADEISnSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNdRFRKSNIQVDNLNtELAGERSAAQKSE 1799
Cdd:PRK04863 453 EATEELLSLEQKLS-VAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR-RLREQRHLAEQLQ-QLRMRLSELEQRL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1800 NARQQMERQNKDLKaKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAankivrrTEKKLKEVMMQVEDERRH 1879
Cdd:PRK04863 530 RQQQRAERLLAEFC-KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA-------LRQQLEQLQARIQRLAAR 601
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804600 1880 ADQYKEqmekANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1945
Cdd:PRK04863 602 APAWLA----AQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1053-1355 |
1.64e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1053 DLEERLKKEEKTRQELEKAKRKLDAettdLQDQIVELQAQIEELKFQLtkkeEELQAALARSDEEtlqknnalkqvrelq 1132
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEE----LRADEAERARELDLLRFQL----EELEAAALQPGEE--------------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1133 ahlaelqEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELrskreQEVAElkkaideetknHEAQIQE 1211
Cdd:COG0497 209 -------EELEEERRRLSNAEKLREALQEALEALSGGEGGALDLlGQALRAL-----ERLAE-----------YDPSLAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1212 MRQRqataLEELSEQLEQAKRfksNLEKNKQSLENDNKELscdvktlqqaktesehkrkkleAQLQEFMARATEAER--- 1288
Cdd:COG0497 266 LAER----LESALIELEEAAS---ELRRYLDSLEFDPERL----------------------EEVEERLALLRRLARkyg 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1289 -TKGELAERSHKLQTELDNactmLEVAEKKGLKLAKEVDKLNSKLQD-SEELRQEetRQK--LNLSTQIRQ 1355
Cdd:COG0497 317 vTVEELLAYAEELRAELAE----LENSDERLEELEAELAEAEAELLEaAEKLSAA--RKKaaKKLEKAVTA 381
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1438-1872 |
1.65e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1438 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLaeEKTISAQYAEERDRAEAEAREKDTKALsMARALEEALEAKEEL 1517
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRARLLLLALAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1518 ERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQA 1597
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1598 RDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELE 1677
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1678 EARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLE 1757
Cdd:COG5278 326 AALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1758 EELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAK 1837
Cdd:COG5278 406 AAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
410 420 430
....*....|....*....|....*....|....*
gi 1604804600 1838 ILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQ 1872
Cdd:COG5278 486 EAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1053-1143 |
1.91e-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: 42.22 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1053 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQ 1132
Cdd:pfam11932 17 QALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERELV 96
|
90
....*....|.
gi 1604804600 1133 AHLAELQEDLE 1143
Cdd:pfam11932 97 PLMLKMLDRLE 107
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
858-1297 |
2.13e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 858 PLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLieeKNILAEQLHAEtelFAEAEEMRVRLLSRK-QELE 936
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAF---SRFIGSHLAVA---FEADPEAELRQLNRRrVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 937 EILHDLESrveeeeeRNQSLQNEKKKmqshiqdleeqldeeeaARQKLQLdkvtaeakIKKMEEDILLLEDQNskflkek 1016
Cdd:PRK04863 851 RALADHES-------QEQQQRSQLEQ-----------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1017 klLEDRISEMTSQLTEEEEKAKNlgkvknkqemmmvdleerLKKEEKTRQELEKAKRKLDAEttdlqdqivelQAQIEEL 1096
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKRF------------------VQQHGNALAQLEPIVSVLQSD-----------PEQFEQL 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1097 KFQLTKKEEELQAALARSDeetlqknnALKQVRELQAHLA--ELQEDLESEKmcrSKAEKLKRDLsEELEALKTELEDTL 1174
Cdd:PRK04863 941 KQDYQQAQQTQRDAKQQAF--------ALTEVVQRRAHFSyeDAAEMLAKNS---DLNEKLRQRL-EQAEQERTRAREQL 1008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1175 DTTAAQ--------QELRSKR---EQEVAELKKAIDEETKNHEAqiqEMRQRQATALEELSEQLEQAKRFKSNLEKNKQS 1243
Cdd:PRK04863 1009 RQAQAQlaqynqvlASLKSSYdakRQMLQELKQELQDLGVPADS---GAEERARARRDELHARLSANRSRRNQLEKQLTF 1085
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1244 LE----NDNKELSCDVKTLQQAKTESEHKRKKLEAQLQefMARATEAER--TKGELAERS 1297
Cdd:PRK04863 1086 CEaemdNLTKKLRKLERDYHEMREQVVNAKAGWCAVLR--LVKDNGVERrlHRRELAYLS 1143
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
866-1417 |
