|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
869-1949 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1485.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 869 TRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDL 948
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 949 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1028
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1029 ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTK 1108
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1109 KEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1188
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1189 LRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAK 1268
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1269 TESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEE 1348
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1349 TRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQC 1428
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1429 LEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALS 1508
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1509 MARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1588
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1589 NMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQL 1668
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1669 RKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSL 1748
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1749 LEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGT 1828
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1829 VKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLE 1908
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1604804596 1909 EAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRL 1949
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1420.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP---------------------GELERQLLQANPILESFGNAKTVKND 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14920 140 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd14920 220 PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAIL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd14920 300 TPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd14920 380 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNET 658
Cdd:cd14920 460 GSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTET 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 AFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14920 540 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14920 620 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-792 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1304.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkpvklqaqhavsgplfYGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKK--------------------KGTLEDQILQANPILEAFGNAKTVRNN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYR-FLSNGNIP 337
Cdd:cd01377 141 NSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAI 417
Cdd:cd01377 221 IDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 418 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCI 497
Cdd:cd01377 301 LKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 498 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLIQE 577
Cdd:cd01377 380 NYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 578 QGTHTK-FQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRivgldqvagmn 656
Cdd:cd01377 458 HLGKSKnFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE----------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 657 ETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 736
Cdd:cd01377 527 SGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGF 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 737 PNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd01377 607 PNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1236.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhavSGPLFYGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS-----------------SIALSHGELEKQLLQANPILEAFGNAKTVKND 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14932 144 NSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd14932 224 PGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd14932 304 SPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd14932 384 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNET 658
Cdd:cd14932 464 GNNPKFQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGES 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 AFGAtYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14932 544 LHGA-FKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPN 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14932 623 RIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1186.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ------------------------GELERQLLQANPILEAFGNAKTVKND 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14919 137 NSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd14919 217 PGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGIL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd14919 297 TPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCIN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd14919 377 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQ 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNET 658
Cdd:cd14919 457 GTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSET 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 AFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14919 537 ALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14919 617 RVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-792 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1171.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhavSGPLFYGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN-----------------SLALSHGELEKQLLQANPILEAFGNAKTVKND 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd15896 144 NSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd15896 224 PGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd15896 304 SPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd15896 384 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNEt 658
Cdd:cd15896 464 GTHPKFFKPKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 aFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd15896 543 -MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd15896 622 RIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1170.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvklqaqhavsgplfYGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI---------------------TGELEKQLLQANPILEAFGNAKTVKND 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14921 140 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd14921 220 PAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSIL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd14921 300 TPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd14921 380 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNET 658
Cdd:cd14921 460 GNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTES 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 AFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14921 540 SLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14921 620 RIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1163.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASShkgrkdhnippeSPKPVKLQAQHAVSGPLFYGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS------------KPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKND 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14911 149 NSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd14911 229 PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd14911 309 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCIN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd14911 389 YTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAH 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrIVGLDQVAgMNET 658
Cdd:cd14911 466 SMHPKFMK-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 AFGAtyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14911 543 QFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPN 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14911 621 RIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1139.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP---------------------GELERQLLQANPILEAFGNAKTVKND 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14930 140 NSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQdKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd14930 220 PGQE-RELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd14930 299 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCIN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd14930 379 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNET 658
Cdd:cd14930 459 GGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 AFGAtyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 738
Cdd:cd14930 539 PPGG--RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPN 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 739 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14930 617 RILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-792 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1098.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 87 VEDMAELTCLNEASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkpvklqaqhavsgplfYGELERQLLQANPIL 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-------------------------VGRLEEQILQSNPIL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 247 ESFGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN 326
Cdd:pfam00063 136 EAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 327 SYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHL 405
Cdd:pfam00063 216 DYHYLSQSGcYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 406 LGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFE 485
Cdd:pfam00063 296 LGIDSTELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 486 IFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKA 565
Cdd:pfam00063 376 IFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 566 TDKTFVDKLIQEQGTHTKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDR 645
Cdd:pfam00063 453 TDQTFLDKLYSTFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYET 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 646 IVGLDQvagmNETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 725
Cdd:pfam00063 532 AESAAA----NESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGV 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 726 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:pfam00063 608 LEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-804 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 997.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 80 NPPKFTKVEDMAELTCLNEASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnippespkpvklqaqhavsgplfyGELERQL 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---------------------------GSVEDQI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 240 LQANPILESFGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSD 319
Cdd:smart00242 134 LESNPILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 320 LLLEGFNSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNT- 397
Cdd:smart00242 214 LGLKSPEDYRYLNQGGcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKe 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 398 AAQKLCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIG 477
Cdd:smart00242 294 ELSNAAELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 478 ILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLD 557
Cdd:smart00242 373 VLDIYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 558 EECWFPKATDKTFVDKLIQEQGTHTKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVG 637
Cdd:smart00242 450 EECRFPKGTDQTFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 638 ELWKDvdrivgldqvagmnetafGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 717
Cdd:smart00242 529 SLFPS------------------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVL 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 718 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFRTGVLA 797
Cdd:smart00242 591 HQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLA 670
|
....*..
gi 1604804596 798 HLEEERD 804
Cdd:smart00242 671 ELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1454 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 910.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 36 VWIPSERNGFEAASVREERGDEVVVELA---ENGKKAVVNKDDIQ--KMNPPKFTKVEDMAELTCLNEASVLYNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 191 VIQYLAHVASSHkgrkdhniPPESpkpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 270
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI------------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 271 FDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQE 349
Cdd:COG5022 226 FDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 350 TMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNsDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPRIKVGRDYV 429
Cdd:COG5022 306 TLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 430 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFN 509
Cdd:COG5022 385 VVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFN 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 510 HTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVDKLIQ--EQGTHTKFQKP 587
Cdd:COG5022 464 QHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKS 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 588 RQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVgldqvagmnetafgatyktK 667
Cdd:COG5022 542 RFRDNK--FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------S 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 668 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 747
Cdd:COG5022 601 KGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQ 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 748 RYEILTPNA----IPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFRTGVLAHLEEERDLKITDIIIYFQSVCRGYLA 823
Cdd:COG5022 681 RYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYL 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 824 RKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEELQAKDEELVKVkerQLKVENELVEMERKH 903
Cdd:COG5022 761 RRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEE 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 904 QqlieEKNILAEQLHAETELFAEAEEmRVRLLSRKQELEEILhdleSRVEEEEERNQSLQNEKKKMQShiqdleeqldee 983
Cdd:COG5022 838 V----EFSLKAEVLIQKFGRSLKAKK-RFSLLKKETIYLQSA----QRVELAERQLQELKIDVKSISS------------ 896
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 984 eAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--ISEMTSQLTEEEEKAKNLGKVKNKQEmMMVDLE 1061
Cdd:COG5022 897 -LKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKLKE-TSEEYE 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1062 ERLKKEEKTRQELEKAKRKLD---AETTDLQDQIVELQAQIEELKfQLTKKEEELQAALARSDEETlqknnalkqvrelq 1138
Cdd:COG5022 975 DLLKKSTILVREGNKANSELKnfkKELAELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSES-------------- 1039
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1139 ahlAELQEDLESEKMcRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNH--EAQIQ 1216
Cdd:COG5022 1040 ---TELSILKPLQKL-KGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLvkPANVL 1115
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1217 EMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCdvkTLQQAKTESEHKRKKLEAQLQEfmaRATEAERTK 1296
Cdd:COG5022 1116 QFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDG---LFWEANLEALPSPPPFAALSEK---RLYQSALYD 1189
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1297 gELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQD----SEELRQEETRQKLNLSTQIRQLEVDRNTLLEQ 1372
Cdd:COG5022 1190 -EKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVpteySTSLKGFNNLNKKFDTPASMSNEKLLSLLNSI 1268
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1373 QEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSmeGLEEVKRKLQKDVELTSQCLEEKtmamdKMEKTKNRLQQELDD 1452
Cdd:COG5022 1269 DNLLSSYKLEEEVLPATINSLLQYINVGLFNALRT--KASSLRWKSATEVNYNSEELDDW-----CREFEISDVDEELEE 1341
|
..
gi 1604804596 1453 LM 1454
Cdd:COG5022 1342 LI 1343
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-792 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 848.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhavsgplfYGELERQLLQANPILESFGNAKTVKN 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS----------------------ASSIEQQILQSNPILEAFGNAKTVRN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFL-----S 332
Cdd:cd00124 139 DNSSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 333 NGNIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNS--DQASMPDNTAAQKLCHLLGLNV 410
Cdd:cd00124 219 SGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 411 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFQL 489
Cdd:cd00124 299 EDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 490 NSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKT 569
Cdd:cd00124 379 NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDAT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 570 FVDKLIQEQGTHTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvgelwkdvdrivgl 649
Cdd:cd00124 456 FLEKLYSAHGSHPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ---------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 650 dqvagmnetafgatyktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGI 729
Cdd:cd00124 519 ----------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAV 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 730 RICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd00124 571 RIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 772.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTG---------------GTLEDQIIEANPAMEAFGNAKTLRND 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKsDLLLEGFN--SYRFLSNGNI 336
Cdd:cd14927 146 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRA 416
Cdd:cd14927 225 TVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 417 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMC 496
Cdd:cd14927 305 LLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLC 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 497 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQ 576
Cdd:cd14927 384 INFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 577 EQ-GTHTKFQKPR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdriVGLDQV 652
Cdd:cd14927 461 NHlGKSPNFQKPRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 653 AgmnETAFGATYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 731
Cdd:cd14927 538 E---DPKSGVKEKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRI 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 732 CRQGFPNRIVFQEFRQRYEILTPNAIPK-GFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14927 615 CRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 758.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKPVKLQaqhavsgplfyGELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMK-----------GTLEDQIISANPLLEAFGNAKTVRNDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNSYR--FLSNGNIP 337
Cdd:cd14913 143 SSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEIL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRA 416
Cdd:cd14913 222 VASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 417 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMC 496
Cdd:cd14913 301 LCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 497 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI- 575
Cdd:cd14913 380 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYd 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 576 QEQGTHTKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivgldqVA 653
Cdd:cd14913 457 QHLGKSNNFQKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 GMNETAFGATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14913 528 TADADSGKKKVAKKKGsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRIC 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 733 RQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14913 608 RKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 738.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKPvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKT------DEAAKSK---------------GSLEDQVVQTNPVLEAFGNAKTVRND 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIP 337
Cdd:cd14909 140 NSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAI 417
Cdd:cd14909 220 VPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 418 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCI 497
Cdd:cd14909 300 LKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 498 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQE 577
Cdd:cd14909 379 NFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 578 Q-GTHTKFQKPRQLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivgLDQVA 653
Cdd:cd14909 456 HlGKSAPFQKPKPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD------HAGQS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 GMNETAFGATYKtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14909 530 GGGEQAKGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICR 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 734 QGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14909 609 KGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 719.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK-----------------------GSLEDQIIQANPVLEAFGNAKTTRNN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHL-KSDLLLEGFNSYRFLSNGNIP 337
Cdd:cd14934 138 NSSRFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAI 417
Cdd:cd14934 218 VDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 418 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCI 497
Cdd:cd14934 298 TRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 498 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQE 577
Cdd:cd14934 377 NFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 578 Q-GTHTKFQKPRQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdKFVGELWKDvdrivgldqva 653
Cdd:cd14934 454 HlGKSSNFLKPKGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFK----------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 gmNETAFGATYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14934 522 --EEEAPAGSKKQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRIC 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 733 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14934 600 RKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-792 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 714.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkpvklqaqhavsgplfygELERQLLQANPILESFGNAKTVKND 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET-------------------QVEEKVLASNPIMEAFGNAKTTRND 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIP- 337
Cdd:cd01380 135 NSSRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAI 417
Cdd:cd01380 215 IDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 418 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQMC 496
Cdd:cd01380 295 CKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 497 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLIQ 576
Cdd:cd01380 375 INYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYN 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 577 EQGTHTK--FQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvgelwkdvdrivgldqvag 654
Cdd:cd01380 451 QHLKKPNkhFKKPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR-------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 655 mnetafgatyktKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd01380 509 ------------KK----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAA 572
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 735 GFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd01380 573 GFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 698.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPKPvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPGK---------------GTLEDQIIQANPALEAFGNAKTVRND 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--SYRFLSNGNI 336
Cdd:cd14917 142 NSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGET 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTR 415
Cdd:cd14917 221 TVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 416 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQM 495
Cdd:cd14917 300 GLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 496 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI 575
Cdd:cd14917 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 576 QEQ-GTHTKFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivgldqV 652
Cdd:cd14917 456 DNHlGKSNNFQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------Y 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 653 AGMNETAFGATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 731
Cdd:cd14917 527 AGADAPIEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRI 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 732 CRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14917 607 CRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-792 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 694.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkpvKLqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK------------KL------------GALEDQIMQANPVLEAFGNAKTLRND 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEhlKSDLLLEGFN--SYRFLSNGNI 336
Cdd:cd14929 137 NSSRFGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRA 416
Cdd:cd14929 215 AVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 417 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMC 496
Cdd:cd14929 295 LIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLC 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 497 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQ 576
Cdd:cd14929 374 INFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 577 EQ-GTHTKFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrivglDQVA 653
Cdd:cd14929 451 NHfGKSVHFQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YIST 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 GmNETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14929 524 D-SAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICR 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 734 QGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14929 603 EGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-792 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 680.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 101 VLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 181 GAGKTENTKKVIQYLAHVASSHKGRKDhnippESPKpvklqaqhavsgplFYGELERQLLQANPILESFGNAKTVKNDNS 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKE-----ESGK--------------MQGTLEDQIISANPLLEAFGNAKTVRNDNS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 261 SRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIPIP 339
Cdd:cd14918 144 SRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 340 GQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd14918 224 SIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALC 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd14918 303 YPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCIN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI-QE 577
Cdd:cd14918 382 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQH 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 578 QGTHTKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdrivgldqVAGM 655
Cdd:cd14918 459 LGKSANFQKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 656 NETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQG 735
Cdd:cd14918 531 ADSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 736 FPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14918 611 FPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 680.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnipPESPKpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN---PNANK----------------GTLEDQIIQANPALEAFGNAKTVRND 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--SYRFLSNGNI 336
Cdd:cd14916 143 NSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNTA-AQKLCHLLGLNVMEFTR 415
Cdd:cd14916 222 SVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 416 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQM 495
Cdd:cd14916 301 GLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 496 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI 575
Cdd:cd14916 380 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 576 QEQ-GTHTKFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdrivgldQV 652
Cdd:cd14916 457 DNHlGKSNNFQKPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------AS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 653 AGMNETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14916 530 ADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRIC 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 733 RQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14916 610 RKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 678.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvklqaqhaVSGPLFYGELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEE-----------------ITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIPI 338
Cdd:cd14912 145 SSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAI 417
Cdd:cd14912 225 ASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 418 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCI 497
Cdd:cd14912 304 CYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 498 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI-Q 576
Cdd:cd14912 383 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 577 EQGTHTKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAG 654
Cdd:cd14912 460 HLGKSANFQKPKVVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 655 MNETAfgatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd14912 540 AKKGG-----KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 735 GFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14912 615 GFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 677.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKPVKLQaqhavsgplfyGELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQ-----------GTLEDQIIQANPLLEAFGNAKTVRNDN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNSYR--FLSNGNIP 337
Cdd:cd14923 144 SSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRA 416
Cdd:cd14923 223 VASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 417 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMC 496
Cdd:cd14923 302 LCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 497 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI- 575
Cdd:cd14923 381 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYd 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 576 QEQGTHTKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdriVGLDQVA 653
Cdd:cd14923 458 QHLGKSNNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGD 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 GMNETAFGatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14923 535 SGGSKKGG---KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICR 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 734 QGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14923 612 KGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 675.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvklqaqhaVSGPLFYGELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEE-----------------ATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNSYRFLSNGNIPI 338
Cdd:cd14910 145 SSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRAI 417
Cdd:cd14910 225 PSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 418 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMCI 497
Cdd:cd14910 304 CYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 498 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQE 577
Cdd:cd14910 383 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 578 Q-GTHTKFQKPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVdrivgldqVAG 654
Cdd:cd14910 460 HlGKSNNFQKPKPAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 655 MNETAFGATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14910 532 EAEEGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICR 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 734 QGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14910 612 KGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-792 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 670.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkpvklqaQHAVSGPLfYGELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK----------------EEAASGKM-QGTLEDQIISANPLLEAFGNAKTVRNDN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNSYRF--LSNGNIP 337
Cdd:cd14915 145 SSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEIT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmPDNT-AAQKLCHLLGLNVMEFTRA 416
Cdd:cd14915 224 VPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 417 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQMC 496
Cdd:cd14915 303 LCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLC 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 497 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLIQ 576
Cdd:cd14915 382 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 577 EQ-GTHTKFQKPRQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgldqvA 653
Cdd:cd14915 459 QHlGKSNNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------T 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 GMNETAFGATYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd14915 531 AEAEGGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRIC 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 733 RQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14915 611 RKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-792 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 636.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpVKlqaqhavsgplfygeleRQLLQANPILESFGNAKTVKNDN 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VK-----------------DMLLASNPLLEAFGNAKTLRNDN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-IPI 338
Cdd:cd01378 136 SSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFkKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd01378 216 DGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVG---RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQM 495
Cdd:cd01378 295 HRTIETGgggRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 496 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVDKL 574
Cdd:cd01378 375 CINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 575 IQEQGTHTKFQKPRQLKD--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRivgldqv 652
Cdd:cd01378 452 NQLFSNHPHFECPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 653 agmnetafgatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd01378 525 ------------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVR 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 733 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd01378 593 RAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-792 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 634.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavsgplfygELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------------------------------WVEQQILEANTILEAFGNAKTVRNDN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGE--HLKSDLLLEGFNSYRFLS-NGNI 336
Cdd:cd14883 132 SSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK-ERNSDQASMPDNTAAQKLCHLLGLNVMEFTR 415
Cdd:cd14883 212 RIDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 416 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQM 495
Cdd:cd14883 292 ALTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 496 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLI 575
Cdd:cd14883 371 CINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLH 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 576 QEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrIVGLDQVAGM 655
Cdd:cd14883 448 AAHEKHPYYEKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSIS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 656 NETAFGATyKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQG 735
Cdd:cd14883 527 LGGDTTSR-GTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEG 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 736 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14883 605 FPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-792 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 628.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavsgplfygeLERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG------------------------------IENEILQTNPILEAFGNAKTLRNDN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-IPI 338
Cdd:cd01383 130 SSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVMEFTRAIL 418
Cdd:cd01383 210 DGVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 419 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCIN 498
Cdd:cd01383 290 TRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCIN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 499 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLIQEQ 578
Cdd:cd01383 370 YANERLQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 579 GTHTKFQKPRqlkDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELwkdvdrivgldqVAGMNET 658
Cdd:cd01383 447 KSNSCFKGER---GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF------------ASKMLDA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 659 AFGATYKTKKGMF----RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd01383 511 SRKALPLTKASGSdsqkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRS 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 735 GFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd01383 591 GYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-792 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 607.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPPespkpvklqaqhavsgplfygeLERQLLQANPILESFGNAKTVKN 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS----------------------VEQQVLESNPLLEAFGNAKTVRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-I 336
Cdd:cd01384 135 NNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKL---CHLLGLNVMEF 413
Cdd:cd01384 215 ELDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKAL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 414 TRAILSpRIKVGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSF 492
Cdd:cd01384 295 EDALCK-RVIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 493 EQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVD 572
Cdd:cd01384 373 EQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 573 KLIQEQGTHTKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRivgldqv 652
Cdd:cd01384 450 KLYQTLKDHKRFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 653 agmnetafgatYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 731
Cdd:cd01384 521 -----------EGTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 732 CRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIQALELDPnlFRIGQSKIFFR 792
Cdd:cd01384 590 SCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-792 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 598.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavsgplfygELERQLLQANPILESFGNAKTVKND 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS------------------------------WIEQQILEANPILEAFGNAKTIRND 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN-IP 337
Cdd:cd01381 131 NSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK--ERNSDQASMPDNTAAQKLCHLLGLNVMEFTR 415
Cdd:cd01381 211 CEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 416 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFQLNSFE 493
Cdd:cd01381 291 ALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 494 QMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVD 572
Cdd:cd01381 371 QLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 573 KLIQEQGTHTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgldqv 652
Cdd:cd01381 447 KLHSTHGNNKNYLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI-------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 653 agmnetAFGATYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 732
Cdd:cd01381 518 ------SMGSETRKKS---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIR 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 733 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd01381 589 KAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-792 |
1.08e-177 |
|
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: 554.77 E-value: 1.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavsgplfygeLERQLLQANPILESFGNAKTVKND 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG------------------------------VEQRVLLANPILEAFGNAKTLRNN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNSYRFLSNGN-IP 337
Cdd:cd14872 131 NSSRFGKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCH---LLGLNVMEFT 414
Cdd:cd14872 209 VEGVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 415 RAILSPRIKV-GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFE 493
Cdd:cd14872 289 EALTSRLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 494 QMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDK 573
Cdd:cd14872 369 QLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 574 LIQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgLDQva 653
Cdd:cd14872 446 ANQTHAAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQ-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 gmnetafgatyKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14872 520 -----------KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 734 QGFPNRIVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14872 586 TGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-792 |
1.84e-177 |
|
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: 554.17 E-value: 1.84e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKN 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGA-----------------------------GPIEQRILEANPLLEAFGNAKTVRN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLegfnsyrflsngnip 337
Cdd:cd01382 132 NNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK--------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERN-SDQASMPDNTAAQKL---CHLLGLNVMEF 413
Cdd:cd01382 197 DPLLDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSdSGGGCNVKPKSEQSLeyaAELLGLDQDEL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 414 -----TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFQ 488
Cdd:cd01382 277 rvsltTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 489 LNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDK 568
Cdd:cd01382 355 VNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQ 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 569 TFVDKLIQEQGTHTKFQKPRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELW 640
Cdd:cd01382 432 HFTSAVHQKHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 641 KDvdrivgldqvagmnETAFGATYKTKKG--MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 718
Cdd:cd01382 512 ES--------------STNNNKDSKQKAGklSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILS 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 719 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd01382 578 QLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-792 |
2.17e-174 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 546.68 E-value: 2.17e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhniPPESPKPVKLQAQHAvsgplfyGELERQLLQANPILESFGNAK 253
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGA----SGEGEAASEAIEQTL-------GSLEDRVLSSNPLLESFGNAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 254 TVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSN 333
Cdd:cd14890 150 TLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 334 GNIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASmpDNTAAQKLCH---LLGLNV 410
Cdd:cd14890 230 ECSSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 411 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLN 490
Cdd:cd14890 308 DALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 491 SFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--D 567
Cdd:cd14890 387 TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 568 KTFVDKLIQEQGT-------------HTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdk 634
Cdd:cd14890 465 KKFVSQLHASFGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 635 fvgelwkdvdrivgldqvagmnetafgatyKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 714
Cdd:cd14890 542 ------------------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGL 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 715 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14890 590 DCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-792 |
2.10e-170 |
|
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: 535.49 E-value: 2.10e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnippesPKPVKLQAQhavsgplfygelerQLLQANPILESFGNAKTVKND 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------------QRRNNLVTE--------------QILEATPLLEAFGNAKTVRND 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNG-NIP 337
Cdd:cd01387 132 NSSRFGKYLEVFFEG-GVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK---ERNSDQASMPDNTAAQKLCHLLGLNVMEFT 414
Cdd:cd01387 211 IAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 415 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFQLNSFEQ 494
Cdd:cd01387 291 KALTFKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 495 MCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL 574
Cdd:cd01387 370 LCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKC 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 575 IQEQGTHTKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAG 654
Cdd:cd01387 447 HYHHALNELYSKPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 655 MNetafgATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd01387 525 GK-----GRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 735 GFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIQALELDP-NLFRIGQSKIFFR 792
Cdd:cd01387 600 GYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-792 |
2.03e-168 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 530.12 E-value: 2.03e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkpvklqaqhavsgplfygeleRQLLQANPILESFGNAKTVKN 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI--------------------------KKIIEVNPLLESFGNAKTVRN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNSYRFL-SNGNI 336
Cdd:cd14903 132 DNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASM--PDNTAAQKLCHLLGLNVMEFT 414
Cdd:cd14903 210 KIEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 415 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQ 494
Cdd:cd14903 290 KALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 495 MCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKL 574
Cdd:cd14903 369 FCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 575 iqeQGTHTKFQK----PRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDvdrIVGLD 650
Cdd:cd14903 445 ---SSIHKDEQDviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESP 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 651 QVAGMNETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 730
Cdd:cd14903 517 AAASTSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIR 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 731 ICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIQALELD-PNLFRIGQSKIFFR 792
Cdd:cd14903 597 ISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-792 |
4.34e-161 |
|
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: 509.72 E-value: 4.34e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespKPVKLQAQHavsgplfygeLERQLLQANPILESFGNAKTVKN 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLE-----------LSLKEKTSC----------VEQAILESSPIMEAFGNAKTVYN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLS-NGNI 336
Cdd:cd14873 140 NNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKkerNSDQASMPDNTAAQKLCHLLGLNVMEFTRA 416
Cdd:cd14873 220 EDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 417 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQM 495
Cdd:cd14873 297 LTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 496 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLI 575
Cdd:cd14873 374 NINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 576 QEQGTHTKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgldqvAGM 655
Cdd:cd14873 450 SQHANNHFYVKPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 656 NETAFGATYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQG 735
Cdd:cd14873 520 NQDTLKCGSKHRR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAG 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 736 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKqaCERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14873 597 YAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-790 |
5.94e-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: 509.72 E-value: 5.94e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEIPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklQAQHAVSgplfYGELERQLLQANPILES 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATT-----------------HGQNATE----RENVRDRVLESNPILEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 249 FGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSY 328
Cdd:cd14901 140 FGNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 329 RFL--SNGNIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF-KKERNSDQASMPDNTAAQKLCHL 405
Cdd:cd14901 220 KYLnsSQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 406 LGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGF 484
Cdd:cd14901 300 LGLDMDVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 485 EIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIDLIErpANPPGVLALLDEEC 560
Cdd:cd14901 380 EIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQC 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 561 WFPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGElw 640
Cdd:cd14901 453 LLPRGNDEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS-- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 641 kdvdrivgldqvagmnetafgatyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 720
Cdd:cd14901 531 --------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQL 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 721 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERM-----IQALELDPNLFRIGQSKIF 790
Cdd:cd14901 579 RCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMsqlqhSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-792 |
8.29e-161 |
|
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: 510.38 E-value: 8.29e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLahVASSHKGrkdhnippespkpvklqaqHAvSGplfygeLERQLLQANPILESFGNAKTVKND 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG-------------------YG-SG------VEQTILGAGPVLEAFGNAKTAHNN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLS-NGNIP 337
Cdd:cd01385 133 NSSRFGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKER-NSDQASMPDNTAAQKL-CHLLGLNVMEFTR 415
Cdd:cd01385 213 LEGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 416 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFQLNS 491
Cdd:cd01385 293 ALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 492 FEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFV 571
Cdd:cd01385 372 FEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 572 DKLIQEQGTHTKFQKPrQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELwkdvdriVGLDQ 651
Cdd:cd01385 449 AKFKQQHKDNKYYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDP 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 652 VA----GMNETAFGATY--------------------------------KTKKGMfrTVGQLYKESLTKLMATLRNTNPN 695
Cdd:cd01385 520 VAvfrwAVLRAFFRAMAafreagrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPF 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 696 FVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMiqal 775
Cdd:cd01385 598 FIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL---- 673
|
730
....*....|....*..
gi 1604804596 776 ELDPNLFRIGQSKIFFR 792
Cdd:cd01385 674 NLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-754 |
1.98e-158 |
|
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: 503.07 E-value: 1.98e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvklqaqhavsgplfygELERQLLQANPILESFGNAKTVKN 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS--------------------------LVEAQVLESNPLLEAFGNARTLRN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFD---------VIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSY 328
Cdd:cd14888 134 DNSSRFGKFIELQFSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 329 RFLSNGNIP------------------------IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK 384
Cdd:cd14888 214 LAKGADAKPisidmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 385 ERNSDQASMPDNTAAQKL---CHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRI 461
Cdd:cd14888 294 NEACSEGAVVSASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 462 NKALDRTKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID 541
Cdd:cd14888 374 NESIGYSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 542 LIErpANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLN 621
Cdd:cd14888 453 LLQ--EKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 622 DNVATLLHQSTDKFVGELWKD-VDRIVGLdqvagmnetafgatyKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCI 700
Cdd:cd14888 529 VDAQEVIKNSKNPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCI 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 701 IPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 754
Cdd:cd14888 594 KPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-792 |
5.25e-158 |
|
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: 501.60 E-value: 5.25e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEI---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKPVKLQAQhavsgplfygeLERQLLQANPILESFGN 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHES-----------IEECVLLSNLILEAFGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 252 AKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFL 331
Cdd:cd14892 144 AKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 332 SNGN-IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF----KKERNSDQASMPDNTAaqKLCHLL 406
Cdd:cd14892 224 NQGNcVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFeenaDDEDVFAQSADGVNVA--KAAGLL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 407 GLNVMEFTRAILSPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFI 476
Cdd:cd14892 302 GVDAAELMFKLVTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 477 GILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALL 556
Cdd:cd14892 382 GILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 557 DEECWFP-KATDKTFVDKLIQEQ-GTHTKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDk 634
Cdd:cd14892 459 EEQMLLKrKTTDKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 635 fvgelwkdvdrivgldqvagmnetafgatyktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 714
Cdd:cd14892 536 ------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCE 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 715 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IQALELDPNLFRIGQSK 788
Cdd:cd14892 573 LVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTK 652
|
....
gi 1604804596 789 IFFR 792
Cdd:cd14892 653 VFLR 656
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-792 |
6.13e-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: 500.65 E-value: 6.13e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLahvasshkgrkdhnippespkpVKLqaqhavsGPLFYGELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd01379 82 SGAGKTESANLLVQQL----------------------TVL-------GKANNRTLEEKILQVNPLMEAFGNARTVINDN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGagehLKSDLLLEGFNS-------YRFLS 332
Cdd:cd01379 133 SSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKLpenkpprYLQND 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 333 NGNIPIPGQQD--KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF----KKERNSDQASMPDNTAAQKLCHLL 406
Cdd:cd01379 209 GLTVQDIVNNSgnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 407 GLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGF 484
Cdd:cd01379 289 GIEADELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 485 EIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFP 563
Cdd:cd01379 369 ENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 564 KATDKTFVDKLiqEQGTHTKFQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGElwkdv 643
Cdd:cd01379 445 KATDQTLVEKF--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ----- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 644 drivgldqvagmnetafgatyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 723
Cdd:cd01379 517 -----------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYT 567
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 724 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIQALELDPnlFRIGQSKIFFR 792
Cdd:cd01379 568 GVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-792 |
8.51e-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: 494.59 E-value: 8.51e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVASShkgrkDHnippespkpvklqaqhavsgplfyGELERQLLQANPILESFGNAKTVKN 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----DD------------------------SDLLDKIVQINPLLEAFGNASTVMN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIP 337
Cdd:cd14897 132 DNSSRFGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQD-------KDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNV 410
Cdd:cd14897 212 RPVFNDseeleyyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 411 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEI 486
Cdd:cd14897 292 VELTEALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFEN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 487 FQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKAT 566
Cdd:cd14897 372 FKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQST 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 567 DKTFVDKLIQEQGTHTKFQKPrqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKdvdri 646
Cdd:cd14897 449 DSSLVQKLNKYCGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 647 vgldqvagmnetafgatyktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 726
Cdd:cd14897 522 -----------------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLM 572
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 727 EGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIQALELDPnlFRIGQSKIFFR 792
Cdd:cd14897 573 EIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-752 |
2.77e-144 |
|
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: 462.47 E-value: 2.77e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEIPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkdhnippESPKPVKLQAQHAVSGplfygeLERQLLQAN 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------------DNNLAASVSMGKSTSG------IAAKVLQTN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 244 PILESFGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEhlksdllle 323
Cdd:cd14900 143 ILLESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE--------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 324 gfnsyrflsngnipipGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSD-QASMPDNTAAQKL 402
Cdd:cd14900 214 ----------------AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 403 ------CHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGA 473
Cdd:cd14900 278 wsrdaaATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 474 S-FIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGV 552
Cdd:cd14900 358 LhFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 553 LALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQST 632
Cdd:cd14900 435 LSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 633 dkfvgelwkdVDrivgldqvagmnetafgatyktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 712
Cdd:cd14900 507 ----------VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYE 550
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1604804596 713 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 752
Cdd:cd14900 551 RERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-755 |
1.71e-141 |
|
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: 456.41 E-value: 1.71e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EIPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKLQAQhavsgplfygELERQLLQANPILESF 249
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKSTK----------SIEQKILSCNPILEAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 250 GNAKTVKNDNSSRFGKFIRINFD-VIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLE----G 324
Cdd:cd14907 151 GNAKTVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 325 FNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFK-KERNSDQASMPDNTAA-QKL 402
Cdd:cd14907 231 DRYDYLKKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQII 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 403 CHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASF 475
Cdd:cd14907 311 AKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 476 IGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIDLIERPanPPGVL 553
Cdd:cd14907 391 IGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 554 ALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTD 633
Cdd:cd14907 468 NLLDDSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 634 KFVGELWkdvdriVGLDQVAGMNETAFGATYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEP 713
Cdd:cd14907 547 RIISSIF------SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQ 616
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1604804596 714 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 755
Cdd:cd14907 617 GYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-792 |
7.20e-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: 451.67 E-value: 7.20e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 101 VLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavsgplfygELERQLLQANPILESFGNAKTVK 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS------------------------------QLEQQILQVNPLLEAFGNAQTVM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 257 NDNSSRFGKFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG--AGEHLKSDLLLEGFnsYRFLSN- 333
Cdd:cd14889 133 NDNSSRFGKYIQLRFRN-GHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNg 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 334 -GNIPIPgQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFkkERNSDQASMPDNTAAQKL---CHLLGLN 409
Cdd:cd14889 210 aGCKREV-QYWKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 410 VMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIF 487
Cdd:cd14889 287 EEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 488 QLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATD 567
Cdd:cd14889 367 AVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 568 KTFVDKLIQEQGTHTKFQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWK-DVDRI 646
Cdd:cd14889 444 ESFVDKLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 647 VGLDQVAGM---NETAFGATYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 723
Cdd:cd14889 522 GTLMPRAKLpqaGSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYN 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 724 GVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIQALELDPnlFRIGQSKIFFR 792
Cdd:cd14889 596 GLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-792 |
1.92e-138 |
|
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: 446.80 E-value: 1.92e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 172 QSILCTGESGAGKTENTKKVIQYLAHvaSSHKGRKDHNipPESPKPVKLQAQHAVSgplfygeLERQLLQANPILESFGN 251
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTT--RAVGGKKASG--QDIEQSSKKRKLSVTS-------LDERLMDTNPILESFGN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 252 AKTVKNDNSSRFGKFIRINFDVIGY-IVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRF 330
Cdd:cd14891 145 AKTLRNHNSSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 331 LSNGN-IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNS----DQASMPDNTAAQKLCHL 405
Cdd:cd14891 225 LNQSGcVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSegeaEIASESDKEALATAAEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 406 LGLNVMEFTRAILSPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGF 484
Cdd:cd14891 305 LGVDEEALEKVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 485 EIFQL-NSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIDLIErpANPPGVLALLDE 558
Cdd:cd14891 383 ESFETkNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIA--SKPNGILPLLDN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 559 ECWFPKATDKTFVDKLIQEQGTHTKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQStDKFvg 637
Cdd:cd14891 455 EARNPNPSDAKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKF-- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 638 elwkdvdrivgLDQVAGMNEtafgatyktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 717
Cdd:cd14891 531 -----------SDQMQELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVV 569
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 718 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14891 570 DQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-792 |
8.61e-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: 431.29 E-value: 8.61e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkpvklqaqhavsgplfygelerQLLQANPILESFGNAKTVKN 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA--------------------------KVIDVNPLLESFGNAKTTRN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFL--SNGN 335
Cdd:cd14904 132 DNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 336 IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK--ERNSDQASMpdnTAAQKLCHLLGLNVMEF 413
Cdd:cd14904 212 MQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKsdENGSRISNG---SQLSQVAKMLGLPTTRI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 414 TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFE 493
Cdd:cd14904 289 EEALCNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 494 QMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDK 573
Cdd:cd14904 369 QFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 574 L---IQEQGTHTKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDrivgld 650
Cdd:cd14904 445 IrtnHQTKKDNESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 651 qvaGMNETAFGATYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 730
Cdd:cd14904 517 ---APSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIR 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 731 ICRQGFPNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIQAL-ELDPNLFRIGQSKIFFR 792
Cdd:cd14904 593 ITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-792 |
1.14e-132 |
|
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: 430.74 E-value: 1.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkpvklqaqhavsgplfygeleRQLLQANPILESFGNAKTVKND 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL--------------------------RQPEDVLPILESFGHAKTILNA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNI-P 337
Cdd:cd14896 132 NASRFGQVLRLHLQH-GVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKK-ERNSDQ-ASMPDNTAAQKLCHLLGLNVMEFTR 415
Cdd:cd14896 211 LQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSsERESQEvAAVSSWAEIHTAARLLQVPPERLEG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 416 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQ 494
Cdd:cd14896 291 AVTHRVTETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 495 MCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKL 574
Cdd:cd14896 371 LCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKC 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 575 IQEQGTHTKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAG 654
Cdd:cd14896 448 HYHHGDHPSYAKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 655 mnetafgatyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd14896 526 ------------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSE 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 735 GFPNRIVFQEFRQRYEILTpNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14896 588 GFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-792 |
1.67e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 431.64 E-value: 1.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------IPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhavsGPLFYGELERQLLQANPILES 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEG------------------EELGKLSIMDRVLQSNPILEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 249 FGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGE--------HLKSDL 320
Cdd:cd14908 143 FGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 321 LLEGFNSYRFLSNGNIPIPGQ-QDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNsDQASMPDNTAA 399
Cdd:cd14908 223 GLQLPNEFHYTGQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 400 QK----LCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGA 473
Cdd:cd14908 302 EKclarVAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 474 SfIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVL 553
Cdd:cd14908 382 S-VGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGIL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 554 ALLDEECWFP-KATDKTFVDKLI--------QEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdn 623
Cdd:cd14908 458 TMLDDECRLGiRGSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 624 vatllhqstdkfvgelwkdvdrivgldqvagmnetafgatyKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPN 703
Cdd:cd14908 536 -----------------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPN 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 704 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQ 766
Cdd:cd14908 574 DAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDL 652
|
730 740 750
....*....|....*....|....*....|
gi 1604804596 767 ACERMIQALELDPNL----FRIGQSKIFFR 792
Cdd:cd14908 653 VKGVLSPAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-754 |
3.41e-129 |
|
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: 423.53 E-value: 3.41e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEIPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 169 REDQSILCTGESGAGKTENTKKVIQYLAHVasshkGRKDHNIPPESPKPVKLQaqhavsgplfygeleRQLLQANPILES 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-----GRDQSSTEQEGSDAVEIG---------------KRILQTNPILES 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 249 FGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSY 328
Cdd:cd14902 141 FGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 329 RFLSN---GNIPIPGQQDKDN--FQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDqasmpDNTAAQKLC 403
Cdd:cd14902 221 ELLNSygpSFARKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQE-----DATAVTAAS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 404 --------HLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------R 467
Cdd:cd14902 296 rfhlakcaELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 468 TKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPA 547
Cdd:cd14902 376 DEDEELATIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 548 NppGVLALLDEECWFPKATDKTFVDKLIQeqgTHTKfqkprqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATL 627
Cdd:cd14902 455 N--GLFSLLDQECLMPKGSNQALSTKFYR---YHGG---------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDI 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 628 LHQSTDkfvgelwkDVDRIVGLDQVAGMNETAFGATYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHE 705
Cdd:cd14902 521 LSSSSN--------EVVVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEV 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1604804596 706 KRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 754
Cdd:cd14902 593 KKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-845 |
1.33e-124 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 414.04 E-value: 1.33e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 97 NEASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEI-PPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvklqaQHAVsgplfygelerqlLQANPILESFGNAKTV 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI------------QNAI-------------MAANPVLEAFGNAKTI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 256 KNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGN 335
Cdd:PTZ00014 240 RNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKC 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 336 IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF--KKERNSDQASM--PDNTAA-QKLCHLLGLNV 410
Cdd:PTZ00014 320 LDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDY 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 411 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFQLN 490
Cdd:PTZ00014 400 ESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 491 SFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTF 570
Cdd:PTZ00014 479 SLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKF 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 571 VDKLIQEQGTHTKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGld 650
Cdd:PTZ00014 556 VSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG-- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 651 qvagmnetafgatyKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 730
Cdd:PTZ00014 633 --------------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQ 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 731 ICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFF-RTGV--LAHLEEERDLKI 807
Cdd:PTZ00014 697 LRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAAkeLTQIQREKLAAW 776
|
730 740 750
....*....|....*....|....*....|....*...