2.20e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 866 EEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLhaeTELFAEAEEMRvRLLSRKQELEEILHDLESR 945
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY---NNLKSALNELS-SLEDMKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 946 VEEEEERN---QSLQNEKKKMQS--------HIQDLEEQLDEEEAARQKLQ---LDKVTAEAKIKKMEEdillLEDQNSK 1011
Cdd:PRK01156 265 LSMELEKNnyyKELEERHMKIINdpvyknrnYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1012 FLKEKKLLED---RISEM-------TSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTD 1081
Cdd:PRK01156 341 YIKKKSRYDDlnnQILELegyemdyNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1082 LQDQIVELQAQIEELkfqltkkeeelqaalaRSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRdLSE 1161
Cdd:PRK01156 421 ISSKVSSLNQRIRAL----------------RENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSR-LEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1162 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKS----NL 1237
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkleDL 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1238 EKNKQSLENDNKELS-CDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAErtkgelaERSHKLQTELDNACTMLEVAEK 1316
Cdd:PRK01156 564 DSKRTSWLNALAVISlIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK-------SYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1317 KGLKLAKEVDKLNSKLQDseeLRQEetrqklnlSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLE 1396
Cdd:PRK01156 637 EIQENKILIEKLRGKIDN---YKKQ--------IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
570 580
....*....|....*....|.
gi 1604804600 1397 EDLGSMEGLEEVKRKLQKDVE 1417
Cdd:PRK01156 706 ILRTRINELSDRINDINETLE 726
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1387-1945 |
2.24e-03 |
|
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: 43.29 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1387 QMFETKKKLEEDLGSMEG----LEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTK-NRLQQELDDLMVDLDHQRQIVSNL 1461
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFgyksDETLIASRQEERQETSAELNQLLRTLDDQWKEKrDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1462 EKKQKKFDQLLAEEKtisAQYAEERD--RAEAEAREKDTKALSMAraleealeAKEELERFNKQLRAEMEDLmssKDDVG 1539
Cdd:pfam12128 328 EDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKALTGK--------HQDVTAKYNRRRSKIKEQN---NRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1540 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT--------EDAKLRLEVNMQAMKAQFDrDLQARDEQgEEKKRLLVK 1611
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQleagklefNEEEYRLKSRLGELKLRLN-QATATPEL-LLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1612 QVREMEAELEDERKQR---TLAVASKKKLEMDLNELEGQIEAA---NKGRDEAVKQ---------LRKLQAQMKDYQREL 1676
Cdd:pfam12128 472 RIERAREEQEAANAEVerlQSELRQARKRRDQASEALRQASRRleeRQSALDELELqlfpqagtlLHFLRKEAPDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1677 EEARASR--------DEIFTQSKENEKKLKG--LEAEILQLQEDHAASERARRHAEQERDELADEISNSAsgksslleek 1746
Cdd:pfam12128 552 GKVISPEllhrtdldPEVWDGSVGGELNLYGvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA---------- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1747 rRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKS--------ENARQQMERQNKDLK----- 1813
Cdd:pfam12128 622 -AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAlaerkdsaNERLNSLEAQLKQLDkkhqa 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1814 -----------------AKLAELEGTVKSK---FKASIAALE----AKILQLEDQLEQEAKERAAANKIVRRTEKKLKEV 1869
Cdd:pfam12128 701 wleeqkeqkreartekqAYWQVVEGALDAQlalLKAAIAARRsgakAELKALETWYKRDLASLGVDPDVIAKLKREIRTL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1870 MMQVEDERR------------------HADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAtrrKLQRELDDATEASEG 1931
Cdd:pfam12128 781 ERKIERIAVrrqevlryfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRA---KLEMERKASEKQQVR 857
|
650
....*....|....
gi 1604804600 1932 LTREVSSLKNRLRR 1945
Cdd:pfam12128 858 LSENLRGLRCEMSK 871
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1045-1278 |
2.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1045 NKQEMMMVDLEERLKKEEKTRQELEKAKRKLD---AETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQK 1121
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDelnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1122 NNALKQVRELQAHLAELQEDLESekmcRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQEL--RSKR-EQEVAELKKAI 1198
Cdd:COG1340 81 DELNEKLNELREELDELRKELAE----LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1199 DEETKNHE--AQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQL 1276
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
..