gi 1604804596 808 TDIIIYFQSVCRGYLARKAFAKKqqqlsaLKVLQRNCA 845
Cdd:PTZ00014 777 EPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
105-753 |
3.36e-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: 406.26 E-value: 3.36e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 105 LKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------IPPHIYAISESAYRCMLQ-------DRE 170
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhepgaSKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvklQAQHAVSGPlfygelerQLLQANPILESFG 250
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSS------------KRRRAISGS--------ELLSANPILESFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 251 NAKTVKNDNSSRFGKFIRINF-----DVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGF 325
Cdd:cd14895 140 NARTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 326 NS--YRFLSNGNIPI--PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSD------------ 389
Cdd:cd14895 220 SAqeFQYISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapc 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 390 ---QASMPDNTAAQKL---CHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINK 463
Cdd:cd14895 300 rlaSASPSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 464 ALDRTK----------RQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFG 533
Cdd:cd14895 380 ASPQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 534 LDlQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRqlKDKAD--FCIIHYAGKVDYKADE 611
Cdd:cd14895 460 DN-SVCLEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 612 WLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVAGMNETAFGATYKTKKGmfrtVGQLYKESLTKLMATLRN 691
Cdd:cd14895 535 FCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQ 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 692 TNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 753
Cdd:cd14895 611 TQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-792 |
2.51e-122 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 402.84 E-value: 2.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPEspkpvKLQAqhavsgplfygelerqllqANPILESFGNAKTVKND 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE-----KLNA-------------------ALTVLEAFGNVRTALNG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSyrflSNGNIPI 338
Cdd:cd01386 133 NATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKD------NFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNVME 412
Cdd:cd01386 209 PLQKPEDkqkaaaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 413 FTRAI------------LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILD 480
Cdd:cd01386 289 LSSAIfkhhlsggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 481 IAGfeiFQLN---------SFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERP---AN 548
Cdd:cd01386 368 TPG---FQNPahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqAL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 549 PP---------GVLALLDEECWFPKATDKTFVDKLIQEQG--THTKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLM 614
Cdd:cd01386 445 VRsdlrdedrrGLLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 615 K-NMDPLNDNVATLLHQSTDKFvgelwkdvdrivgldqvAGMnetafgatykTKKGMFRTVgqlyKESLTKLMATLRNTN 693
Cdd:cd01386 525 AaKENPSAQNATQLLQESQKET-----------------AAV----------KRKSPCLQI----KFQVDALIDTLRRTG 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 694 PNFVRCIIPNHEkrAGKLEPH--------------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 759
Cdd:cd01386 574 LHFVHCLLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKK 651
|
730 740 750
....*....|....*....|....*....|....*...
gi 1604804596 760 GF-----MDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd01386 652 LGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-790 |
1.43e-121 |
|
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: 399.36 E-value: 1.43e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EIPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvklqaQHAVsgplfygelerqlLQANPILESFGNAKTVKN 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI------------QTAI-------------MAANPVLEAFGNAKTIRN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIP 337
Cdd:cd14876 133 NNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 338 IPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKErnsDQASMPDntAA----------QKLCHLLG 407
Cdd:cd14876 213 VPGIDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 408 LNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEI 486
Cdd:cd14876 288 LDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 487 FQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKAT 566
Cdd:cd14876 366 FKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 567 DKTFVDKLIQEQGTHTKFqKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRI 646
Cdd:cd14876 443 DEKFVSACVSKLKSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 647 VGldqvagmnetafgatyKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 726
Cdd:cd14876 522 KG----------------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSIL 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 727 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIF 790
Cdd:cd14876 584 EALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-790 |
1.22e-115 |
|
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: 382.66 E-value: 1.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEIPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPEspkpvklqaqhavsgplfygeLERQLLQANPILESFGNAKT 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER---------------------IEQRILNSNPVMEAFGNACT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 255 VKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNG 334
Cdd:cd14880 140 LRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 335 NIPIpgqqDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTA---AQKLCHLLGLNVM 411
Cdd:cd14880 220 ERNL----EEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPED 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 412 EFTRAILSPRIKVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQL 489
Cdd:cd14880 296 HLLETLQIRTIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 490 NSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKT 569
Cdd:cd14880 376 NSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 570 FVDKLIQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGL 649
Cdd:cd14880 453 QLQTRIESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 650 DQVAGMNETAfgatyktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGI 729
Cdd:cd14880 533 EEPSGQSRAP-----------VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETI 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 730 RICRQGFPNRIVFQEFRQRYEILTPN--AIPKGFMDGKQAcermiqalELDPNLFRIGQSKIF 790
Cdd:cd14880 602 HISAAGFPIRVSHQNFVERYKLLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-755 |
3.39e-113 |
|
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: 377.78 E-value: 3.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEIPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 177 TGESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKpvklqaqhavsgplfygeLERQLLQANPILESFGNAKTVK 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSS-NQQQNNNNNNNNNS------------------IEKDILTSNPILEAFGNSRTTK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 257 NDNSSRFGKFIRINFDVIGYIV-GANIETYLLEKSR-AIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEG-FNSYRFL-- 331
Cdd:cd14906 142 NHNSSRFGKFLKIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLda 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 332 ------------SNGNIPIPGQQDKD-NFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERN-SDQASMPDNT 397
Cdd:cd14906 222 rddvissfksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDfSKYAYQKDKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 398 AA--QKLCHLLGLNVMEFTRAILSPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR------ 467
Cdd:cd14906 302 TAslESVSKLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsnd 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 468 ----TKRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLI 543
Cdd:cd14906 382 laggSNKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 544 ERPANppGVLALLDEECWFPKATDKTFVDKLIQE-QGTHTKFQkpRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLND 622
Cdd:cd14906 461 EKKSD--GILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 623 NVATLLHQSTDKFVGELWKdvdrivgldqvagMNETAFGATYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIP 702
Cdd:cd14906 536 DVEDLLLASSNFLKKSLFQ-------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKP 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 703 NHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 755
Cdd:cd14906 602 NQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-792 |
1.36e-110 |
|
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: 368.37 E-value: 1.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEIPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnippespkpvklQAQHAVSGplfygELERQLLQANPILESFGNAKTV 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSN---------------TSQRSIAD-----KIDENLKWSNPVMESFGNARTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 256 KNDNSSRFGKFIRINFD-VIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDL-LLEGFNSYRFLSN 333
Cdd:cd14875 141 RNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 334 GNI----PIPGQ--QDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNsDQASMPDNTAAQKLCHLLG 407
Cdd:cd14875 221 GNTfvrrGVDGKtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 408 LNVMEFTRAILsprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEI 486
Cdd:cd14875 300 LDPAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFEN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 487 FQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKAT 566
Cdd:cd14875 377 FTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 567 DKTFVDKLIQEQGTHTK-FQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELwkdvdr 645
Cdd:cd14875 454 TERFTTNLWDQWANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 646 ivgLDQVAGMNETAfgatyktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 725
Cdd:cd14875 527 ---LSTEKGLARRK------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 726 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIQALE-----LDPNlFRIGQSKIFFR 792
Cdd:cd14875 592 LQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-792 |
7.53e-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: 365.75 E-value: 7.53e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EIPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 173 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavsgplfygELERQLLQANPILESFGNA 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST-----------------------------DVQSLILGSNPLLESFGNA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 253 KTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLS 332
Cdd:cd14886 132 KTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 333 NGNI-PIPGQQDKDNFQETMEAMHIMsFGHEEILAMLKVVSSVLQFGNINFKKERN--SDQASMPDNTAA-QKLCHLLGL 408
Cdd:cd14886 212 ASKCyDAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 409 NVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFE 485
Cdd:cd14886 291 ESSKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 486 IFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECwfpka 565
Cdd:cd14886 367 FFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQC----- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 566 tdktfvdkLIQeQGTHTKFQKPRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDK 634
Cdd:cd14886 439 --------LIQ-TGSSEKFTSSCKSKIKNNsfipgkgsqcnFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNP 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 635 FVGELWKDVDRIVGLdqvagmnetafgatyktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 714
Cdd:cd14886 510 IVNKAFSDIPNEDGN-----------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETK 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 715 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14886 571 SVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-749 |
3.82e-104 |
|
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: 351.71 E-value: 3.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEIPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 168 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPPESPKPVKLQAQhavsgplfygeLERQLLQANPILE 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTT-----------IEEQVLQSNPILE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 248 SFGNAKTVKNDNSSRFGKFIRINF-DVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG-----AGEHLKSDLL 321
Cdd:cd14899 149 AFGNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 322 LEGFNSYRFLSNG--NIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF-----KKERNS--DQAS 392
Cdd:cd14899 229 SGGPQSFRLLNQSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 393 MPDNTAA-----QKLCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR 467
Cdd:cd14899 309 VMSSTTGafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 468 T--------------KRQGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFG 533
Cdd:cd14899 389 QasapwgadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 534 lDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL---IQEQGTHTKFQKPRQLKDKADFCIIHYAGKVDYKAD 610
Cdd:cd14899 469 -NNRACLELFEH--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTID 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 611 EWLMKNMDPLNDNVATLLHQSTDKFVGEL-WKDVDRIVGLDQVAGMNETAFGATYKTKKGMFrTVGQLYKESLTKLMATL 689
Cdd:cd14899 546 GFLAKNKDSFCESAAQLLAGSSNPLIQALaAGSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTV 624
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 690 RNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 749
Cdd:cd14899 625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-792 |
1.53e-93 |
|
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: 320.83 E-value: 1.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvklqaqhavsgplfygeLERQLLQANPILESFG 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-------------------------LEARLLQSGPVLEAFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 251 NAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLlegfnsyrf 330
Cdd:cd14887 136 NAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS--------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 331 lsngnipiPGQQDKD--NFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTA--------AQ 400
Cdd:cd14887 207 --------AGEGDPEstDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 401 KLCHLL-------GLNVMEFTRAILS--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERL 453
Cdd:cd14887 279 DRSHSSevkclssGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 454 FRWLVHRINKALDRTKR-------------QGASFIGILDIAGFEIFQ---LNSFEQMCINYTNEKLQQLFNHTMFILEQ 517
Cdd:cd14887 359 FDAVVARINAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEH 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 518 EEYQREG--IEWSFIDFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDK 568
Cdd:cd14887 439 MLYTQEGvfQNQDCSAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 569 TFVDKLIQEQGTHTKFQK--PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKFVgelwkdvdRI 646
Cdd:cd14887 519 LFYEKLNKNIINSAKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 647 VGLDQVAGMNetafgaTYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 726
Cdd:cd14887 590 VGSKKNSGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMS 660
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 727 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIQALELDPNLFRIGQSKIFFR 792
Cdd:cd14887 661 DLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-756 |
2.62e-93 |
|
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: 315.30 E-value: 2.62e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeIPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvklqaqhavsgplfygELERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT------------------------------SIEKLITAANLILEAFGNAKTQLNDN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDviGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLlegfNSYRFLSNGNIPIP 339
Cdd:cd14898 128 SSRFGKRIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 340 GQQDKDNFQETMEAMHIMSFGHEEILAMlkvvsSVLQFGNINFKkerNSDQASMPDNTAAQKLCHLLGLNVMEFTRAILS 419
Cdd:cd14898 202 LSEKYKMTCSAMKSLGIANFKSIEDCLL-----GILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVK 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 420 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFQLNSFEQMCINY 499
Cdd:cd14898 274 FSIQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINW 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 500 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLiqeqg 579
Cdd:cd14898 351 TNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI----- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 580 thTKFQKPRqLKDKADFCII--HYAGKVDYKADEWLMKNMDPlndnvatllhqstdkfvGELwkdvdRIVGLDQVagmne 657
Cdd:cd14898 422 --KKYLNGF-INTKARDKIKvsHYAGDVEYDLRDFLDKNREK-----------------GQL-----LIFKNLLI----- 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 658 tafgATYKTKKGMFRtvgqLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 737
Cdd:cd14898 472 ----NDEGSKEDLVK----YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFP 543
|
650
....*....|....*....
gi 1604804596 738 NRIVFQEFRQRYEILTPNA 756
Cdd:cd14898 544 QEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-792 |
3.22e-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: 309.05 E-value: 3.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEIPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 176 CTGESGAGKTENTKKVIQYLAHVASShkgrkdhnippespkpvklqaqhavSGPLFYGELErqllQANPILESFGNAKTV 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-------------------------SRTTFDSRFK----HVNCILEAFGHAKTT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 256 KNDNSSRFGKFIRINF-DVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNG 334
Cdd:cd14878 132 LNDLSSCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 335 ----NIPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSDQASMPDNTAAQKLCHLLGLNV 410
Cdd:cd14878 212 mredVSTAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVST 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 411 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIF 487
Cdd:cd14878 292 DELASALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 488 QLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIewsfidfgldlqpCIDLIERPAN-----------PPGVLALL 556
Cdd:cd14878 372 QKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 557 DEECWFPKATDKTFVDKL---IQEQGTHTKFQKPRQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVAT 626
Cdd:cd14878 439 DEESQMIWSVEPNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLF 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 627 LLHQSTDKFVGELwkdvdrivgldqvagmnetafgatYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 706
Cdd:cd14878 519 VMKTSENVVINHL------------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSK 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 707 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACERMIQALELDPnlFRIG 785
Cdd:cd14878 572 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMG 649
|
....*..
gi 1604804596 786 QSKIFFR 792
Cdd:cd14878 650 VRKVFLK 656
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-791 |
9.92e-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: 304.47 E-value: 9.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 96 LNEASVLYNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEIPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKPVKLQAQhavsgplfygelerqLLQANPI 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTKLSSQ---------------ISAAEFV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 246 LESFGNAKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGF 325
Cdd:cd14879 132 LDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 326 NSYRFLSNGN----IPIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF--KKERNSDQASMpDNTAA 399
Cdd:cd14879 212 SDYALLASYGchplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 400 -QKLCHLLGLNVMEFtRAILSPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGA 473
Cdd:cd14879 291 lDIVAAFLGVSPEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 474 SFIGILDIAGfeiFQL------NSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPa 547
Cdd:cd14879 366 TFISLLDFPG---FQNrsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK- 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 548 nPPGVLALLDEEC-WFPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndn 623
Cdd:cd14879 441 -PGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL--- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 624 vatllhqSTDkFVgelwkdvdrivgldqvagmnetafgatyktkkGMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPN 703
Cdd:cd14879 517 -------SPD-FV--------------------------------NLLRGATQL-NAALSELLDTLDRTRLWSVFCIRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 704 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaiPKGFMDGKQACERMIQALELDpnlFR 783
Cdd:cd14879 556 DSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR---GSAAERIRQCARANGWWEGRD---YV 629
|
....*...
gi 1604804596 784 IGQSKIFF 791
Cdd:cd14879 630 LGNTKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-792 |
2.27e-86 |
|
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: 297.31 E-value: 2.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAhvasshKGRKDHNippespkpvklqaqhavsgplfygELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN------------------------EISNTLWDSNFILEAFGNAKTLKNN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14937 127 NSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFgHEEILAMLKVVSSVLQFGNINFK---KERNSDQASMPDNT--AAQKLCHLLGLNVMEF 413
Cdd:cd14937 207 PEIDDAKDFGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 414 TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFQLNSFE 493
Cdd:cd14937 286 KDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 494 QMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVDK 573
Cdd:cd14937 365 QLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 574 LIQEQGTHTKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRIVGLDQVA 653
Cdd:cd14937 441 YTNKFSKHEKYASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 654 GMnetafgaTYKtkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIcR 733
Cdd:cd14937 520 LI-------TFK------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-S 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 734 QGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQAlELDPNLFRIGQSKIFFR 792
Cdd:cd14937 580 FFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-744 |
2.10e-77 |
|
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: 272.16 E-value: 2.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------IPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 171 DQSILCTGESGAGKTENTKKVIQYLahvasshkgrkdhnippespkpvklqaqHAVSGPLFYGELERQLLQANPILESFG 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF----------------------------HYIQTDSQMTERIDKLIYINNILESMS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 251 NAKTVKNDNSSRFGKFIRINFDVI---------GYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG-AGEHLKSDL 320
Cdd:cd14884 133 NATTIKNNNSSRCGRINLLIFEEVentqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 321 LLEGFNSYRFLSN----------GNIPIPG----------QQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNI 380
Cdd:cd14884 213 LVRNCGVYGLLNPdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 381 NFKKernsdqasmpdntaaqkLCHLLGLNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHR 460
Cdd:cd14884 293 AYKA-----------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIED 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 461 INKALDRTKRQGA-----------SFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF 529
Cdd:cd14884 356 INRNVLKCKEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 530 IDFGlDLQPCIDLIERpanppgVLALLDE-----ECWFPKATDKTFVD-----KLIQEQGTHTK-FQKPR--------QL 590
Cdd:cd14884 436 DVAP-SYSDTLIFIAK------IFRRLDDitklkNQGQKKTDDHFFRYllnneRQQQLEGKVSYgFVLNHdadgtakkQN 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 591 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGElwkdvdrivgldqvagmnetafgATYKTKKGM 670
Cdd:cd14884 509 IKKNIFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGN 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 671 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 744
Cdd:cd14884 566 FLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-779 |
3.81e-73 |
|
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: 258.12 E-value: 3.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRHEIPPHIYA-------ISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpkpvklqaqhavsgplfygELERQLLQANPILESFGNA 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET-------------------DAFKHLAAAFTVLRSLGSA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 253 KTVKNDNSSRFGKFIRINFdVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--SYRF 330
Cdd:cd14881 122 KTATNSESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 331 LSNGNIPIPGQQDKDNFQETMEAMHIMSFgheEILAMLKVVSSVLQFGNINFkKERNSDQASMPDNTAAQKLCHLLGLNV 410
Cdd:cd14881 201 LSHGDTRQNEAEDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 411 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIA 482
Cdd:cd14881 277 AALFRGLTTRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 483 GFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIDLIErpANPPGVLALLDEECw 561
Cdd:cd14881 353 GFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 562 FPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvgelwk 641
Cdd:cd14881 429 SPRGTAESYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN--------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 642 dvdrivgldqvagmneTAFGatyktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 721
Cdd:cd14881 499 ----------------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIR 553
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 722 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIQ--ALELDP 779
Cdd:cd14881 554 SLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-750 |
1.53e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 250.27 E-value: 1.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 102 LYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEIPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvklQAQHAVSGPLfygelERQLLQANPILESFGN 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDS------------EGASGVLHPI-----GQQILHAFTILEAFGN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 252 AKTVKNDNSSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAgEH---LKSDLLL-EGFNS 327
Cdd:cd14893 147 AATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 328 YRFLSN-----GNIPIpgqqDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINF------KKERN-------SD 389
Cdd:cd14893 226 FVMLKQadplaTNFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 390 QASMPDNTAAQKL--CHLLGLNVMEF-----TRAILSpriKVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHR 460
Cdd:cd14893 302 AQSCALKDPAQILlaAKLLEVEPVVLdnyfrTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVET 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 461 INKAL----DRTKRQG----ASFIGILDIAGFEIF--QLNSFEQMCINYTNEKLQQLF-NHTMFI----LEQEEYQREG- 524
Cdd:cd14893 379 LNGILggifDRYEKSNivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENr 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 525 -IEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKFQKPRQLKDKAD-------- 595
Cdd:cd14893 459 lTVNSNVDITSEQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskd 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 596 ----FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvgelwkdVDRIVGLDQVAGmNETAFGATYKTKKG-- 669
Cdd:cd14893 537 wrllFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAA-ASSEKAAKQTEERGst 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 670 --MFRTVGQLYKESLT--------------KLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 733
Cdd:cd14893 608 ssKFRKSASSARESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASR 687
|
730
....*....|....*..
gi 1604804596 734 QGFPNRIVFQEFRQRYE 750
Cdd:cd14893 688 SIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-792 |
3.93e-69 |
|
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: 247.70 E-value: 3.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 105 LKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 184 KTENTKKVIQYLAHV-ASSHKGRKDHnippespkpvklqaqhavsgplfygelerqLLQANPILESFGNAKTVKNDNSSR 262
Cdd:cd14905 85 KSENTKIIIQYLLTTdLSRSKYLRDY------------------------------ILESGIILESFGHASTDSNHNSSR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 263 FGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSN-GNIPIPGQ 341
Cdd:cd14905 135 WGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 342 QDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKErnSDQASMPDNTAAQKLCHLLGLNVMEFTRAILSPR 421
Cdd:cd14905 215 DDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 422 IKVGRDYVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFQLNSFEQMCINYTN 501
Cdd:cd14905 293 SMPVNEAVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 502 EKLQQLFNHTMFILEQEEYQREGIEW-SFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVDKLIQEQGT 580
Cdd:cd14905 361 ERLQQIYLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSR 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 581 HTKF-QKPRQlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKF-------------VGELWKDVD-- 644
Cdd:cd14905 434 HHLFgKKPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDak 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 645 --------RIVGL---------DQVAGMNETAFGATYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHE 705
Cdd:cd14905 508 ntakksplSIVKVllscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSK 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 706 KRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIQALELDPNLFRI 784
Cdd:cd14905 588 KTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQV 665
|
....*...
gi 1604804596 785 GQSKIFFR 792
Cdd:cd14905 666 GNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-792 |
7.28e-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: 245.55 E-value: 7.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 99 ASVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrheippHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 178 GESGAGKTENTKKVIQYLAhvasshkgrkdhnippESPKPvKLQAQHAVSgplfygelerqllqANPILESFGNAKTVKN 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT----------------SQPKS-KVTTKHSSA--------------IESVFKSFGCAKTLKN 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 258 DNSSRFGKFIRINFDViGYIVGANIE-TYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNI 336
Cdd:cd14874 120 DEATRFGCSIDLLYKR-NVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 337 PIPGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKERNSD---QASMPDNTAAQK-LCHLLGLNVME 412
Cdd:cd14874 199 TENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 413 FTrAILSPRIKVGrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFQLNSF 492
Cdd:cd14874 279 LV-NFLLPKSEDG-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 493 EQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDF----GLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDK 568
Cdd:cd14874 351 EEFLINSVNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 569 TFVDKLIQEQGTHTKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKdvdrivg 648
Cdd:cd14874 426 SYLEHCNLNHTDRSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 649 ldqvagmNETAfgatykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEG 728
Cdd:cd14874 498 -------SYSS------NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAEL 564
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 729 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKgFMDGKQACERMIQALELD-PNLFRIGQSKIFFR 792
Cdd:cd14874 565 LSFRIKGYPVKISKTTFARQYRCLLPGDIAM-CQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-752 |
5.24e-60 |
|
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: 219.61 E-value: 5.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvklqaqhavsgplfygeLERQLLQANPILESFGNAKTVKNDN 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG------------------------------ATGRVESSIKAILALVNAGTPLNAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 260 SSRFGKFIRINFDVIGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG--AGEHLKSDLLLEGFNsYRFL--SNGN 335
Cdd:cd14882 132 STRCILQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 336 IPIPGQQDKDN-------FQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNINFKKerNSDQASMPDNTAAQKLCHLLGL 408
Cdd:cd14882 211 PPSKLKYRRDDpegnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 409 NVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAG 483
Cdd:cd14882 289 DEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 484 FEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECwfP 563
Cdd:cd14882 366 FECFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--R 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 564 KATDKTFVDKLIQEQgtHTKFQKPRQlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDv 643
Cdd:cd14882 441 SCQDQNYIMDRIKEK--HSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 644 drivglDQVAGMnetafgatyKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLEPHLVLDQL 720
Cdd:cd14882 515 ------SQVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQM 573
|
650 660 670
....*....|....*....|....*....|..
gi 1604804596 721 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 752
Cdd:cd14882 574 RALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-790 |
4.31e-58 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 215.47 E-value: 4.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 100 SVLYNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEIPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 179 ESGAGKTENTKKVIQYLAHVAsshKGRKDHNIPPESPKPVKlqaQHAVSGPLFYGELERQLLQANPILESFGNAKTVKND 258
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQV---KGSRRLPTNLNDQEEDN---IHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 259 NSSRFGKFIRINFDViGYIVGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNSYRFLSNGNIPI 338
Cdd:cd14938 156 NSSRFSKFCTIHIEN-EEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 339 PGQQDKDNFQETMEAMHIMSFGHEEILAMLKVVSSVLQFGNI--------------------NFKKE------RNSDQAS 392
Cdd:cd14938 235 KFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkksllmgknqcgqNINYEtilselENSEDIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 393 MPDNTAAQKL-CHLLGLNVMEFTRAILSPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR- 470
Cdd:cd14938 315 LDENVKNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNi 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 471 -QGASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANp 549
Cdd:cd14938 394 nINTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 550 pGVLALLDEECWFPKATDKTFVDKLIQEQGTHTKF--QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATL 627
Cdd:cd14938 473 -GSLFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 628 LHQSTDKFVGEL-----WKDVDRIVGLDQVAGM--NETAFGATYKTKKGMFRTvgqLYKESLTKLMATLRNTNPNFVRCI 700
Cdd:cd14938 552 VKQSENEYMRQFcmfynYDNSGNIVEEKRRYSIqsALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCM 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 701 IPNHEKRA-GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIQALELDP 779
Cdd:cd14938 629 KPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISN 700
|
730
....*....|.
gi 1604804596 780 NLFRIGQSKIF 790
Cdd:cd14938 701 YEWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-276 |
1.72e-56 |
|
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: 193.72 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEIPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 200 SSHKGRKDHNIPPESPKpvklqaqhavsgplFYGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVIGY 276
Cdd:cd01363 81 FNGINKGETEGWVYLTE--------------ITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1126-1955 |
1.16e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 145.58 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1126 QKNNALKQVRELQAHLA-------ELQEDLESEKMCRSKAEKLKrDLSEELEALKTELEdTLDTTAAQQELRSKREQEva 1198
Cdd:TIGR02168 173 RRKETERKLERTRENLDrledilnELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELEELQEEL-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1199 elkkaideetknheAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKL 1278
Cdd:TIGR02168 249 --------------KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1279 EAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEEtRQKLNLSTQ 1358
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL-RSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1359 irQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFE-TKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMD 1437
Cdd:TIGR02168 394 --QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1438 KMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEarEKDTKALSMAraleeal 1517
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD--EGYEAAIEAA------- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1518 eakeelerfnkqLRAEMEDL-MSSKDDVGKNVHELEKS---KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAM 1593
Cdd:TIGR02168 543 ------------LGGRLQAVvVENLNAAKKAIAFLKQNelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1594 KAQFDRDLQA---------RDEQGEEKKRLLVKQVREMEAELE------------DERKQRTLAVASK-KKLEMDLNELE 1651
Cdd:TIGR02168 611 DPKLRKALSYllggvlvvdDLDNALELAKKLRPGYRIVTLDGDlvrpggvitggsAKTNSSILERRREiEELEEKIEELE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1652 GQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARasrdeifTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQER 1731
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELS-------RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1732 DELADEISNSASGKSSLLEEKRRLEARIAQleeeleeEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQM 1811
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1812 ERQNKDLKAKLAELEGTVKSkFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKE 1891
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1892 QMEKANSRMKQLKRQLEEAEEEATRANAT-RRKLQRELDDA-------TEASEGLTREVSSLKNRLRRGGPV 1955
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1025-1853 |
1.73e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.55 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1025 LEDRISEMTSQ---LTEEEEKAKNLGKVKNKQE-----MMMVDLEERLKKEEKTRQELEKAKRKLDAettdLQDQIVELQ 1096
Cdd:TIGR02168 191 LEDILNELERQlksLERQAEKAERYKELKAELRelelaLLVLRLEELREELEELQEELKEAEEELEE----LTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1097 AQIEELK---FQLTKKEEELQAALARSDEEtlqKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALK 1173
Cdd:TIGR02168 267 EKLEELRlevSELEEEIEELQKELYALANE---ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1174 TELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATaLEELSEQLEQAKRFKSNLEKNKQSLEND 1253
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1254 NkelscdvktlqqakteSEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDK 1333
Cdd:TIGR02168 423 I----------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1334 LNSKLQDSEELRQEetrqKLNLSTQIRQLEVDRNTLleqqeeeeearrnleKQLQMVQSQMFETKKK----LEEDLGS-- 1407
Cdd:TIGR02168 487 LQARLDSLERLQEN----LEGFSEGVKALLKNQSGL---------------SGILGVLSELISVDEGyeaaIEAALGGrl 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1408 ----MEGLEEVKrklqKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAeekT 1483
Cdd:TIGR02168 548 qavvVENLNAAK----KAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---Y 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1484 ISAQYAEERDRAEAEAREKDTKALSM----------ARALEEALEAKEELERFNKqlRAEMEDLmsskddvGKNVHELEK 1553
Cdd:TIGR02168 621 LLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITGGSAKTNSSILER--RREIEEL-------EEKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1554 SKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQGEEKKRLLVKQVREMEAELEDERKQR 1633
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1634 TLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQL 1713
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1714 QEDHAASERARRHAEQERDELADEIsnsasgkSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTE 1793
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1794 LAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQ 1853
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-733 |
2.81e-28 |
|
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: 124.47 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 105 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYSENIIEMYRGKKRHE--IPPHIYAISE---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 160 ----SAYRCMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVAS----------------------------------- 200
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQpalskgseetckvsgstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 201 -----------SHKGRKDHNIPPESPKPVKLQAQHAVSGP----------LFYG--------ELERQL------------ 239
Cdd:cd14894 166 rteeartiallEAKGVEKYEIVLLDLHPERWDEMTSVSRSkrlpqvhvdgLFFGfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 240 ----LQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVIGY---IVGANIETYLLEKSRAIRQA------KDERTFHI 304
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 305 FYQLLAGAGEH-----LKSDLLLEGFN--SYRFLSNGNIPIPG--------QQDKDNFQETMEAMHIMSFGHEEILAMLK 369
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 370 VVSSVLQFGNINFKKERNSDQASMPDN---TAAQKLCHLLGLNVMEFTRAIL---SPRIKVGRDYVQKAQTKEQADFAVE 443
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLmtkSVSLQSTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 444 ALAKATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQMCINYTNEKLQQl 507
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 508 fnhtmfileqEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVdKLIQE 577
Cdd:cd14894 565 ----------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFV-RNIYD 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 578 QGTHTKFQKPRQLKDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVGELWKDVDRiv 647
Cdd:cd14894 634 RNSSRLPEPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ-- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 648 gLDQVAGMNETAFGATYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 727
Cdd:cd14894 712 -LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIR 789
|
....*.
gi 1604804596 728 GIRICR 733
Cdd:cd14894 790 QMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1759 |
7.20e-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: 123.63 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 870 RQEEELQakdeeLVKVKERQLKVENELVEMERKHQQLiEEKNILAEQLHaetELFAEAEEMRVRLLS-RKQELEEILHDL 948
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQLKSL-ERQAEKAERYK---ELKAELRELELALLVlRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 949 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1028
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1029 ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTK 1108
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1109 KEEELQAalarsdeetlqknnalkqvreLQAHLAELQEDLESEKMCRSKAEKlkRDLSEELEALKTELEDTLDTTAAQQE 1188
Cdd:TIGR02168 405 LEARLER---------------------LEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1189 LRSKREQEVAELKKAIDEEtknhEAQIQEMRQRQAtALEELSEQLEQAKRFKSNLEKNKQSLENDNKELScdvktlQQAK 1268
Cdd:TIGR02168 462 ALEELREELEEAEQALDAA----ERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLS------ELIS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1269 TESEHkRKKLEAQLQEFMA-----RATEAERTKGELAERSHKLQT--ELD-------NACTMLEVAEKKG-LKLAKEVDK 1333
Cdd:TIGR02168 531 VDEGY-EAAIEAALGGRLQavvveNLNAAKKAIAFLKQNELGRVTflPLDsikgteiQGNDREILKNIEGfLGVAKDLVK 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1334 LNSKLQDSEELR------QEETRQKLNLSTQIRQlevdRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGS 1407
Cdd:TIGR02168 610 FDPKLRKALSYLlggvlvVDDLDNALELAKKLRP----GYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1408 MEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKT 1483
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1484 ISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQ---LRAEMEDLMSSKDDVGKNVHELEKSKRTLEQ 1560
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1561 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQgEEKKRLLVKQVREMEAELEDERKQRTLAVASK 1640
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL-RSELEELSEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1641 KKLEMDLNELEGQIEaankgrdeavkqlRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAAS 1720
Cdd:TIGR02168 925 AQLELRLEGLEVRID-------------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
|
890 900 910
....*....|....*....|....*....|....*....
gi 1604804596 1721 ERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARI 1759
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1039-1879 |
7.59e-27 |
|
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: 120.17 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1039 EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALA 1118
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1119 RSDEETLQ-KNNALKQVRELQAHLAELQEDLESekmCRSKAEKLKRDLsEELEALKTELEDTLDTTAAQQELRSKREQEV 1197
Cdd:TIGR02169 273 LLEELNKKiKDLGEEEQLRVKEKIGELEAEIAS---LERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1198 AELKKAIDEETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKK 1277
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAE----LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1278 LEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEElrqeetrqklnlst 1357
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR-------------- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1358 QIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVqsqmfetkkkleedLGSMEGLEEVKRKLQKDVE------LTSQCLEE 1431
Cdd:TIGR02169 491 ELAEAEAQARASEERVRGGRAVEEVLKASIQGV--------------HGTVAQLGSVGERYATAIEvaagnrLNNVVVED 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1432 KTMAMDKMEKTK------------NRLQQELDDL--------------MVDLDHQRQ-----------IVSNLEKKQKKF 1474
Cdd:TIGR02169 557 DAVAKEAIELLKrrkagratflplNKMRDERRDLsilsedgvigfavdLVEFDPKYEpafkyvfgdtlVVEDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1475 DQL--------LAE-----------EKTISAQYAEERDRAEAEAREKDtkalSMARALEEALEAKEELERFNKQLRAEME 1535
Cdd:TIGR02169 637 GKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1536 DLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrdlQARDEQGEEKKRLL 1615
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLS 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1616 VKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQ 1695
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1696 SKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQgnmel 1775
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----- 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1776 lndrfrksniqvdnlntELAGERSAAQKSENARQQMERQNKDLkaklaeleGTVKSKFKASIAALEAKILQLEDQLEQEA 1855
Cdd:TIGR02169 945 -----------------EIPEEELSLEDVQAELQRVEEEIRAL--------EPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
|
890 900
....*....|....*....|....
gi 1604804596 1856 KERAAANKIVRRTEKKLKEVMMQV 1879
Cdd:TIGR02169 1000 EERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
991-1761 |
3.37e-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: 117.86 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 991 QLDKVTAEaKIKKMEEDILLLEDQNSKF---LKEKKLLEDRISEMTSQLTEEEEKaknlgkvknkQEMMMVDLEERLKKE 1067
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEGyelLKEKEALERQKEAIERQLASLEEE----------LEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1068 EKTRQELEKAKRKLDAETTD----LQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAE 1143
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1144 LQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID----------EETKNHEA 1213
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlqeelqrlsEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1214 QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKL---EAQLQEFMARAT 1290
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1291 EAERTKGEL----------------AERSHKLQTE------LDNACTMLEVAEKKGLKLAKEV----------DKLNSKL 1338
Cdd:TIGR02169 508 GGRAVEEVLkasiqgvhgtvaqlgsVGERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRRkagratflplNKMRDER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1339 QDSEELRQEETRQ-KLNLSTQIRQLE-----VDRNTLLeqQEEEEEARRnlekqlQMVQSQMFETKKKLEEDLGSMEGLE 1412
Cdd:TIGR02169 588 RDLSILSEDGVIGfAVDLVEFDPKYEpafkyVFGDTLV--VEDIEAARR------LMGKYRMVTLEGELFEKSGAMTGGS 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1413 EVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKTISAQY 1488
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERL 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1489 AEERDRAEAEAREKDTKALSMARALEEALEAKEELErfnkQLRAEMEDLMSSKDDVGknVHELEKSKRTLEQQVEEMRTQ 1568
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLH----KLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEAR 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1569 LEELEDELQATEDAKLRLEVNMQAMKAQFdRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLN 1648
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1649 ELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKE------NEKKLKGLEAEILQLQEDHAASER 1722
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEP 972
|
810 820 830
....*....|....*....|....*....|....*....
gi 1604804596 1723 ARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1761
Cdd:TIGR02169 973 VNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1761 |
2.46e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1075 EKAKRKLDAETTDL---QDQIVELQAQIEELkfqltkkeeELQAALAR------SDEETLQKNNALKQVRELQAHLAELQ 1145
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPL---------ERQAEKAEryrelkEELKELEAELLLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1146 EDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEEtknheaqiQEMRQRQATA 1225
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------EERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1226 LEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHK 1305
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1306 LQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEK 1385
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1386 QLQmvqsqmfetkkKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKtmamdKMEKTKNRLQQELDDLMVDldhqrqivs 1465
Cdd:COG1196 478 ALA-----------ELLEELAEAAARLLLLLEAEADYEGFLEGVKAA-----LLLAGLRGLAGAVAVLIGV--------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1466 nlEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKA-----LSMARALEEALEAKEELERFNKQLRAEMEDLMSS 1540
Cdd:COG1196 533 --EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1541 KD----DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLV 1616
Cdd:COG1196 611 ADaryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1617 KQVREMEAELEDERKQRTLAvaskkklEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQS 1696
Cdd:COG1196 691 EELELEEALLAEEEEERELA-------EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1697 kENEKKLKGLEAEI--------LQLQEDHAASERARRHAEQERDeladeisnsasgkssLLEEKRRLEARIAQ 1761
Cdd:COG1196 764 -ELERELERLEREIealgpvnlLAIEEYEELEERYDFLSEQRED---------------LEEARETLEEAIEE 820
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1066-1761 |
7.45e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 110.16 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1066 KEEKTRQELEKAKRKLDaettdlqdqivELQAQIEELKFQLTKKEEELQAAL-----------ARSDEETLQKNNALKQV 1134
Cdd:TIGR02169 171 KKEKALEELEEVEENIE-----------RLDLIIDEKRQQLERLRREREKAEryqallkekreYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1135 RELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKREQEVAELKKAID------EE 1207
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAekerelED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1208 TKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMA 1287
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1288 RATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKL-------AKEVDKLNSKLQDSEELRQEETRQKLNLSTQIR 1360
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELeeekedkALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1361 QLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVE------LTSQCLEEKTM 1434
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1435 AMDKMEKTK------------NRLQQELDDL--------------MVDLDHQRQ-----------IVSNLEKKQKKFDQL 1477
Cdd:TIGR02169 560 AKEAIELLKrrkagratflplNKMRDERRDLsilsedgvigfavdLVEFDPKYEpafkyvfgdtlVVEDIEAARRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1478 --------LAE-----------EKTISAQYAEERDRAEAEAREKDtkalSMARALEEALEAKEELERFNKQLRAEMEDLM 1538
Cdd:TIGR02169 640 rmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1539 SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrdlQARDEQGEEKKRLLVKQ 1618
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1619 VREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKE 1698
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1699 N-------EKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1761
Cdd:TIGR02169 873 LeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1195-1949 |
9.79e-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: 109.82 E-value: 9.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1195 QEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHK 1274
Cdd:pfam15921 85 HQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1275 RKKLEAQLQEFMARATEAERTKGEL-------AERSHKLQTELDNACTM----LEVAEKKGLK-LAKEVDKLNSKL---Q 1339
Cdd:pfam15921 165 LEDSNTQIEQLRKMMLSHEGVLQEIrsilvdfEEASGKKIYEHDSMSTMhfrsLGSAISKILReLDTEISYLKGRIfpvE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1340 DSEELRQEETRQKLNLSTQ-----IRQL----EVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEG 1410
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQqhqdrIEQLisehEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLES 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1411 --------LEEVKR-------KLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK-- 1473
Cdd:pfam15921 325 tvsqlrseLREAKRmyedkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrl 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1474 FDQLLAEEKTISAQYAEERDR----AEAEAREKDTKALSMARALEEALEAKEELERFNK--QLRAEMEdlmSSKDDVGKN 1547
Cdd:pfam15921 404 WDRDTGNSITIDHLRRELDDRnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvsSLTAQLE---STKEMLRKV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1548 VHELEKSKRTLE---QQVEEMRTQLEELEDELQAT--EDAKLRLEVNMQAmkaqfdRDLQARDEQGEekkrllvkQVREM 1622
Cdd:pfam15921 481 VEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEITKLRSRVDLKL------QELQHLKNEGD--------HLRNV 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1623 EAELEDERKQRTlavASKKKLEMDLNELEGQIE-AANKGRDEAVKQLRK--LQAQMKDYQRELEEARASRDEIFTQSKEN 1699
Cdd:pfam15921 547 QTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1700 EKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEkrrleariaqleeeleeeqgnMELLNDR 1779
Cdd:pfam15921 624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED---------------------YEVLKRN 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1780 FRKSNIQVD----NLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEA 1855
Cdd:pfam15921 683 FRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNAN 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1856 KERaaanKIVRRTEKKLKEVMMQVEDERrhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRAN----------------A 1919
Cdd:pfam15921 762 KEK----HFLKEEKNKLSQELSTVATEK---NKMAGELEVLRSQERRLKEKVANMEVALDKASlqfaecqdiiqrqeqeS 834
|
810 820 830
....*....|....*....|....*....|
gi 1604804596 1920 TRRKLQRELDDATEASEGLTREvSSLKNRL 1949
Cdd:pfam15921 835 VRLKLQHTLDVKELQGPGYTSN-SSMKPRL 863
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1343-1955 |
1.43e-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: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1343 ELRQEETRQKLN--------LSTQIRQLEVDRNTlleqqeeeeeARRNLEKQLQmvqsqmfETKKKLEEDLGSMEGLEEV 1414
Cdd:COG1196 178 ERKLEATEENLErledilgeLERQLEPLERQAEK----------AERYRELKEE-------LKELEAELLLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1415 KRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDR 1494
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1495 AEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1574
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1575 ELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEmDLNELEGQI 1654
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE-EAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1655 EAANKGRDEAVKQLRKLQAQMKDYQRELEEARAsrdeiftqsKENEKKLKGLEAEILQLQEDHAASERARRHAEQER--- 1731
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKA---------ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAlqn 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1732 ---------DELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQ 1802
Cdd:COG1196 551 ivveddevaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1803 KSENARQQMERQNKDLKAKLAELEGtvkskFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDE 1882
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEG-----GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1883 RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEAS----EGLTREVSSLKNRLRRGGPV 1955
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppdlEELERELERLEREIEALGPV 782
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
987-1576 |
2.02e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 105.15 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 987 RQKLQLDKV-TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLK 1065
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1066 KEEKTRQELEKAKR---KLDAETTDLQDQIVELQAQIEELKfqltKKEEELQAALARSDEetlqknnaLKQVRELQAHLA 1142
Cdd:PRK03918 232 ELEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKELKE--------LKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1143 ELQEDLESEKmcrSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ---EVAELKKAID--EETKNHEAQIQE 1217
Cdd:PRK03918 300 EFYEEYLDEL---REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1218 MRQRQA-TALEELSEQLEQAKRFK-------SNLEKNKQSLENDNKELSCDVKTLQQAKTE--------SEHKRKKLeaq 1281
Cdd:PRK03918 377 LKKRLTgLTPEKLEKELEELEKAKeeieeeiSKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKEL--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1282 LQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEK--KGLKLAKEVDKLNSKLQ--DSEELRQ-----EETRQK 1352
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKkyNLEELEKkaeeyEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1353 LN-LSTQIRQLEVDrntlLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDlgSMEGLEEVKRKLQKDVELTSQCLEE 1431
Cdd:PRK03918 534 LIkLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEEL--GFESVEELEERLKELEPFYNEYLEL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1432 KtmamdKMEKTKNRLQQELDDLMVDLDhqrQIVSNLEKKQKKFDQLLAEEKTISAQYAEErdraeaEAREKDTKALSMAR 1511
Cdd:PRK03918 608 K-----DAEKELEREEKELKKLEEELD---KAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1512 ALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1576
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
867-1565 |
6.24e-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: 103.98 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 867 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKN-------ILAEQLHAETELFAEAEEMRVRLLSRKQ 939
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleqqkqILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 940 ELEEILHDLESR-------VEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLE 1012
Cdd:TIGR02168 334 ELAEELAELEEKleelkeeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1013 DQNSKFLKEKKLLEDRISEMTSQLTEE--EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD---AETTD 1087
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAqlqARLDS 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1088 LQDQIVELQAQIEELKFQLTKKE----------------------------EELQAALARSDEETLQKNNALKQVRELQA 1139
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSglsgilgvlselisvdegyeaaieaalgGRLQAVVVENLNAAKKAIAFLKQNELGRV 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1140 HLAELQE----DLESEKMCRSKAEKLKRDLSEELEALKTELEDTL-----------DTTAAQQELRSKREQEVAELKK-- 1202
Cdd:TIGR02168 574 TFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvdDLDNALELAKKLRPGYRIVTLDgd 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1203 ------AIDEETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRK 1276
Cdd:TIGR02168 654 lvrpggVITGGSAKTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1277 KLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLS 1356
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1357 TQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVEL-------TSQCL 1429
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEAL 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1430 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERDRAEAEAREKDTKALS 1508
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1509 MARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1565
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
865-1423 |
5.02e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 865 LLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEI 944
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 945 LHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1024
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1025 LEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKF 1104
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1105 QLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCR---------SKAEKLKRDLSEELEALKTE 1175
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavliGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1176 LEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQslendnk 1255
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL------- 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1256 elscdVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELdnactmlevAEKKGLKLAKEVDKLN 1335
Cdd:COG1196 624 -----GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA---------LLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1336 SKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVK 1415
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
....*...