gi 1604804600 1277 QE 1278
Cdd:COG1340 237 KE 238
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
861-1477 |
2.58e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 861 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEA-EEMRVRLLSRKQELEEIL 939
Cdd:TIGR01612 1170 EIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKiDEEKKKSEHMIKAMEAYI 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 940 HDLESrveeEEERNQSLQNE-------KKKMQS-----------HIQDLEEQLDEEEAARQKLQLDKVTAEAK----IKK 997
Cdd:TIGR01612 1250 EDLDE----IKEKSPEIENEmgiemdiKAEMETfnishdddkdhHIISKKHDENISDIREKSLKIIEDFSEESdindIKK 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 998 -MEEDILLLEDQNSKF---------------LKEKKLLEDRISEMTSQLteeEEKAKNLgkvknKQEMmmvDLEERLKKE 1061
Cdd:TIGR01612 1326 eLQKNLLDAQKHNSDInlylneianiynilkLNKIKKIIDEVKEYTKEI---EENNKNI-----KDEL---DKSEKLIKK 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1062 EKTRQELEKAKRKLDAeTTDLQDqIVELQAQIEELKFQLTKKEEELQAALARSDEET----------------------L 1119
Cdd:TIGR01612 1395 IKDDINLEECKSKIES-TLDDKD-IDECIKKIKELKNHILSEESNIDTYFKNADENNenvlllfkniemadnksqhilkI 1472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1120 QKNNAlkqVRELQAHLAELQEDLESEKMCRSKAEKLKRDLS---EELEALKTELEDTLDTTAAqQELRSKREQ------- 1189
Cdd:TIGR01612 1473 KKDNA---TNDHDFNINELKEHIDKSKGCKDEADKNAKAIEknkELFEQYKKDVTELLNKYSA-LAIKNKFAKtkkdsei 1548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1190 ---EVAELKKAIDEETKNHEAQIQEMRQRQATALEELseqleqAKRFKSN-----LEKNKQSLENDNKELSCDVKTLQQA 1261
Cdd:TIGR01612 1549 iikEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDA------AKNDKSNkaaidIQLSLENFENKFLKISDIKKKINDC 1622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1262 KTESEhkrkKLEAQLQEFMARATEAERTkgELAERSHKLQTELDNactmLEVAEKKGLKLAKEVDKLNSKLQDSE-ELRQ 1340
Cdd:TIGR01612 1623 LKETE----SIEKKISSFSIDSQDTELK--ENGDNLNSLQEFLES----LKDQKKNIEDKKKELDELDSEIEKIEiDVDQ 1692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1341 EETRQKLNLSTQIRQLEV-DRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEvkrKLQKDVELT 1419
Cdd:TIGR01612 1693 HKKNYEIGIIEKIKEIAIaNKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYE---EFIELYNII 1769
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804600 1420 SQCLE---EKTMAMDKMEKTKNRLQQElddLMVDLDHQRQIVSNLEK-KQKKFDQLLAEEKT 1477
Cdd:TIGR01612 1770 AGCLEtvsKEPITYDEIKNTRINAQNE---FLKIIEIEKKSKSYLDDiEAKEFDRIINHFKK 1828
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1542-1943 |
2.87e-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: 42.71 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1542 VHELEKSKrTLEQQVEEMRTQLEELEDELQATEDAKLR----LEVN---MQAMKAQFDRdLQARDEQGEEKKRLLVKQVR 1614
Cdd:pfam05701 31 IQTVERRK-LVELELEKVQEEIPEYKKQSEAAEAAKAQvleeLESTkrlIEELKLNLER-AQTEEAQAKQDSELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1615 EME------------AELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRklqaqmkdyqreleearas 1682
Cdd:pfam05701 109 EMEqgiadeasvaakAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAE------------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1683 rdEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELA----DEISNSASGKSSLLEEKRRLEARIAQLEE 1758
Cdd:pfam05701 170 --EAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareQDKLNWEKELKQAEEELQRLNQQLLSAKD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1759 ELEEEQGNMELLNDrfrksniqvdnLNTELAGERSAAQKSENARQQMERQ-NKDLKAKLA----ELEgtvksKFKASI-- 1831
Cdd:pfam05701 248 LKSKLETASALLLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALAsakkELE-----EVKANIek 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1832 AALEAKILQ-----LEDQLEQEAKERAAankiVRRTEKKLKEVMMQVEDERRHADQ----YKEQMEKANSRMKQLKRQLE 1902
Cdd:pfam05701 312 AKDEVNCLRvaaasLRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQ 387
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1604804600 1903 EAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRL 1943
Cdd:pfam05701 388 QAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRL 428
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1051-1146 |
3.07e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1051 MVDLEERLKKEEKTRQELEKAKRKLDAET-TDLQDQIVELQAQIEELKFQLtKKEEELQAALARSDEETLQKNNALKqvr 1129
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARW-EAEKELIEEIQELKEELEQRYGKIP--- 488
|
90
....*....|....*..