gi 1604804596 1416 RKLQKDVE 1423
Cdd:COG1196 770 ERLEREIE 777
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1038-1741 |
5.18e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.37 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1038 EEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKaKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAAL 1117
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1118 ARSDEETLQKNNALKQVRELQAHLAELQEDLESEKmcrsKAEKLKRDlSEELEAlKTELEDTLDTTAAQQELRSKREQEV 1197
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK----KAEEAKKK-ADAAKK-KAEEAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1198 AELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLE-----NDNKELSCDVKTLQQAKTESE 1272
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAakkkaDEAKKKAEEKKKADEAKKKAE 1441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1273 HKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEK--KGLKLAKEVDKLNSKLQDSEELRQEETR 1350
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1351 QKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLE 1430
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1431 EKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ----KKFDQLLAEEKTISAQYAEERDRAEAEAR--EKDT 1504
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAK 1681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1505 KALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGK----NVHELEKSKRTLEQ---QVEEMRTQLEELEDELQ 1577
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaeeeNKIKAEEAKKEAEEdkkKAEEAKKDEEEKKKIAH 1761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1578 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKklEMDLNELEGQIEAA 1657
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSK 1839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1658 NKGRDEAvkqlrklqaqmkdyqRELEEARASRDEIftqSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADE 1737
Cdd:PTZ00121 1840 NMQLEEA---------------DAFEKHKFNKNNE---NGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
....
gi 1604804596 1738 ISNS 1741
Cdd:PTZ00121 1902 IPNN 1905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
997-1628 |
1.18e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.54 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 997 AEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGkvknkqemmmvdleERLKKEEKTRQELEK 1076
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------AEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1077 AKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEkmcRS 1156
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1157 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAElKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQA 1236
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1237 KRFKSNLEKNKQSLENDNKELscDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDnactm 1316
Cdd:COG1196 459 EALLELLAELLEEAALLEAAL--AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG----- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1317 LEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQmvqsqmfe 1396
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL-------- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1397 tkkkLEEDLgsmEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQ 1476
Cdd:COG1196 604 ----VASDL---READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1477 LLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKR 1556
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1557 TLEQQVEEMRTQLEELEDELQATEDaklrleVNMQAMkaqfdrdlqarDEQGEEKKRL--LVKQVREMEAELED 1628
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 ... |
1320-1951 |
6.18e-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: 94.09 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1320 AEKKGLKLAKEV-DKLNSKLQDSEELRQEETRQKLNLSTQIRQlevdrNTLLEQQEEEEEARrnLEKQLQMVQSQMFETK 1398
Cdd:pfam01576 9 AKEEELQKVKERqQKAESELKELEKKHQQLCEEKNALQEQLQA-----ETELCAEAEEMRAR--LAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1399 KKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL 1478
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1479 AEektISAQYAEERDRAEAEAREKdTKALSMAraleealeakeelerfnkqlrAEMEDLMSSKDdvgKNVHELEKSKRTL 1558
Cdd:pfam01576 162 SE---FTSNLAEEEEKAKSLSKLK-NKHEAMI---------------------SDLEERLKKEE---KGRQELEKAKRKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1559 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVA 1638
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1639 SKKKLEMDLNELEGQIEAAnKGRDEAVKQLR-KLQAQMKDYQRELE-EARASRDEIFTQSKENEKKLKGLEAEILQLQED 1716
Cdd:pfam01576 293 QRRDLGEELEALKTELEDT-LDTTAAQQELRsKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1717 HAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAG 1796
Cdd:pfam01576 372 KANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1797 ERSAAQKSENARQQMERQNKDLKAKLAElEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVM 1876
Cdd:pfam01576 452 AEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1877 MQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1951
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 ... |
868-1738 |
7.44e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.88 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 868 VTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVrlLSRKQELEEILHD 947
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 948 LESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1027
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1028 RISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKrkldaetTDLQDQIVELQAQIEELKFQLT 1107
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE-------EELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1108 KKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTtaaqQ 1187
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1188 ELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSeQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQA 1267
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS-QKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1268 KTESEHKRKKLEAQLQEFMARATEAErTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKE----VDKLNSKLQDSEE 1343
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVE-ERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpILNLAQLDKATLE 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1344 LRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVE 1423
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1424 LTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERDRAEAEAREK 1502
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEeEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1503 DTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDA 1582
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1583 KLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRD 1662
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1663 EAVKQLRKLQAQMKDYQRE-LEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEI 1738
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
870-1420 |
1.01e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 870 RQEEELQAKD--EELVKVKERQL-KVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQE---LEE 943
Cdd:PRK03918 180 RLEKFIKRTEniEELIKEKEKELeEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrkLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 944 ILHDLESRVEEEEERNQSLQNEKKKMqshiqdleeqldeeeaarQKLQLDKVTAEAKIKKMEEdillLEDQNSKFLKEKK 1023
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKEL------------------KELKEKAEEYIKLSEFYEE----YLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1024 LLEDRISEMTSQLTEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLD------AETTDLQ-DQIVELQ 1096
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEAKAKKEelerlkKRLTGLTpEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1097 AQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHL----AELQEDLESEKMCRSKAE-----KLKRDLSE 1167
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELLEEYTAElkrieKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1168 ELEALKTELEDTLDTTAAQQELRskREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLE-QAKRFKSNLEKn 1246
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgEIKSLKKELEK- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1247 KQSLENDNKELSCDVKTLQQAKTESEHKRKK--------LEAQLQEF------MARATEAERTKGELAERSHKLQTELDN 1312
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELepfyneYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1313 ACTMLEVAEKKGLKLAKEVDKLNSKLqdSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQmvqs 1392
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE---- 704
|
570 580
....*....|....*....|....*...
gi 1604804596 1393 QMFETKKKLEEDLGSMEGLEEVKRKLQK 1420
Cdd:PRK03918 705 EREKAKKELEKLEKALERVEELREKVKK 732
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
998-1598 |
5.48e-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: 84.30 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 998 EAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKA 1077
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1078 KRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQaalarSDEETLQKNNalKQVRELQAHLAELQEDLESEKMCRSK 1157
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL-----NIQKNIDKIK--NKLLKLELLLSNLKKKIQKNKSLESQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1158 AEKLKRDLSEeleaLKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQrQATALEELSEQLEQAK 1237
Cdd:TIGR04523 220 ISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ-NNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1238 RFKSNLEKNKQslENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTML 1317
Cdd:TIGR04523 295 SEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1318 EVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEAR-------RNLEKQLQMV 1390
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIiknnseiKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1391 QSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1470
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1471 QKKFDQLLA--EEKTISAQYAEERDRAEAEAREKDTKALSMaraleeaLEAKEELERFNKQLRAEMEDLMSSKDDVGKNV 1548
Cdd:TIGR04523 533 KKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1549 HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFD 1598
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1215-1826 |
6.35e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1215 IQEMRQRqataLEELSEQLEQAKRFKsnleknkqslendnkelscdvkTLQQAKTESEHKRKKLEaqLQEFMARATEAER 1294
Cdd:COG1196 195 LGELERQ----LEPLERQAEKAERYR----------------------ELKEELKELEAELLLLK--LRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1295 TKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLleqqe 1374
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1375 eeEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLE-----------EVKRKLQKDVELTSQCLEEKTMAMDKMEKTK 1443
Cdd:COG1196 322 --EEELAELEEELEELEEELEELEEELEEAEEELEEAEaelaeaeeallEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1444 NR---LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEA------REKDTKALSMARALE 1514
Cdd:COG1196 400 AQleeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEeallelLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1515 EALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK 1594
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1595 AQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQ 1674
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1675 MKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEisnsasgksslLEEKRR 1754
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA-----------EEEEER 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1755 LEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENA-RQQMERQNKDLKAKLAELE 1826
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdLEELERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1550-1875 |
6.44e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1550 ELEKSKRTLE---QQVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaqfdRDLQARDEQGEEKKRLLVKQVREMEAEL 1626
Cdd:TIGR02169 171 KKEKALEELEeveENIERLDLIIDEKRQQLERLRREREKAE-----------RYQALLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1627 EDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKL--------QAQMKDYQRELEEARASRDEIFTQSKE 1698
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1699 NEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLND 1778
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1779 RFRKSNIQVDNLNTELagersaaQKSENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEAKER 1858
Cdd:TIGR02169 400 EINELKRELDRLQEEL-------QRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQEL 471
|
330
....*....|....*..
gi 1604804596 1859 AAANKIVRRTEKKLKEV 1875
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKL 488
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
867-1761 |
1.90e-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: 82.79 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 867 QVTRQEEELQAKDEELVKVKERQLKVEnelvEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLL-SRKQELEEIL 945
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIE----HNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFqGTDEQLNDLY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 946 HDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLL 1025
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1026 EDRISEMTSQLTEEEEK------AKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQaQI 1099
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEdeaktaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ-QL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EELKFQLTKKEEELQAALArsDEETLQKNNALKQVRELQAHLAELQEDLESEKmcRSKAEKLKrDLSEELEALKTELEDT 1179
Cdd:TIGR00606 467 EGSSDRILELDQELRKAER--ELSKAEKNSLTETLKKEVKSLQNEKADLDRKL--RKLDQEME-QLNHHTTTRTQMEMLT 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1180 LDTTAAQQELRSKREQEVAEL---------KKAIDEETKNHEAQIQEMRQRQATALEELsEQLEQAKRFKSNLEKNKQSL 1250
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKEL-ASLEQNKNHINNELESKEEQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1251 ENDNKELSCDVKTLQQAKTESEHKRKKLE-------------AQLQEFMARATEAE-----------RTKGELAERSHKL 1306
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlagatAVYSQFITQLTDENqsccpvcqrvfQTEAELQEFISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1307 QTELDNACTMLEVAEKKGLKLAKEVDKLNSKLqdseELRQEETRQKlnlstqIRQLEVDRNTLLEQQEEEEEARRNLEKQ 1386
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLA----PGRQSIIDLK------EKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1387 LQMVQSQMFETK--KKLEEDLGSMEGLEEVKRKLQKDVELTSQCLE--EKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQ 1462
Cdd:TIGR00606 771 ETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1463 IVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEA---EAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMS 1539
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1540 SKDDVGKNVH-ELEKSKRTLEQQVEEMRTQLEELEDelqATEDAKLRLEVNMQAMKAQFdrdlqardEQGEEKKRLLVKQ 1618
Cdd:TIGR00606 931 SKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL--------EECEKHQEKINED 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1619 VREMEAELeDERKQRTLAVASKKKLEMDLNELEgQIEAANKGRDEAVKQLRKLQaQMKDYQRELEEARASRDE---IFTQ 1695
Cdd:TIGR00606 1000 MRLMRQDI-DTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLKEMGQMQVLQ-MKQEHQKLEENIDLIKRNhvlALGR 1076
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 1696 SKENEKKLKGLEAEIlqlqedhaaSERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1761
Cdd:TIGR00606 1077 QKGYEKEIKHFKKEL---------REPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMK 1133
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
937-1477 |
2.22e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.42 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 937 RKQELEEIL---HDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVtaeaKIKKMEEDILLLED 1013
Cdd:PRK03918 177 RIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1014 QNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEmMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIV 1093
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1094 ELQAQIEELKfQLTKKEEELQAALARSDEetlqKNNALKQVRELQAHLaelqEDLESEKMCRSKaEKLKRDLsEELEALK 1173
Cdd:PRK03918 332 ELEEKEERLE-ELKKKLKELEKRLEELEE----RHELYEEAKAKKEEL----ERLKKRLTGLTP-EKLEKEL-EELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1174 TELEDTLDTTAAQqelRSKREQEVAELKKAIDEETKNH-----------EAQIQEMRQRQATALEELSEQLEQAKRFKSN 1242
Cdd:PRK03918 401 EEIEEEISKITAR---IGELKKEIKELKKAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1243 LEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTeLDNACTMLEVAEK 1322
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1323 KGLKLAKEVDKLNSKLQDSE-ELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRnLEKQLQMVQSQMFETKKKL 1401
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLkELEELGFESVEELEERLKELEPFYNEYLELKDAEKELER-EEKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1402 EEDLGSMEG----LEEVKRKL-QKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQ 1476
Cdd:PRK03918 636 AETEKRLEElrkeLEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
.
gi 1604804596 1477 L 1477
Cdd:PRK03918 716 L 716
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1060-1735 |
4.29e-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: 81.81 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1060 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVR-ELQ 1138
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRsELE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1139 A----HLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETknheAQ 1214
Cdd:pfam12128 326 AledqHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL----AK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1215 IQEMRQRQATALEELSEQLE----------------QAKRFKSNLEKNKQSL--------ENDNKELSCD-VKTLQQAKT 1269
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALEselreqleagklefneEEYRLKSRLGELKLRLnqatatpeLLLQLENFDErIERAREEQE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1270 ESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLK-LAKEV---DKLNSKLQDSE--- 1342
Cdd:pfam12128 482 AANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEApdwEQSIGKVISPEllh 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1343 ------ELRQEETRQKLNL-STQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQsqmfETKKKLEEDLGSMEG-LEEV 1414
Cdd:pfam12128 562 rtdldpEVWDGSVGGELNLyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR----EKQAAAEEQLVQANGeLEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1415 KRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDdlmvdlDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDR 1494
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA------ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1495 AEAEAREK-----DTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEemrtql 1569
Cdd:pfam12128 712 ARTEKQAYwqvveGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE------ 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1570 eeledelqatedaklRLEVNMQAMkAQFDRDLQardEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKkleMDLNE 1649
Cdd:pfam12128 786 ---------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQLARLIADTK---LRRAK 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1650 LEGQIEAANKGRDEAVKQLRKLQAQMKDYQR-----ELEEARASRDEIFTQSKENEKKLKGLEAEILQLQE-------DH 1717
Cdd:pfam12128 844 LEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEhfknviaDH 923
|
730
....*....|....*...
gi 1604804596 1718 AASERArRHAEQERDELA 1735
Cdd:pfam12128 924 SGSGLA-ETWESLREEDH 940
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1380-1951 |
5.54e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1380 RRNLEKQLQMVQSQMFETKKK-LEEDLGSMEG-LEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRlQQELDDLMVDL 1457
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdLHERLNGLESeLAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1458 DHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERD--RAEAEAREKDTKALSMARALEEALEAkeelerfnkQLRAEME 1535
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARREELEDRDE---------ELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1536 DLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqardEQGEEKKRLL 1615
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV----------------------EDRREEIEEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1616 VKQVREMEAELEDerkqrtlavaskkkLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDE---- 1691
Cdd:PRK02224 390 EEEIEELRERFGD--------------APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcp 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1692 ----------IFTQSKENEKKLKGLEAEILQLQEDHAASErarrhaeqERDELADEISNSASGKSSLLEEKRRLEARIAQ 1761
Cdd:PRK02224 456 ecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1762 LEEELEEEQGNMELLNDRfrksniqVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSkfKASIAALE 1841
Cdd:PRK02224 528 RRETIEEKRERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES--LERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1842 AKILQLEDQLEqeakeraaankivRRTEKklKEVMMQVEDERRhadqykEQMEKANSRMKQLKRQLEEAEEEATRANATR 1921
Cdd:PRK02224 599 AAIADAEDEIE-------------RLREK--REALAELNDERR------ERLAEKRERKRELEAEFDEARIEEAREDKER 657
|
570 580 590
....*....|....*....|....*....|....*
gi 1604804596 1922 -----RKLQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:PRK02224 658 aeeylEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
886-1717 |
5.65e-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: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 886 KERQLKVENELVEMERKHQQLIEEKNilaeQLHAETELFaeaeeMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNE 965
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESN----ELHEKQKFY-----LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 966 KKKMQSHIQDLEEQldeeeaarqklqldkvtaeakiKKMEEDilLLEDQNSKFLKEKKLL---EDRISEMTSQLTEEEEK 1042
Cdd:pfam15921 144 RNQLQNTVHELEAA----------------------KCLKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1043 AknlGKVKNKQEMMMVDLEERLKkeektrQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQ--------LTKKEEELQ 1114
Cdd:pfam15921 200 S---GKKIYEHDSMSTMHFRSLG------SAISKILRELDTEISYLKGRIFPVEDQLEALKSEsqnkiellLQQHQDRIE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1115 AALARSDEE----TLQKNNALKQVRELQAHLAELQEDLESEK---MCR-SKAEKLKRDLSEELEALKTELEDTLDTTAAQ 1186
Cdd:pfam15921 271 QLISEHEVEitglTEKASSARSQANSIQSQLEIIQEQARNQNsmyMRQlSDLESTVSQLRSELREAKRMYEDKIEELEKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1187 QELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscDVKTLQQ 1266
Cdd:pfam15921 351 LVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL--DDRNMEV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1267 AKTESEHKRKKLEAQLQefMARATEAERTKGELAERSHKLQTELDNACTMLEvaekkglklaKEVDKLNSKLQDSEElrQ 1346
Cdd:pfam15921 429 QRLEALLKAMKSECQGQ--MERQMAAIQGKNESLEKVSSLTAQLESTKEMLR----------KVVEELTAKKMTLES--S 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1347 EETRQKLNLSTQIRqlevdrntlleqqeeeeearrnlEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQkdvELTS 1426
Cdd:pfam15921 495 ERTVSDLTASLQEK-----------------------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR---NVQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1427 QClEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKA 1506
Cdd:pfam15921 549 EC-EALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1507 LSMARALEEALEAKEELERFNKQLRAEMEDLM----SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedA 1582
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS---A 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1583 KLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVK--QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKG 1660
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1661 RDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDH 1717
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQH 841
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
936-1894 |
1.26e-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: 80.02 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 936 SRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaARQKLQLDKVTAEAKIKKMEEDILLLEDQN 1015
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-------KLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1016 SKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAEttdlqdqIVEL 1095
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE-------EEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1096 QAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTE 1175
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1176 LedtLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNK 1255
Cdd:pfam02463 379 K---KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1256 ELSCDVKTLQQAKTESehKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLN 1335
Cdd:pfam02463 456 QELKLLKDELELKKSE--DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1336 SKLQDSEELRQEETRQklnlstqirqlEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVK 1415
Cdd:pfam02463 534 LGVAVENYKVAISTAV-----------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1416 RKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKqkkfdqlLAEEKTISAQYAEERDRA 1495
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEG-------LAEKSEVKASLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1496 EAEAREKDTKALSMARALEEALEAKEElerfNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1575
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIK----KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1576 LQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQGEEKKRLLVKQVREMEAELEDERKqrtlAVASKKKLEMDLNELEGQIE 1655
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEKEL---AEEREKTEKLKVEEEKEEKLKAQEEELR----ALEEELKEEAELLEEEQLLI 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1656 AANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKgleaeilqlqedhaaserarrhaEQERDELA 1735
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELL-----------------------LKEEELEE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1736 DEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQN 1815
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1816 KDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQME 1894
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
872-1424 |
1.32e-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: 79.68 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 872 EEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHaetelfaeaeemrvRLLSRKQELEEILHDLESR 951
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN--------------LLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 952 VEEEEERNQSLQ--NEK-KKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSkflKEKKLLEDR 1028
Cdd:TIGR04523 196 LLKLELLLSNLKkkIQKnKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN---KIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1029 ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTR-QELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLT 1107
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1108 KKEEELQaalaRSDEETLQKNNALKQVRELQAHLAELQEDLESEK----MCRSKAEKLKRDLSEELEALKTELEDTLDTt 1183
Cdd:TIGR04523 353 NSESENS----EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndleSKIQNQEKLNQQKDEQIKKLQQEKELLEKE- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1184 aaQQELRSKREQEVAELKKAIDEETKnHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscdvKT 1263
Cdd:TIGR04523 428 --IERLKETIIKNNSEIKDLTNQDSV-KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL----KK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1264 LQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTmlevaEKKGLKLAKEVDKLNSKLQDSEE 1343
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF-----ELKKENLEKEIDEKNKEIEELKQ 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1344 LRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQmvqsqmfETKKKLEEDLGSMEGLEEVKRKLQKDVE 1423
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE-------KAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
.
gi 1604804596 1424 L 1424
Cdd:TIGR04523 649 Q 649
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
865-1347 |
1.62e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 865 LLQVTRQEEELQAKDeelvkVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLlsrkQELEEI 944
Cdd:PRK02224 189 LDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 945 LHDLESRVEEEEERNQSLQNEkkkMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAkikkmeedillLEDQNSKFLKEKKL 1024
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLDDADAEA-----------VEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1025 LEDRISEMTSQLTEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKF 1104
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDAD-------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1105 QLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKM-------------------------CRSKAE 1159
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1160 KLKRDLS----------------EELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID---EETKNHEAQIQEMRQ 1220
Cdd:PRK02224 479 ELEAELEdleeeveeveerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEelrERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1221 RQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKelscdVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELA 1300
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESLER-----IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1604804596 1301 ERSHKLQTELDNActMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQE 1347
Cdd:PRK02224 634 ERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1191-1951 |
2.19e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1191 SKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDnkelscDVKTLQQAKTE 1270
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE------DARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1271 SEHKRKKLEAQLQEfmARATEAERtKGELAERshklqteLDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETR 1350
Cdd:PTZ00121 1149 EDAKRVEIARKAED--ARKAEEAR-KAEDAKK-------AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1351 QklnlSTQIRQLEVDRNTllEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKdveltSQCLE 1430
Cdd:PTZ00121 1219 K----AEDAKKAEAVKKA--EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE-----LKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1431 EKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL--AEEKTISAQYAEERDRAEAEAREKDTKALS 1508
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1509 MARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKsKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1588
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1589 NMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRtlAVASKKKLEmdlnELEGQIEAANKGrDEAVKQL 1668
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK--AEEAKKKAD----EAKKAAEAKKKA-DEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1669 RKLQAqmkDYQRELEEARASRDEIFTQSKENEKKLKglEAEILQLQEDHAASERARRhAEQERDELADEISNSASGKSSL 1748
Cdd:PTZ00121 1520 EAKKA---DEAKKAEEAKKADEAKKAEEKKKADELK--KAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEAR 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1749 LEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQmERQNKDLKAKLAELEGT 1828
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1829 VKSKfkasiaALEAKilqledQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKR--- 1905
Cdd:PTZ00121 1673 DKKK------AEEAK------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeae 1740
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1906 -------QLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:PTZ00121 1741 edkkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
870-1470 |
2.30e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 870 RQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNilAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLE 949
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 950 SRveeeEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEdillledqnSKFLKEKKLLEDRI 1029
Cdd:PTZ00121 1456 AK----KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---------KKKADEAKKAEEAK 1522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1030 SEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaETTDLQDQIVELQAQIEELKFQ---- 1105
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmk 1599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1106 LTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKmcrSKAEKLKRdlSEELEALKTELEdtldttaA 1185
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------A 1667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1186 QQELRSKREQEvaELKKAIDEETKNHEAQIQEmrQRQATALEEL----SEQLEQAKRFKSNLEKNKQSLENDNKELSCDV 1261
Cdd:PTZ00121 1668 KKAEEDKKKAE--EAKKAEEDEKKAAEALKKE--AEEAKKAEELkkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1262 KTLQQAKTESEHKrKKLEAQLQEFMARATEAERTKGELAErshklqteldnactmlEVAEKKGLKLAKEVDKLNSKLQDS 1341
Cdd:PTZ00121 1744 KKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIE----------------EELDEEDEKRRMEVDKKIKDIFDN 1806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1342 EELRQEETRQ--------KLNLSTQIRQLEVDRNTLLEQQEEEEEAR--RNLEKQLQMVQSQMFETKKKLEEDLgsMEGL 1411
Cdd:PTZ00121 1807 FANIIEGGKEgnlvindsKEMEDSAIKEVADSKNMQLEEADAFEKHKfnKNNENGEDGNKEADFNKEKDLKEDD--EEEI 1884
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1412 EEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQElDDLMVDLDHQRQIVSNLEKK 1470
Cdd:PTZ00121 1885 EEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD-EYIKRDAEETREEIIKISKK 1942
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1067-1951 |
2.53e-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: 79.25 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1067 EEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALarsDEETLQKNNALKQVRELQAHLAELQE 1146
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAL---EYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1147 DLESEKmcrskaEKLKRDLSEELEALKTELEDtldttaaqqelrskrEQEVAELKKAIDEETKNHEAQIQEMRQRQATAL 1226
Cdd:pfam02463 237 ERIDLL------QELLRDEQEEIESSKQEIEK---------------EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1227 EELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKL 1306
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1307 QTELDNACTMLEVAEK-KGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEK 1385
Cdd:pfam02463 376 LAKKKLESERLSSAAKlKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1386 QLQMVQSQMFETKKKLEEdlgsMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQrqiVS 1465
Cdd:pfam02463 456 QELKLLKDELELKKSEDL----LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIIS---AH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1466 NLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRA--EMEDLMSSKDD 1543
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvlEIDPILNLAQL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1544 VGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREME 1623
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1624 AELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAvkQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKL 1703
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE--AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1704 KGLEAEILQLQEDHAASERARRHAEQERDELADEIS-NSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRK 1782
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEElRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1783 SNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAAN 1862
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1863 KIVRR-----TEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEG 1937
Cdd:pfam02463 927 AEILLkyeeePEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
890
....*....|....
gi 1604804596 1938 LTREVSSLKNRLRR 1951
Cdd:pfam02463 1007 LIRAIIEETCQRLK 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
921-1257 |
2.99e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.96 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 921 TELFAEAEEMRVRLLSRKQELEEILHDLESRveeeeernqslQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAK 1000
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRI-----------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1001 IKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNL------GKVKNKQEMMMvDLEERLKKEEKTRQEL 1074
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshSRIPEIQAELS-KLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1075 EKAKRKLDAETTDLQDQIVELQAQIEELKFQ---LTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESE 1151
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1152 KmcrSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKnhEAQIQEMRQRQATALEELS- 1230
Cdd:TIGR02169 898 L---RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRALEp 972
|
330 340 350
....*....|....*....|....*....|...
gi 1604804596 1231 ------EQLEQAKRFKSNLEKNKQSLENDNKEL 1257
Cdd:TIGR02169 973 vnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
865-1663 |
3.76e-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: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 865 LLQVTRQEEELQAKDEELVKVKERqLKVENELVEmerKHQQLIEEKNILA--EQLHAETELFAEAEEMRVRLLSRKQELE 942
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLER-LRREREKAE---RYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 943 EILHDLESRVEEEEERNQSLQNEKKKMqshiqdleEQLDEEEAARQKLQLDKVTAEakIKKMEEDILLLEDQNSKFLKEK 1022
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI--------KDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1023 KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEEL 1102
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1103 KFQLTKKEEELQaalaRSDEETLQKNNALKQVRE-----------LQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEA 1171
Cdd:TIGR02169 405 KRELDRLQEELQ----RLSEELADLNAAIAGIEAkineleeekedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1172 LKTELE------DTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALE----------------EL 1229
Cdd:TIGR02169 481 VEKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1230 SEQLEQAKRFK----SNLEKNK-QSLENDNKELSCD-----------------------------VKTLQQAKTESEHKR 1275
Cdd:TIGR02169 561 KEAIELLKRRKagraTFLPLNKmRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMGKYR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1276 K-KLEAQLQEFMARATEAERTKGELAERSHKLQTELdnactmLEVAEKKGlKLAKEVDKLNSKLQDSEELRQEETRQKLN 1354
Cdd:TIGR02169 641 MvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL------QRLRERLE-GLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1355 LSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVE-----LTSQCL 1429
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1430 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKAlsm 1509
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL--- 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1510 araleealeakEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMR-------TQLEELEDELQATEDA 1582
Cdd:TIGR02169 871 -----------EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRkrlselkAKLEALEEELSEIEDP 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1583 KLRLEvnmqamkaqfdrdlqaRDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRD 1662
Cdd:TIGR02169 940 KGEDE----------------EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
.
gi 1604804596 1663 E 1663
Cdd:TIGR02169 1004 A 1004
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
910-1484 |
4.24e-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: 78.14 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 910 KNILAEQLHAETELFAEAEEMRVRLLSRKQELEeilhDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK 989
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELK----NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 990 LQLDKVTAEAKIKKMEEDILLLEDQNSK--------------FLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEM 1055
Cdd:TIGR04523 101 LNSDLSKINSEIKNDKEQKNKLEVELNKlekqkkenkknidkFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1056 MMVDLEER-----------------LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALA 1118
Cdd:TIGR04523 181 EKLNIQKNidkiknkllklelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1119 RSDEETLQKNNALKQVRELQAHLAELQEDL-----ESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1193
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1194 EQEVAELKKAIDEETKNHEAQIQEMRQRQaTALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEH 1273
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1274 KRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKL 1353
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1354 NLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSM--EGLEEVKRKLQKDVELTSQCLEE 1431
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKS 579
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1432 KTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKTI 1484
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNI 636
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
865-1671 |
5.79e-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: 78.09 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 865 LLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETEL----FAEAEEMRVRLLSRKQE 940
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 941 LEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLD-KVTAEAKIKKMEEDILLLEDQNSKFL 1019
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLlKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1099
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EELKF--------QLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLS--EEL 1169
Cdd:pfam02463 528 HGRLGdlgvavenYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIlnLAQ 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1170 EALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQS 1249
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1250 LENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERShklqtELDNACTMLEVAEKKGLKLAK 1329
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL-----KQKIDEEEEEEEKSRLKKEEK 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1330 EVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEvdrntlleqqeeeeearRNLEKQLQMVQSQMFETKKKLEEDLGSME 1409
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL-----------------KAQEEELRALEEELKEEAELLEEEQLLIE 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1410 GLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQivSNLEKKQKKFDQLLAEEKTISAQYA 1489
Cdd:pfam02463 826 QEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE--LEEQKLKDELESKEEKEKEEKKELE 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1490 EERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDdvgknvhELEKSKRTLEQQVEEMRTQL 1569
Cdd:pfam02463 904 EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-------EEEERNKRLLLAKEELGKVN 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1570 EELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNE 1649
Cdd:pfam02463 977 LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDP 1056
|
810 820
....*....|....*....|..
gi 1604804596 1650 LEGQIEAANKGRDEAVKQLRKL 1671
Cdd:pfam02463 1057 FSGGIEISARPPGKGVKNLDLL 1078
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1219-1941 |
6.29e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1219 RQRQATALEELSEQLEQAKRFKSNLEKNKQSLENdnkelscdvktLQQAKTESEHKRKKLEaqlqEFMARATEAERTKGE 1298
Cdd:PRK03918 133 RQGEIDAILESDESREKVVRQILGLDDYENAYKN-----------LGEVIKEIKRRIERLE----KFIKRTENIEELIKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1299 LAERSHKLQTELDNActmlevaEKKGLKLAKEVDKLNSKLQDSEELRQEETrqklNLSTQIRQLEVDRntlleqqeeeee 1378
Cdd:PRK03918 198 KEKELEEVLREINEI-------SSELPELREELEKLEKEVKELEELKEEIE----ELEKELESLEGSK------------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1379 arRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELtSQCLEEKTMAMDKMEKTKNRLQQELDDLmvdld 1458
Cdd:PRK03918 255 --RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL-SEFYEEYLDELREIEKRLSRLEEEINGI----- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1459 hQRQIvSNLEKKQKKFDQLLAEEKTISAQYAEerdraeaeaREKDTKALSMARALEEALeakeelerfnKQLRAEMEDLm 1538
Cdd:PRK03918 327 -EERI-KELEEKEERLEELKKKLKELEKRLEE---------LEERHELYEEAKAKKEEL----------ERLKKRLTGL- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1539 sSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFDRDLQARDEQGEEKKRLLvkq 1618
Cdd:PRK03918 385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL--- 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1619 vREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGR--DEAVKQLRKLQAQMKDYQRE-LEEARASRDEIFTQ 1695
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEK 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1696 SKENEKKLKGLEAEILQLQE---DHAASERARRHAEQERDELADEISNSasGKSSLLEEKRRLEariaqleeeleeeqgN 1772
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEEL--GFESVEELEERLK---------------E 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1773 MELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLE 1852
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1853 QEAKERAAANKIVRRTEKKLKEVMMQVEdERRHADQYKEQMEKANSRMKQLKRQLEEAeeeatRANATRRKLQRELDDAT 1932
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKVKKY-----KALLKERALSKVGEIAS 750
|
....*....
gi 1604804596 1933 EASEGLTRE 1941
Cdd:PRK03918 751 EIFEELTEG 759
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1067-1757 |
2.53e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1067 EEKTRQELEKAKRKLDA-ETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLqknnALKQVRELQAHLAELQ 1145
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE----VLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1146 EDLESEKMCRSKAEKLKRDLSEELEALK---TELEDTLDTTAAQQELRSKREQEVAELKKAIDEEtknhEAQIQEMRQRQ 1222
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRerlEELEEERDDLLAEAGLDDADAEAVEARREELEDR----DEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1223 ATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAER 1302
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1303 SHKLQTELDnactmlevaekkglklakevdklnsklqdseELRQEETrqklnlstqirQLEVDRNTlleqqeeeeeARRN 1382
Cdd:PRK02224 414 LEELREERD-------------------------------ELREREA-----------ELEATLRT----------ARER 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1383 LEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLqkdveltsqclEEKTMAMDKMEKTKNRLQQELDDLmVDLDHQRQ 1462
Cdd:PRK02224 442 VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERV-----------EELEAELEDLEEEVEEVEERLERA-EDLVEAED 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1463 IVSNLEKKQKKFDQLLAEEKTISAqyaEERDRAEaearekdtkalsmaraleealeakeelerfnkQLRAEMEDLMSSKD 1542
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIE---EKRERAE--------------------------------ELRERAAELEAEAE 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1543 dvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaQFDRDLQARDEQGEEKKRLLVKqvREM 1622
Cdd:PRK02224 555 -------EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE--------RIRTLLAAIADAEDEIERLREK--REA 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1623 EAELEDERKQRTLAVASKKKlemdlnELEGQIEAANkgrdeavkqlrklqaqmkdyqreLEEARASRDEIFTQSKENEKK 1702
Cdd:PRK02224 618 LAELNDERRERLAEKRERKR------ELEAEFDEAR-----------------------IEEAREDKERAEEYLEQVEEK 668
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1703 LKGLEAEILQLQEDHAASERARRHAEQERDELaDEISNSASGKSSLLEEKRRLEA 1757
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEELEELRERR-EALENRVEALEALYDEAEELES 722
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
873-1588 |
3.11e-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: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 873 EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETElfAEAEEMRVRLLSRK---QELEEILHDLE 949
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 950 SRVEEEEERNQSLQNEK-KKMQSHIQDLEEQLDEEEAARQ------KLQLDKVTAEAKiKKMEediLLLEDQNSKflkek 1022
Cdd:pfam15921 198 EASGKKIYEHDSMSTMHfRSLGSAISKILRELDTEISYLKgrifpvEDQLEALKSESQ-NKIE---LLLQQHQDR----- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1023 klLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEErlkkeeKTRQELEKAKRKLdaetTDLQDQIVELQAQIEEL 1102
Cdd:pfam15921 269 --IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE------QARNQNSMYMRQL----SDLESTVSQLRSELREA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1103 KFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDT 1182
Cdd:pfam15921 337 KRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1183 TAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSE---QLEQAK----RFKSNLEKNKQSLENDNK 1255
Cdd:pfam15921 417 LRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKemlrKVVEELTAKKMTLESSER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1256 ELSCDVKTLQQAK-------TESEHKRKKLEAQLQEFM----------ARATEAERTKGELAERSHKLQTELDNACTMLE 1318
Cdd:pfam15921 497 TVSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQhlknegdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1319 VAEKKG----------LKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQlq 1388
Cdd:pfam15921 577 LVGQHGrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQE-- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1389 mvQSQMFETKKKLEEDLGSM-EGLEEVKRKLQKDVEltsqcleektmamdKMEKTKNRLQQELDDLMVDLDHQRQIVSNL 1467
Cdd:pfam15921 655 --RDQLLNEVKTSRNELNSLsEDYEVLKRNFRNKSE--------------EMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1468 EKKQKKFDQL-LAEEKTISAQyaeerdRAEAEAREKDTKALSMARALEEALEAKEELERfnKQLRAEMEDLMSSKDDVGK 1546
Cdd:pfam15921 719 EGSDGHAMKVaMGMQKQITAK------RGQIDALQSKIQFLEEAMTNANKEKHFLKEEK--NKLSQELSTVATEKNKMAG 790
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1604804596 1547 NVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1588
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1034-1782 |
3.46e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1034 SQLTEEEEKAKNLGKVKNKQEMMMVDlEERLKKEEKTRQEleKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEEL 1113
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAE-EARKAEEAKKKAE--DARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1114 -QAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRsKAEKLKRdlseELEALKTELEDTLDTTAAQQELRSK 1192
Cdd:PTZ00121 1164 rKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR-KAEEERK----AEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1193 REqevaELKKAidEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESE 1272
Cdd:PTZ00121 1239 AE----EAKKA--EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1273 HKRKkleaqlqefmarATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKlQDSEELRQEETRQK 1352
Cdd:PTZ00121 1313 EAKK------------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1353 LNlSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEdlgsMEGLEEVKRKLQ---KDVELTSQCL 1429
Cdd:PTZ00121 1380 AD-AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE----KKKADEAKKKAEeakKADEAKKKAE 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1430 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL----AEEKTISAQYAEERDRAE----AEARE 1501
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaaeAKKKADEAKKAEEAKKADeakkAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1502 KDTKALSMARALEEALEAKEELERFNKQLRaEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE----DELQ 1577
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAK 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1578 ATEDAKLRLEvnmQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRtlavasKKKLEMDLNELEgqiEAA 1657
Cdd:PTZ00121 1614 KAEEAKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE------AKKAEEDKKKAE---EAK 1681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1658 NKGRDEavkqlRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADE 1737
Cdd:PTZ00121 1682 KAEEDE-----KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1604804596 1738 ISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRK 1782
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1157-1756 |
3.80e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1157 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNheaqiqemrqrqataLEELSEQLEQA 1236
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE---------------LPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1237 KRFKSNLEKNKQSLENDNKELscdvKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAErshklqteldnactm 1316
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1317 LEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEvdrntlleqqeeeeearrNLEKQLQMVQSQMFE 1396
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE------------------EKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1397 TKKKLEEDLGSMEGLEEVKRKLQK----DVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1472
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1473 KFD----------QLLAEE--KTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKqLRAEMEDLMSS 1540
Cdd:PRK03918 430 ELKkakgkcpvcgRELTEEhrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1541 KDDVGK-NVHELEKSK---RTLEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqfdrdlqaRDEQGEEKKRLLV 1616
Cdd:PRK03918 509 EEKLKKyNLEELEKKAeeyEKLKEKLIKLKGEIKSLKKELE--------------------------KLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1617 KQVREMEAELED-ERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDeAVKQLRKLQAQMKDYQRELEEARASRDEIFTQ 1695
Cdd:PRK03918 563 KKLDELEEELAElLKELEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1696 SKENEKKL------------KGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLE 1756
Cdd:PRK03918 642 LEELRKELeelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
994-1716 |
4.43e-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: 75.01 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 994 KVTAEAKIKKMEEDILLLED----QNSKFLKEKKLLEDRISEMTS---QLTEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1066
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLctpcMPDTYHERKQVLEKELKHLREalqQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1067 EEKTRQE---LEKAKRKLDAETTDLQdqIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAE 1143
Cdd:TIGR00618 269 IEELRAQeavLEETQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1144 LQEDLESEKMCRSKAEKLKRDLSEELEAlkTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQE---MRQ 1220
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdLQG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1221 RQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscdvKTLQQAKTEsehkRKKLEAQLQEFMARATEAERTKGELA 1300
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL----QESAQSLKE----REQQLQTKEQIHLQETRKKAVVLARL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1301 ERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEEtrqklnlstqirqlevdrntlleqqeeeeear 1380
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSE-------------------------------- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1381 RNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQ 1460
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1461 rQIVSNLEKKQKKFDQLLAEEKTISAQYAEE---RDRAEAEAREKDTKALSMARALEEALEAKEELERFN------KQLR 1531
Cdd:TIGR00618 625 -QDLQDVRLHLQQCSQELALKLTALHALQLTltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywkemlAQCQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1532 AEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEK 1611
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1612 KRLLVKQVREMEaelEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLR---KLQAQMKDYQRELEEARAS 1688
Cdd:TIGR00618 784 AAEIQFFNRLRE---EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEeksATLGEITHQLLKYEECSKQ 860
|
730 740 750
....*....|....*....|....*....|.