gi 1604804600 1130 ELQAHLAELQEDLESEK 1146
Cdd:COG0542 489 ELEKELAELEEELAELA 505
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1651-1734 |
3.25e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.98 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1651 ANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEI---FTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDE 1727
Cdd:PRK05431 19 AKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEIKALEAELDELEAELEE 98
|
....*..
gi 1604804600 1728 LADEISN 1734
Cdd:PRK05431 99 LLLRIPN 105
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1385-1603 |
3.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1385 QSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1464
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1465 QKK-------FDQLLAeektiSAQYAEERDRAEAEAR--EKDTKALSMARALEealeakeelerfnKQLRAEMEDLMSSK 1535
Cdd:COG3883 95 LYRsggsvsyLDVLLG-----SESFSDFLDRLSALSKiaDADADLLEELKADK-------------AELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804600 1536 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGE 1603
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1647-1927 |
3.57e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1647 QIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASR----DEIFTQSKENEKKLKGLEAEILQLQEDhaasERARRHAE 1722
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1723 QERDELADEISNSASGKSSLLEEKRRLEaRIAQLEEELEEEQgnmELLNDRFRKSNIQVDNLNtELAGERSAAQKSENAR 1802
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVK---ILEEERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1803 QQMERQNKDLKAKLAELEGTVK-SKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMmqVEDERRHAD 1881
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM--IEEERKRKL 517
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1604804600 1882 QYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATE 1927
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| CCDC90-like |
pfam07798 |
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ... |
1132-1231 |
3.59e-03 |
|
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.
Pssm-ID: 462268 [Multi-domain] Cd Length: 175 Bit Score: 40.57 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1132 QAHLAELQEDLES-EK----MCRSKAEKLKRDLseelEALKTELEDTLDTTAAQQELrskreqEVAELKKAIDEETKNHE 1206
Cdd:pfam07798 56 KADLAELRSELQIlEKsefaALRSENEKLRREL----EKLKQRLREEITKLKADVRL------DLNLEKGRIREELKAQE 125
|
90 100
....*....|....*....|....*
gi 1604804600 1207 AQIQEMRQRQATALEELSEQLEQAK 1231
Cdd:pfam07798 126 LKIQETNNKIDTEIANLRTQIESVK 150
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
1029-1114 |
4.31e-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: 41.57 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1029 QLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD----------QIVELQAQIEELKF 1098
Cdd:smart00435 278 SMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKekkkeekkkkQIERLEERIEKLEV 357
|
90
....*....|....*.
gi 1604804600 1099 QLTKKEEELQAALARS 1114
Cdd:smart00435 358 QATDKEENKTVALGTS 373
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1019-1166 |
4.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1019 LEDRISEMTSQLTEE---EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEE 1095
Cdd:PRK04863 518 LRMRLSELEQRLRQQqraERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1096 LKfQLTKKEEELQAALARSDEetlQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEAL 1166
Cdd:PRK04863 598 LA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
990-1216 |
5.05e-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: 41.37 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 990 TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRisemtsQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELE 1069
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQA------RQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1070 KAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCR 1149
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804600 1150 SKAEKLKRdLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKnHEAQIQEMRQRQ 1216
Cdd:TIGR02794 211 AKAEAEAA-AAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK-YAAIIQQAIQQN 275
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1058-1378 |
5.51e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1058 LKKEEKTRQELEKAKR-KLDAETTDLQDQIVELQAQIEELKfQLTKKEEELQAAL--ARSDEETLQKNNALKQVRELQAH 1134
Cdd:PRK10246 535 LEKEVKKLGEEGAALRgQLDALTKQLQRDESEAQSLRQEEQ-ALTQQWQAVCASLniTLQPQDDIQPWLDAQEEHERQLR 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1135 LAELQEDLESEKmcrSKAEKLKRDLSEELEALKTELEDTLDTTA-------AQQELRSKREQEVAELkkaidEETKNHEA 1207
Cdd:PRK10246 614 LLSQRHELQGQI---AAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSW-----QQRQNELT 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1208 QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQL----------- 1276
Cdd:PRK10246 686 ALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFdtalqasvfdd 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1277 QEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEK----------KGLKLAKEVDKLNSKL-QDSEELRQEETRQ 1345
Cdd:PRK10246 766 QQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQalaqhqqhrpDGLDLTVTVEQIQQELaQLAQQLRENTTRQ 845
|
330 340 350
....*....|....*....|....*....|...