gi 1604804596 1689 RDEIFTQSK---ENEKKLKGLEAEILQLQED 1716
Cdd:TIGR00618 861 LAQLTQEQAkiiQLSDKLNGINQIKIQFDGD 891
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1059-1233 |
4.62e-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: 70.72 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1059 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQvRELQ 1138
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1139 AhlaeLQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDEETKNHEAQIQEM 1218
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 1604804596 1219 RQRQATALEELSEQL 1233
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1020-1587 |
4.81e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.69 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKakrkLDAETTDLQDQIVE----- 1094
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1095 --LQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLE----SEKMCRSKAEKLK---RDL 1165
Cdd:PRK02224 275 eeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLRedaDDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1166 SEELEALKTELEDTLDTTAAQQELRSKREQEVAELkkaideetknhEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEK 1245
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEEL-----------EEEIEELRER----FGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1246 NKQSLENDNKELSCDVKTLQQAKTESEHKRKK-------LEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLE 1318
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1319 VAEKKgLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETK 1398
Cdd:PRK02224 500 RAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1399 KKLEEDLGSMEGLEEVkRKLQKDVELTSQCLEEKTmamdkmEKTKNrlQQELDDLMVD-LDHQRQIVSNLEKKqkkFD-- 1475
Cdd:PRK02224 579 SKLAELKERIESLERI-RTLLAAIADAEDEIERLR------EKREA--LAELNDERRErLAEKRERKRELEAE---FDea 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1476 --QLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLmsskDDVGKNVHELEK 1553
Cdd:PRK02224 647 riEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAL----EALYDEAEELES 722
|
570 580 590
....*....|....*....|....*....|....*....
gi 1604804596 1554 SKRTL-----EQQVEEMRTQLEELEDeLQATEDAKLRLE 1587
Cdd:PRK02224 723 MYGDLraelrQRNVETLERMLNETFD-LVYQNDAYSHIE 760
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
828-1480 |
6.33e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 6.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 828 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEELQAKDEELvKVKERQLKVENELVEMERKhqqli 907
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERINRARK----- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 908 eeKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAAR 987
Cdd:TIGR00618 292 --AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 988 QKLQldKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKE 1067
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1068 EKTRQ-------ELEKAKRKLDAETTDLQDQIV-----------------ELQAQIEELKFQLTKKEEELQAA------- 1116
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKEQihlqetrkkavvlarllELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1117 --LARSDEETLQKNNALKQVR----ELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1190
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1191 SK-----REQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKelscdvktlQ 1265
Cdd:TIGR00618 608 DMlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS---------R 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1266 QAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLevaekkGLKLAKEVDKLNSKLQDSEELR 1345
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL------GSDLAAREDALNQSLKELMHQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1346 QEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVK-RKLQKDVEL 1424
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQcETLVQEEEQ 832
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 1425 TSQCLEEKTmamdkmektknRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE 1480
Cdd:TIGR00618 833 FLSRLEEKS-----------ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
861-1347 |
9.41e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 861 KVKPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQE 940
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 941 LEEILHDLESRVeeeeERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKL----QLDKVTAEAKIKKMEEDILLLEDQNS 1016
Cdd:PRK03918 326 IEERIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEKLEKELEELEKAKE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1017 KFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEektrqelekAKRKLDAETTDLQDQIVELQ 1096
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE---------LLEEYTAELKRIEKELKEIE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1097 AQIEELKFQLTKKEEELqaalarSDEETLQKNNAL-KQVRELQAHLAELQ-EDLEsekmcrsKAEKLKRDLSEELEALKT 1174
Cdd:PRK03918 473 EKERKLRKELRELEKVL------KKESELIKLKELaEQLKELEEKLKKYNlEELE-------KKAEEYEKLKEKLIKLKG 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1175 ELEDTLDTTAAQQELRSKREqevaELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRF----------KSNLE 1244
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdaEKELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1245 KNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFmarateAERTKGELAERSHKLQTELDNACTMLEVAEKKG 1324
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY------SEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
490 500
....*....|....*....|...
gi 1604804596 1325 LKLAKEVDKLNSKLQDSEELRQE 1347
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKE 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1193-1906 |
1.29e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1193 REQEVAELKKAIDEETK-NHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSC--DVKTLQQAKT 1269
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKaeEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1270 ESEHKRKKLEAQLQEFMARATEAERTKgelAERSHKLQTELDNAcTMLEVAEKkglklAKEVDKLNSKLQDSEELRQEET 1349
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAE---DAKRVEIARKAEDA-RKAEEARK-----AEDAKKAEAARKAEEVRKAEEL 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1350 RQklnlSTQIRQLEVDRntlleqqeeEEEARRNLEKQLQMVQSQMFETKKKLEEdlgSMEGLEEVKRKLQKDVELTSQCL 1429
Cdd:PTZ00121 1194 RK----AEDARKAEAAR---------KAEEERKAEEARKAEDAKKAEAVKKAEE---AKKDAEEAKKAEEERNNEEIRKF 1257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1430 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqllAEEKTISAQYAEERDRAEAEAREKDTKALSM 1509
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1510 ARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRtQLEELEDelQATEDAKLRLEVN 1589
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKK--KAEEDKKKADELK 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1590 MQAMKAQFDRDLQARDEQgeekkrllVKQVREMEAELEDERKqrtlAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLR 1669
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEE--------KKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1670 KLQAQMKDYQRELEEARASRDEIftQSKENEKKlkglEAEILQLQEDHAASERARRHAEQERdelADEIsNSASGKSSLL 1749
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEA--KKAAEAKK----KADEAKKAEEAKKADEAKKAEEAKK---ADEA-KKAEEKKKAD 1549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1750 EEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNI--QVDNLNTELAG---ERSAAQKSENARQQMERQNKDLKAKLAE 1824
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMklyEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1825 LEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANsRMKQLK 1904
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELK 1708
|
..
gi 1604804596 1905 RQ 1906
Cdd:PTZ00121 1709 KK 1710
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
999-1826 |
1.84e-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: 73.16 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 999 AKIKKMEEDILLLEDQNSKFLKEKKLLEdRISEMTSQLTEEE--EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEK 1076
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELE-LKMEKVFQGTDEQlnDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1077 AKRKLDAETTDLQDQIVELQAQIeeLKFQLTKKEEELQAAL---ARSDEETLQKNNALKQVRELQAHLAELQEDLESEkm 1153
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHI--RARDSLIQSLATRLELdgfERGPFSERQIKNFHTLVIERQEDEAKTAAQLCAD-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1154 cRSKAEKLKRDLSEELEALKTELEDTLDT-----TAAQQELRSKReQEVAELKKAIDEETKNHEAQIQEMRQ----RQAT 1224
Cdd:TIGR00606 417 -LQSKERLKQEQADEIRDEKKGLGRTIELkkeilEKKQEELKFVI-KELQQLEGSSDRILELDQELRKAERElskaEKNS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1225 ALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEaQLQEFMARATEA------------ 1292
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDEltsllgyfpnkk 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1293 ---------ERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKlNLSTQIRQLE 1363
Cdd:TIGR00606 574 qledwlhskSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLE-RLKEEIEKSS 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1364 VDRNTLLEQQEEEEEARRNLEKQLQM---VQSQMFETKKKLEE---DLGSM--------EGLEEVKRKLQKDVELTSQCL 1429
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEfisDLQSKlrlapdklKSTESELKKKEKRRDEMLGLA 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1430 EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRqivSNLEKKQKKFDQLLAEEKTISAQyaeERDRAEAEAREKDTKALSM 1509
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLLGTIMPEEESAKVC---LTDVTIMERFQMELKDVER 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1510 ARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDElqatedaKLRLEVN 1589
Cdd:TIGR00606 807 KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-------KLQIGTN 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1590 MQamkaqfdrdlqaRDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLR 1669
Cdd:TIGR00606 880 LQ------------RRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1670 KLQAQMKDYQRELEEARASRDEIFTQSKENEkklkgLEAEILQLQEdhaaSERARRHAEQERDELADEISNSASGKSSLL 1749
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKETE-----LNTVNAQLEE----CEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1750 EEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELE 1826
Cdd:TIGR00606 1019 DNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
870-1503 |
2.55e-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: 72.45 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 870 RQEEELQAKDEELVKVKER---QLKVENELVEME-----RKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQEL 941
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKaiqELQFENEKVSLKleeeiQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREET 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 942 EEILHDLESRVEEEEERNQSL--QNEKKKMQSHIQDLEEQLDEEEAARQ----------KLQLDKVTAEAKIKKMEEDIL 1009
Cdd:pfam05483 182 RQVYMDLNNNIEKMILAFEELrvQAENARLEMHFKLKEDHEKIQHLEEEykkeindkekQVSLLLIQITEKENKMKDLTF 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1010 LLEDQNSKF--LKEKKLLED----RISEMTSQLTEEEEKAK-NLGKVKNKQEMMMVDLEERLKK-----EEKTRQ--ELE 1075
Cdd:pfam05483 262 LLEESRDKAnqLEEKTKLQDenlkELIEKKDHLTKELEDIKmSLQRSMSTQKALEEDLQIATKTicqltEEKEAQmeELN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1076 KAK-------RKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDL 1148
Cdd:pfam05483 342 KAKaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1149 ESEKMCRSKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEE 1228
Cdd:pfam05483 422 DEKKQFEKIAEELK-GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1229 LSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQT 1308
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1309 ELDNACTMLEVAEKKGLKLAKEVDKLNSKLqdsEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQ 1388
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNI---EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIID 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1389 MVQSQMfETKKKLEEDLgsmegLEEVKR---------KLQKDVELTSQCLEEKTMAMdkMEKTKNrlqqELDDLMVDLDH 1459
Cdd:pfam05483 658 NYQKEI-EDKKISEEKL-----LEEVEKakaiadeavKLQKEIDKRCQHKIAEMVAL--MEKHKH----QYDKIIEERDS 725
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1604804596 1460 QRQIVSNLEKKQKKFDQLLAEE-KTISAQYAEERDRAEAEAREKD 1503
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKE 770
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
827-1150 |
3.35e-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: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 827 FAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTkvkpllQVTRQEEELQAKDEELVKVKERQLKVENELVEmerkhqqL 906
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLSKELTE-------L 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 907 IEEKNILAEQLHAETELFAEAEEmrvrllsRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAA 986
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 987 RQKLQLDKVTAEAKIKKMEEDILLLEDQnskflkekklledrISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1066
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1067 EEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQK-NNALKQVRELQAHLAELQ 1145
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLE 978
|
....*
gi 1604804596 1146 EDLES 1150
Cdd:TIGR02168 979 NKIKE 983
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1061-1761 |
3.98e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.91 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1061 EERLKKEEKT---RQELEKAKRKLDAEttdlQDQIVELQAQIEELKFQLTKKEEELQAAlarsdEETLQK-NNALKQ--- 1133
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAA-----SDHLNLvQTALRQqek 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1134 VRELQAHLAELQEDLESEKMCRskaeklkrdlsEELEALKTELEDTLdtTAAQQELRSKREQeVAELKKAIDEEtknhea 1213
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVV-----------EEAAEQLAEAEARL--EAAEEEVDSLKSQ-LADYQQALDVQ------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1214 QIQEMRQRQA-TALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEA 1292
Cdd:COG3096 409 QTRAIQYQQAvQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1293 ERtkGELAERSHKLQTELDNACTMLEVAEKKGLKLAkEVDKLNSKLQDSEELRQEETRQ-------KLNLSTQIRQLEVD 1365
Cdd:COG3096 489 ER--SQAWQTARELLRRYRSQQALAQRLQQLRAQLA-ELEQRLRQQQNAERLLEEFCQRigqqldaAEELEELLAELEAQ 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1366 RNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKK-------------LEEDLG-SMEGLEEVKRKLQKDVELtsqcLEE 1431
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdalerLREQSGeALADSQEVTAAMQQLLER----ERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1432 KTMAMDKMEKTKNRLQQELDDLM----------------------------VDLD------------HQRQIVSNLEKKQ 1471
Cdd:COG3096 642 ATVERDELAARKQALESQIERLSqpggaedprllalaerlggvllseiyddVTLEdapyfsalygpaRHAIVVPDLSAVK 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1472 KKFDQL---------------LAEEKTISAQYAEERDRAEAE------------------AREKDTKALSMARALEEALE 1518
Cdd:COG3096 722 EQLAGLedcpedlyliegdpdSFDDSVFDAEELEDAVVVKLSdrqwrysrfpevplfgraAREKRLEELRAERDELAEQY 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1519 AKEELER---------------------FNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQL-------- 1569
Cdd:COG3096 802 AKASFDVqklqrlhqafsqfvgghlavaFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLqllnkllp 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1570 --------------EELEDELQATEDAKL----------RLEVNMQAMK---AQFDRdLQARDEQGEEKKRLLVKQVREM 1622
Cdd:COG3096 882 qanlladetladrlEELREELDAAQEAQAfiqqhgkalaQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFAL 960
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1623 EaeledERKQRTLAVASKKKLEM-----DLNE-LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQS 1696
Cdd:COG3096 961 S-----EVVQRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTL 1035
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1697 KENEKKLKGLEaeilqLQEDHAASERARrhaeQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1761
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 ... |
1226-1904 |
5.73e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.20 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1226 LEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHK 1305
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1306 LQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEK 1385
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1386 QLQMVQSQMfETKKKLEEDLgsmEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQivs 1465
Cdd:TIGR04523 202 LLSNLKKKI-QKNKSLESQI---SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1466 NLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEArEKDTKalSMARALEEALEAKEELERFNKQLRAEMEDLMSskdDVG 1545
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-NKELK--SELKNQEKKLEEIQNQISQNNKIISQLNEQIS---QLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1546 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQGEEKKRLLVKQVREMEAE 1625
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDEQIKKLQQEKELLEKE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1626 LEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEavkqlrkLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKG 1705
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-------LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1706 LEAEILQLqedhaaserarrhaEQERDELADEISnsasgksSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNI 1785
Cdd:TIGR04523 501 LNEEKKEL--------------EEKVKDLTKKIS-------SLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1786 --QVDNLNTELagersaaQKSENARQQMERQNKDLKAKLAELEgTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANK 1863
Cdd:TIGR04523 560 ekEIDEKNKEI-------EELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1604804596 1864 IVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLK 1904
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1020-1242 |
9.94e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1099
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDT 1179
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1180 LdttAAQQELRSKREQEVAELKKAIDEEtknhEAQIQEMrQRQATALEELSEQLEQAKRFKSN 1242
Cdd:COG4942 187 R---AALEALKAERQKLLARLEKELAEL----AAELAEL-QQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1146-1906 |
1.06e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1146 EDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATA 1225
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1226 LEELSEQLEQAKRfksnLEKNKQSLENDNKELSCDVKTLQQAKTE--SEHKRKKLEAQLQEFMARATEAeRTKGELAERS 1303
Cdd:PTZ00121 1171 KAEDAKKAEAARK----AEEVRKAEELRKAEDARKAEAARKAEEErkAEEARKAEDAKKAEAVKKAEEA-KKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1304 HKLQTELD----NACTMLEVAEKKGLKLAKEVDKLNsKLQDSEELRQEETRQKLNlstqirqlEVDRNTLLEQQEEEEEA 1379
Cdd:PTZ00121 1246 EEERNNEEirkfEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKADEAKKAE--------EKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1380 RRNLEKQLQMVQSQMFETKKKLEEdlgsMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDH 1459
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEE----AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1460 QRQIVSNLEKKQKKFDQL--LAEEKTISAQY---AEERDRAEaEAREKDTKALSMARALEEALEAKEELERFNKQLRAEM 1534
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELkkAAAAKKKADEAkkkAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1535 EDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE--DELQATEDAKlrlevnmqamKAQFDRDLQARDEQGEEKK 1612
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAK----------KADEAKKAEEAKKADEAKK 1541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1613 RLLVKQVREMeaeledeRKQRTLAVASKKKlemdlnelegQIEAANKGRDEAVKQLRKLQaqmkdyqrELEEARASRDEI 1692
Cdd:PTZ00121 1542 AEEKKKADEL-------KKAEELKKAEEKK----------KAEEAKKAEEDKNMALRKAE--------EAKKAEEARIEE 1596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1693 FTQSKENEKKLKGLEAEilqlqedhaASERARRHAEQERDElADEISNSASGKSSLLEEKRRLEariaqleeeleeeqgn 1772
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAK---------KAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAE---------------- 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1773 mellndRFRKsniqvdnlntelAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLE 1852
Cdd:PTZ00121 1651 ------ELKK------------AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1853 QEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANsRMKQLKRQ 1906
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKE 1765
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
1.88e-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: 1.88e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1604804596 31 TAKRLVWIPSERNGFEAASVREERGDEVVVELaENGKKAVVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1059-1659 |
2.13e-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: 69.00 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1059 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQaalarsdeETLQKNNALKQVRELQ 1138
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR--------EQAELNRLKKKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1139 AHLAELQEDLESEkmcrskAEKLKRDLSEELEALKTELEDtldttaAQQELRSKReQEVAELKKAIDEEtknhEAQIQEM 1218
Cdd:pfam05557 89 NKKLNEKESQLAD------AREVISCLKNELSELRRQIQR------AELELQSTN-SELEELQERLDLL----KAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1219 RQRQATALEELSEQLEQAKRFKsNLEKNKQSLENDNKElscdVKTLqQAKTESEHKRKKLEAQLQEFMARATEAERTKGE 1298
Cdd:pfam05557 152 EQLRQNLEKQQSSLAEAEQRIK-ELEFEIQSQEQDSEI----VKNS-KSELARIPELEKELERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1299 LAERSHKLQTELDNactmLEVAEKKGLKLAKEVDKLNSKLQDSEELRQE---ETRQKLNLSTQIRQLEVDRNTLLEQQEE 1375
Cdd:pfam05557 226 LKEEVEDLKRKLER----EEKYREEAATLELEKEKLEQELQSWVKLAQDtglNLRSPEDLSRRIEQLQQREIVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1376 EEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQcleektmamdkmektknrlqqelddlmv 1455
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTK---------------------------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1456 DLDHQRQIVSNLEKK--QKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQlRAE 1533
Cdd:pfam05557 354 ERDGYRAILESYDKEltMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQ-QES 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1534 MEDLMSSKDDvgknVHELEKSKRTLEQQVEEMRTQLEELEDELqatEDAKLRLEVNMQAMK---------AQFDRDLQAR 1604
Cdd:pfam05557 433 LADPSYSKEE----VDSLRRKLETLELERQRLREQKNELEMEL---ERRCLQGDYDPKKTKvlhlsmnpaAEAYQQRKNQ 505
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1605 DEQGEEKKRLLVKQVREMEAELEDerkQRTLAVASKKKLEMDLNELEGQIEAANK 1659
Cdd:pfam05557 506 LEKLQAEIERLKRLLKKLEDDLEQ---VLRLPETTSTMNFKEVLDLRKELESAEL 557
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1199-1950 |
3.77e-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: 68.56 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1199 ELKKAIDEEtknheAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLEndnkelscdvkTLQQAKTESEhKRKKL 1278
Cdd:TIGR02169 154 ERRKIIDEI-----AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-----------RLRREREKAE-RYQAL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1279 EAQLQEFmaRATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQD-SEELRQEETRQKLNLST 1357
Cdd:TIGR02169 217 LKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1358 QIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVeltsqcleektmamD 1437
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY--------------A 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1438 KMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTisaqyaeERDRAEAEAREKDTKALsmaraleeal 1517
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR-------ELDRLQEELQRLSEELA---------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1518 eakeelerfnkQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF 1597
Cdd:TIGR02169 424 -----------DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1598 DRdLQARDEQGEEKKRLLVKQVREMEAELE------------DERKQRTLAVASKKKLEMDLNELEGQIEAA-------- 1657
Cdd:TIGR02169 493 AE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDDAVAKEAiellkrrk 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1658 ---------NKGRDEAVKQLRKLQAQMKDYQRELEE---------ARASRDEIFTQSKENEKKLKG------LEAEILQ- 1712
Cdd:TIGR02169 572 agratflplNKMRDERRDLSILSEDGVIGFAVDLVEfdpkyepafKYVFGDTLVVEDIEAARRLMGkyrmvtLEGELFEk 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1713 ---LQEDHAASERARRHAEQERDE---LADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQ 1786
Cdd:TIGR02169 652 sgaMTGGSRAPRGGILFSRSEPAElqrLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1787 VDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgTVKSKFKASIAALEAKIL-----QLEDQLEQEAKERAAA 1861
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRI 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1862 NKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTRE 1941
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
....*....