gi 1604804600 1346 KlNLSTQIRQLEVDRNTLLEQQEEEEEARRNLE 1378
Cdd:PRK10246 846 G-EIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1780-1945 |
5.62e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1780 QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgtvkskfkASIAALEAKILQLEDQLEQEA--KERAAANK 1857
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE--------ARIKKYEEQLGNVRNNKEYEAlqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1858 IVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLeeaeeeATRANATRRKLQRELDDATEASEGLTREVS 1937
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL------DEELAELEAELEELEAEREELAAKIPPELL 177
|
....*...
gi 1604804600 1938 SLKNRLRR 1945
Cdd:COG1579 178 ALYERIRK 185
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1088-1274 |
5.64e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.41 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1088 ELQAQIEELKfqlTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEkmcrskaEKLKRDLSEELEALK 1167
Cdd:pfam15665 11 EHEAEIQALK---EAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQH-------ERMKRQALTEFEQYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1168 TELED-TLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELS-------EQLEQAKRFKSN--- 1236
Cdd:pfam15665 81 RRVEErELKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRakhrqeiQELLTTQRAQSAssl 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1604804600 1237 ------LEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEA 1274
Cdd:pfam15665 161 aeqeklEELHKAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQA 204
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1522-1723 |
5.85e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1522 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDEQ 1601
Cdd:COG1340 53 KELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1602 GEEKKRLLVK-------------------QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQL 1662
Cdd:COG1340 132 PEEEKELVEKikelekelekakkalekneKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1663 RKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEdHAASERARRHAEQ 1723
Cdd:COG1340 212 DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR-EKEKEELEEKAEE 271
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
992-1158 |
6.02e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 992 EAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--ISEMTSQLTEEEEKaknLGKVKNKqemmMVDLEERLKKEEKTRQELE 1069
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvCPTCTQQISEGPDR---ITKIKDK----LKELQHSLEKLDTAIDELE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1070 KakrKLDaETTDLQDQIVELQAQIEELKFQLT---KKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEK 1146
Cdd:PHA02562 327 E---IMD-EFNEQSKKLLELKNKISTNKQSLItlvDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
170
....*....|..
gi 1604804600 1147 MCRSKAEKLKRD 1158
Cdd:PHA02562 403 YHRGIVTDLLKD 414
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1015-1209 |
7.16e-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: 41.20 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1015 EKKLLEDRISEMTSQLTEE-EEKAKNLGKVKNKQEMMMVDLEERLKK---EEKTRQELEKAKRKLDAETTDLQDQIVELQ 1090
Cdd:pfam13166 262 GQPLPAERKAALEAHFDDEfTEFQNRLQKLIEKVESAISSLLAQLPAvsdLASLLSAFELDVEDIESEAEVLNSQLDGLR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1091 AQIEELKFQLTKKEEelqaaLARSDEETLQKNNALKQVRELQAHLAELQEDLESEKmcRSKAEKLKRDLSEELEALKTEL 1170
Cdd:pfam13166 342 RALEAKRKDPFKSIE-----LDSVDAKIESINDLVASINELIAKHNEITDNFEEEK--NKAKKKLRLHLVEEFKSEIDEY 414
|
170 180 190
....*....|....*....|....*....|....*....
gi 1604804600 1171 EDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQI 1209
Cdd:pfam13166 415 KDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQL 453
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
993-1173 |
7.33e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.38 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 993 AKIKKMEEDILLLEdQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAK 1072
Cdd:PRK06669 2 PKVIFKRSNVINKE-KLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1073 RKLDAETTDLQDQIVELQAQIEELKFQL-TKKEEELQAALARSDEETLQKNNAlkqvrELQAHLAELQEDLesekmcRSK 1151
Cdd:PRK06669 81 EELLKKTDEASSIIEKLQMQIEREQEEWeEELERLIEEAKAEGYEEGYEKGRE-----EGLEEVRELIEQL------NKI 149
|
170 180
....*....|....*....|..
gi 1604804600 1152 AEKLKRDLSEELEALKTELEDT 1173
Cdd:PRK06669 150 IEKLIKKREEILESSEEEIVEL 171
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
997-1136 |
7.51e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 997 KMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVkNKQEMMMVDLEERLkkeEKTRQELEKAKRKLD 1076
Cdd:pfam15294 144 KLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEI-SDLEEKMAALKSDL---EKTLNASTALQKSLE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1077 AETTDLQDQIVELQAQIEELKFQLTKKEEelQAALARSDEETLQKNNalKQVRELQAHLA 1136
Cdd:pfam15294 220 EDLASTKHELLKVQEQLEMAEKELEKKFQ--QTAAYRNMKEMLTKKN--EQIKELRKRLS 275
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1015-1145 |
8.34e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1015 EKKLLEDRISEMTSQLTEEE----------EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD 1084
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEqrlrqqqnaeRLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804600 1085 QIVELQAQIEELKFQ----------LTKKEEELQAALARSDEETLQKNNALKQVRELQA---HLAELQEDLESE 1145
Cdd:COG3096 586 QLEQLRARIKELAARapawlaaqdaLERLREQSGEALADSQEVTAAMQQLLEREREATVerdELAARKQALESQ 659
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
867-1127 |
8.67e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 867 EELQakDEELVKVKERQLKVENELVEMERKHQQLIEEK----NILAEQLHAETELFAEAEEmrVRLLSRKQELEEILHDL 942
Cdd:PRK05771 23 EALH--ELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklRSYLPKLNPLREEKKKVSV--KSLEELIKDVEEELEKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 943 ESRVEEEEERNQSLQNEKKKMQSHIQDleeqldeeeaarqklqldkvtaeakIKKME----EDILLLEDQNSKFL----- 1013
Cdd:PRK05771 99 EKEIKELEEEISELENEIKELEQEIER-------------------------LEPWGnfdlDLSLLLGFKYVSVFvgtvp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1014 KEKKLLEDRISEMTSQLTEEEEKAKN----LGKVKNKQEmmmvdLEERLKKEEKTRQELEkAKRKLDAETTDLQDQIVEL 1089
Cdd:PRK05771 154 EDKLEELKLESDVENVEYISTDKGYVyvvvVVLKELSDE-----VEEELKKLGFERLELE-EEGTPSELIREIKEELEEI 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1604804600 1090 QAQIEELKFQL---TKKEEELQAALARSDEETLQKNNALKQ 1127
Cdd:PRK05771 228 EKERESLLEELkelAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1522-1852 |
8.99e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1522 KQLRAEMEDLMSSKDDVGKNVHE--------LEKSKRTLE-----QQV--------EEMRTQLEELEDELQATEDAKLRL 1580
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEalqsalnwLEERKGSLErakqyQQVidnfpklsAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1581 EVNMQAMKAQFDRDLQARDEQGE-EKKRLLVKQVREMEAELEDERKQrtlavaskkklemdLNELEGQIEAANKGRDEAV 1659
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQEqDRAREISDSLSQLPQQQTEARRQ--------------LNEIERRLQTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1660 kqlrklQAQMKDYQRELEEARASRDEI-FTQ-SKENEKKLKGLEAEILQLQEDHAASE----------RARRHAEQ--ER 1725
Cdd:PRK10929 172 ------QAQLTALQAESAALKALVDELeLAQlSANNRQELARLRSELAKKRSQQLDAYlqalrnqlnsQRQREAERalES 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804600 1726 DE-LADEISNSASGKSSLLEEKRRLEARIAQLEEEleeeqgnMELLNDRFRKSNIQVDNLNTELAGERSAAQ--KSENAR 1802
Cdd:PRK10929 246 TElLAEQSGDLPKSIVAQFKINRELSQALNQQAQR-------MDLIASQQRQAASQTLQVRQALNTLREQSQwlGVSNAL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1604804600 1803 QQMerqnkdLKAKLAELEGTVKS-KFKASIAALEAKILQLEDQLEQEAKER 1852
Cdd:PRK10929 319 GEA------LRAQVARLPEMPKPqQLDTEMAQLRVQRLRYEDLLNKQPQLR 363
|
|
| |