gi 1604804596 1942 VSSLKNRLR 1950
Cdd:TIGR02169 891 RDELEAQLR 899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
863-1278 |
3.93e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 863 KPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERK-------HQQLIEEKNILAEQLHAETEL----FAEAEEMR 931
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleeleerHELYEEAKAKKEELERLKKRLtgltPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 932 VRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEakIKKMEEDILLL 1011
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAE--LKRIEKELKEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1012 EDQNSKFLKEKKLLEDRISEmTSQLTEEEEKAKNLGKVKNKQEmmMVDLEErLKKEEKTRQELEKAKRKLDAETTDLQDQ 1091
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLK--KYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1092 IVELQA---QIEELKFQLTKKEEELQAALARSDEEtlqknnALKQVRELQAHLAELqEDLESEKMCRSKAEKLKRDLSEE 1168
Cdd:PRK03918 548 LEKLEElkkKLAELEKKLDELEEELAELLKELEEL------GFESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1169 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEET-KNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNK 1247
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
410 420 430
....*....|....*....|....*....|.
gi 1604804596 1248 QSLENdNKELSCDVKTLQQAKTESEHKRKKL 1278
Cdd:PRK03918 701 EELEE-REKAKKELEKLEKALERVEELREKV 730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
873-1257 |
1.26e-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: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 873 EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEK-----NILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHD 947
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 948 LESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1027
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1028 RISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLT 1107
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1108 KKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEK--MCRSKAEKLKRDLSEELEALKTELEDTLDTTAA 1185
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1186 QQELRSKREQEVAELKKAIDEETKnheaQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKEL 1257
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEK----KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1068-1734 |
1.74e-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: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1068 EKTRQELEKAKRKLDA--ETTDLQDQIVELQAQIEELK-----FQLTKKEEELQAALARSDEETLQKNNALKQVRELQAH 1140
Cdd:COG4913 238 ERAHEALEDAREQIELlePIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1141 LAELQEDLESekmcrskAEKLKRDLS-EELEALKTELEDTldttAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMR 1219
Cdd:COG4913 318 LDALREELDE-------LEAQIRGNGgDRLEQLEREIERL----ERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1220 QRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKT----ESEHKRKKLEAQLQ----------EF 1285
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGldeaelpfvgEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1286 MARATEAERTKG--ELAERSHKLqteldnacTMLeVAEKKGLKLAKEVDKLNSKL----QDSEELRQEETRQKLNLSTQI 1359
Cdd:COG4913 467 IEVRPEEERWRGaiERVLGGFAL--------TLL-VPPEHYAAALRWVNRLHLRGrlvyERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1360 RQLEVDRNTLLEQQEEEEEARRNL-----EKQLQMVQ------------SQMFE--TKKKLEED--LGSmegleEVKRKL 1418
Cdd:COG4913 538 GKLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPraitragqvkgnGTRHEkdDRRRIRSRyvLGF-----DNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1419 QkdveltsqcleektmamdkmektknRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAE 1498
Cdd:COG4913 613 A-------------------------ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1499 ARekdtkaLSmaraleealeakeelerfnkQLRAEMEDLMSSKDDVgknvhelekskRTLEQQVEEMRTQLEELEDELQA 1578
Cdd:COG4913 668 RE------IA--------------------ELEAELERLDASSDDL-----------AALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1579 TEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAvaskkklemdlNELEGQIEAAN 1658
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR-----------ENLEERIDALR 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1659 KGRDEAVKQLRKLqaqMKDYQRELEEARASRD----------EIFTQSKENEkkLKGLEAEILQLQED---------HAA 1719
Cdd:COG4913 780 ARLNRAEEELERA---MRAFNREWPAETADLDadleslpeylALLDRLEEDG--LPEYEERFKELLNEnsiefvadlLSK 854
|
730
....*....|....*
gi 1604804596 1720 SERARRHAEQERDEL 1734
Cdd:COG4913 855 LRRAIREIKERIDPL 869
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
915-1299 |
2.04e-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: 65.92 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 915 EQLHAETELFAEAEEMR-------VRLLSRKQELEEILHDLESRVEEEEERNQSLQNEK--KKMQSHIQDLEEQLDEEEA 985
Cdd:pfam17380 234 EKMERRKESFNLAEDVTtmtpeytVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 986 ARQKLQLDKVTAEAKIKKmeEDILLLEDQNSKFLKEKKL----LEDRISEMtsQLTEEEEKAKNLGKVKNKQEMMMvdle 1061
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKREL--ERIRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1062 ERLKKEEKTRQELEKAkRKLDAETTDLQDQIVELQAQIEELKFQltkKEEELQAALARSDEEtlqKNNALKQVRElqahl 1141
Cdd:pfam17380 386 ERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRAE---QEEARQREVRRLEEE---RAREMERVRL----- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1142 AELQEDLESEKMCRSKAEKLKRDLSEELEALKTELedtldttaAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQR 1221
Cdd:pfam17380 454 EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR--------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1222 Q-ATALEELSEQLEQAKRFKSNLEKNKQslendnkelscdvktLQQAKTESEHKRKKLEA--QLQEFMARATEAERTKGE 1298
Cdd:pfam17380 526 QkAIYEEERRREAEEERRKQQEMEERRR---------------IQEQMRKATEERSRLEAmeREREMMRQIVESEKARAE 590
|
.
gi 1604804596 1299 L 1299
Cdd:pfam17380 591 Y 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1059-1294 |
2.93e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1059 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAAlarsdEETLQKNNalKQVRELQ 1138
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-----EAELAELE--KEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1139 AHLAELQEDLesEKMCRSkAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEetknheaqIQEM 1218
Cdd:COG4942 97 AELEAQKEEL--AELLRA-LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--------LAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 1219 RQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAER 1294
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1298-1949 |
2.94e-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: 65.43 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1298 ELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEE 1377
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1378 EARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDL 1457
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1458 DHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLraemedl 1537
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1538 msskDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAqfdRDLQARDEQGEekkrllvK 1617
Cdd:TIGR04523 270 ----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNN-------K 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1618 QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARasrdeifTQSK 1697
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE-------KLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1698 ENEKKLKGLEAEILQLqedhaaserarrhaEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLN 1777
Cdd:TIGR04523 409 QKDEQIKKLQQEKELL--------------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1778 DRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKsKFKASIAALEAKILQLEDQLEqeake 1857
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELN----- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1858 raaaNKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEG 1937
Cdd:TIGR04523 549 ----KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
650
....*....|..
gi 1604804596 1938 LTREVSSLKNRL 1949
Cdd:TIGR04523 625 ENEKLSSIIKNI 636
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
988-1737 |
3.70e-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: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 988 QKLQLDKVTAEAKIK----KMEEDILLLEDQNsKFLKEKKLLEDRISemtSQLTEEEEKAKNLGKVKNKQEMMMVDLEER 1063
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKVS---LKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1064 LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALaRSDEETLQknnalkqvrelqaHLAE 1143
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKL-KEDHEKIQ-------------HLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1144 lqedlESEKMCRSKAEKLKRDLSEelealKTELEDTL-DTTAAQQELRSKREQevaelkkaIDEETKNHEAQIQEMRQRQ 1222
Cdd:pfam05483 230 -----EYKKEINDKEKQVSLLLIQ-----ITEKENKMkDLTFLLEESRDKANQ--------LEEKTKLQDENLKELIEKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1223 atalEELSEQLEQAKRFKSNLEKNKQSLENDnkeLSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAER 1302
Cdd:pfam05483 292 ----DHLTKELEDIKMSLQRSMSTQKALEED---LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1303 SHKLQTELDNACTMLEVAEKKGLKLAKEVDKLnSKLQDSEELRQEETR----QKLNLSTQIRQLEVDRNTLLEQQEEEEE 1378
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVELEELKkilaEDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1379 ARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLE-EVKRKLQKDVELTSQCleektmamDKMEKTKNRLQQELDDLMVDL 1457
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLEL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1458 DHQRQIVSNLEKKQKKfdqLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDL 1537
Cdd:pfam05483 516 KKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1538 MSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVK 1617
Cdd:pfam05483 593 ENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1618 QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRdeiftqsk 1697
Cdd:pfam05483 673 LLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL-------- 744
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1604804596 1698 enEKKLKGLEAEIL----QLQEDHAASERARRHAEQERDELADE 1737
Cdd:pfam05483 745 --EIELSNIKAELLslkkQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1529-1951 |
4.11e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1529 QLRAEMEDLMSSKDDVGKnvheLEKSKRTLEQqVEEMRTQLEELEDELQATEDAKLRLEVnmqAMKAQFDRDLQARDEQG 1608
Cdd:COG4913 229 ALVEHFDDLERAHEALED----AREQIELLEP-IRELAERYAAARERLAELEYLRAALRL---WFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1609 EEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMD-LNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARA 1687
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1688 SRDEIFTQSKENEKKLKGLEAEilqLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELE 1767
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1768 EE-----------------QGNME-LLND----------------------------RFRKSNIQVDNLNTELAGERSAA 1801
Cdd:COG4913 458 AElpfvgelievrpeeerwRGAIErVLGGfaltllvppehyaaalrwvnrlhlrgrlVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1802 QK--------SENARQQMERQNKDLKAKLAE----------LEGTVKSKF---------------------KASIAALEA 1842
Cdd:COG4913 538 GKldfkphpfRAWLEAELGRRFDYVCVDSPEelrrhpraitRAGQVKGNGtrhekddrrrirsryvlgfdnRAKLAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1843 KILQLEDQLEQEAKERAAANKIVRRTEK------KLKEV------MMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEA 1910
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQErrealqRLAEYswdeidVASAEREIAELEAELERLDASSDDLAALEEQLEEL 697
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1604804596 1911 EEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
902-1283 |
4.54e-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: 64.76 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 902 KHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEIlhdlESRVEEEEERNQSLQNEKKKMqshiqdleeqld 981
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAIYAEQERM------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 982 eeeAARQKLQLDKVTAEAKIKKMEEdillledqnskflkekklledrisemtsqlTEEEEKAKNLGKVKNKQEMMMvdle 1061
Cdd:pfam17380 343 ---AMERERELERIRQEERKRELER------------------------------IRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1062 ERLKKEEKTRQELEkAKRKLDAETTDLQDQIVELQAQIEELKF--------QLTKKEEELQAALARSDEETLQKNNALKQ 1133
Cdd:pfam17380 386 ERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAeqeearqrEVRRLEEERAREMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1134 VRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEElealktELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEA 1213
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1214 QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLEndnkelscdvktLQQAKTESEHKRKKLEAQLQ 1283
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE------------MMRQIVESEKARAEYEATTP 596
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1007-1491 |
5.94e-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: 64.21 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1007 DILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETT 1086
Cdd:COG5185 135 DELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGN 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1087 DLQDQIVELQAQIEEL------KFQLTKKEEELQAALARSDEETLQKNNALKQVRelqahLAELQEDLESEKMCRSKAEK 1160
Cdd:COG5185 215 LGSESTLLEKAKEIINieealkGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEK-----LGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1161 LKRDLSEELEALKTELEDTLDTTAAQQELRSKR-EQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQaKRF 1239
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEaEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIEN-IVG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1240 KSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLqefmarateaERTKGELAERSHKLQTELDNACTMLEV 1319
Cdd:COG5185 369 EVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATL----------EDTLKAADRQIEELQRQIEQATSSNEE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1320 AEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQirqlevdrntlleqqeeeeEARRNLEKQLQMVQSQMFETKK 1399
Cdd:COG5185 439 VSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVR-------------------SKKEDLNEELTQIESRVSTLKA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1400 KLEEDLGSMEG-LEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLL 1478
Cdd:COG5185 500 TLEKLRAKLERqLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLST 579
|
490
....*....|...
gi 1604804596 1479 AEEKTISAQYAEE 1491
Cdd:COG5185 580 IESQQAREDPIPD 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1636-1862 |
1.00e-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: 62.86 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1636 AVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQE 1715
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1716 DHAASER--ARRHAEQERDELADEISNSASGKSSLLEEKRR--LEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLN 1791
Cdd:COG4942 98 ELEAQKEelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1792 TELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEAKERAAAN 1862
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1089-1313 |
1.36e-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: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1089 QDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEE 1168
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1169 LEALKTELEDTLDttAAQqelRSKREQEVAELKKAIDEETKNHEAQ-IQEMRQRQATALEELSEQLEQAKRFKSNLEKNK 1247
Cdd:COG4942 99 LEAQKEELAELLR--ALY---RLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 1248 QSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNA 1313
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1058-1399 |
2.39e-09 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 62.05 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1058 VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQ-AQIEELKFQltkkeeelQAALARSDEETLQKNNALKQVR- 1135
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlAKEEDLKRQ--------NAVLQEAQVELDALQNQLALARa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1136 --ELQAHLAELQEDLESEKMcrskaEKLKRDLSEELEALKTELEDTLDTTAAQQELRskREQEVAELkkaiDEETKNHEA 1213
Cdd:pfam03528 76 emENIKAVATVSENTKQEAI-----DEVKSQWQEEVASLQAIMKETVREYEVQFHRR--LEQERAQW----NQYRESAER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1214 QIQEMRQRQATALEElsEQLE-QAKRFKSNLEKNKQSLENDNKELScdvkTLQQAKTESEHKRKKLEAQLQEFMARATEA 1292
Cdd:pfam03528 145 EIADLRRRLSEGQEE--ENLEdEMKKAQEDAEKLRSVVMPMEKEIA----ALKAKLTEAEDKIKELEASKMKELNHYLEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1293 ERT---------------KGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEEL-RQEETRQKLNLS 1356
Cdd:pfam03528 219 EKScrtdlemyvavlntqKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLlMRDMQRMESVLT 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1604804596 1357 T-QIRQLEVdrntlLEQQEEEEEARRNLEKQLQMVQSQMFETKK 1399
Cdd:pfam03528 299 SeQLRQVEE-----IKKKDQEEHKRARTHKEKETLKSDREHTVS 337
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1484 |
3.85e-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: 62.01 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 867 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQL---IEEKNILAEQLHAE--------TELFAEAEEM----- 930
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLTEEyaelkeelEDLRAELEEVdkefa 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 931 --RVRLLSRKQELEEILHDLESrveeeEERNQS-LQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEED 1007
Cdd:TIGR02169 382 etRDELKDYREKLEKLKREINE-----LKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1008 ILLLEDQNSKFLKEK-------KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRK 1080
Cdd:TIGR02169 457 LEQLAADLSKYEQELydlkeeyDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1081 LD-----AETTDLQDQIVE----LQAQIEELK----------------------------------FQLTKKEEELQAAL 1117
Cdd:TIGR02169 537 YAtaievAAGNRLNNVVVEddavAKEAIELLKrrkagratflplnkmrderrdlsilsedgvigfaVDLVEFDPKYEPAF 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1118 ARSDEETLQKNNaLKQVREL--QAHLAELQEDL--ESEKM-----CRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1188
Cdd:TIGR02169 617 KYVFGDTLVVED-IEAARRLmgKYRMVTLEGELfeKSGAMtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1189 LRSKREQEVAELKKAIDEETKNHEA------QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVK 1262
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEiekeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1263 TLQQAKT------------ESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKE 1330
Cdd:TIGR02169 776 KLEEALNdlearlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1331 VDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEG 1410
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 1411 LEEVKRKLQKDVeltsqcleEKTMAMDKMEKTKNRLQQELDDL----MVDLDHQRQIVSNLEKKQKKFDQLLAEEKTI 1484
Cdd:TIGR02169 936 IEDPKGEDEEIP--------EEELSLEDVQAELQRVEEEIRALepvnMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1096-1890 |
3.90e-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: 61.91 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1096 QAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTE 1175
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1176 LEDTLDTTA----------AQQELRSKREQE----VAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKS 1241
Cdd:TIGR00618 231 LREALQQTQqshayltqkrEAQEEQLKKQQLlkqlRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1242 NLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQE--FMARATEAERTKGELAERSHKLQTELDNACTMLEV 1319
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1320 AEKKGLKLAKEVDKLNSKL--QDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEarrNLEKQLQMVQSQMFET 1397
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQatIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA---QCEKLEKIHLQESAQS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1398 KKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKtknrlqqELDDLMVDLDHQRQIVSNLEKKQKKFDQL 1477
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI-------HPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1478 LAEEKTISAQYAEERDRA---EAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHElEKS 1554
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRaslKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA-LLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1555 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQamkaqfdrdlqardeqgEEKKRLLVKQVREMEAELEDERKQRT 1634
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT-----------------QERVREHALSIRVLPKELLASRQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1635 LAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSkenEKKLKGLEAEILQLQ 1714
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS---LKELMHQARTVLKAR 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1715 E-DHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNL--- 1790
Cdd:TIGR00618 760 TeAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRlee 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1791 NTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLeqeakeraAANKIVRRTEK 1870
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEI--------TLYANVRLANQ 911
|
810 820
....*....|....*....|
gi 1604804596 1871 KLKEVMMQVEDERRHADQYK 1890
Cdd:TIGR00618 912 SEGRFHGRYADSHVNARKYQ 931
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1656-1886 |
6.78e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1656 AANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELa 1735
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1736 deisnsasgKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQN 1815
Cdd:COG4942 96 ---------RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1816 KDLKAKLAELEGTVKS--KFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHA 1886
Cdd:COG4942 167 AELEAERAELEALLAEleEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1040-1489 |
8.17e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1040 EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALAR 1119
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1120 SDEETLQK--NNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEV 1197
Cdd:COG4717 132 QELEALEAelAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1198 AELKKAIDEETKNHEAQIQEMRQRQATalEELSEQLEQAKR----------FKSNLEKNKQSLENDNKELSCDVKTLQQA 1267
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEA--AALEERLKEARLllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1268 KTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQE 1347
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1348 ETRQKLNLSTQIRQLEVdrntlLEQQEEEEEARRNLEKQLQMVQSQMfETKKKLEEDLGSMEGLEEVKRKLQKdvelTSQ 1427
Cdd:COG4717 370 QEIAALLAEAGVEDEEE-----LRAALEQAEEYQELKEELEELEEQL-EELLGELEELLEALDEEELEEELEE----LEE 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1428 CLEEKTMAMDKMEKTKNRLQQELDDLMVDldhqrqivSNLEKKQKKFDQLLAEEKTISAQYA 1489
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEED--------GELAELLQELEELKAELRELAEEWA 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1528-1720 |
8.68e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1528 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ 1607
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1608 GEEKKRLLV------------------------KQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDE 1663
Cdd:COG4942 117 GRQPPLALLlspedfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1664 AVKQLRKLQAQMKDYQRELEEARASRDEIftqskenEKKLKGLEAEILQLQEDHAAS 1720
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
872-1190 |
1.12e-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: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 872 EEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEM----RVRLLSRK--------Q 939
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsRIPEIQAElskleeevS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 940 ELEEILHDLESRVeeeeernqslqnekkkmqshiqdleeqldeeeaarQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFL 1019
Cdd:TIGR02169 809 RIEARLREIEQKL-----------------------------------NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 KEKKLLEDRISEMTSQLTEEEEKAKnlgkvknkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1099
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALR--------------DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EELKFQLTKKEEELqAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKA-----EKLKR--DLSEELEAL 1172
Cdd:TIGR02169 920 SELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAiqeyeEVLKRldELKEKRAKL 998
|
330
....*....|....*...
gi 1604804596 1173 KTELEDTLDTTAAQQELR 1190
Cdd:TIGR02169 999 EEERKAILERIEEYEKKK 1016
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1380-1708 |
1.18e-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: 60.14 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1380 RRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCL-EEKTMAMDKmEKTKNRLQQelddlmvdld 1458
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYaEQERMAMER-ERELERIRQ---------- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1459 hqrqivsnlEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLM 1538
Cdd:pfam17380 356 ---------EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1539 SSKDDVGKnvhelEKSKRTLEQQVEEM-RTQLEELEDELQAtedAKLRL-EVNMQAMKAQFDRDLQARDEQGEEKKRLLV 1616
Cdd:pfam17380 427 AEQEEARQ-----REVRRLEEERAREMeRVRLEEQERQQQV---ERLRQqEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1617 KQVRE-MEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMK--DYQRELEEARASRDEIF 1693
Cdd:pfam17380 499 KELEErKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMM 578
|
330
....*....|....*
gi 1604804596 1694 TQSKENEKKLKGLEA 1708
Cdd:pfam17380 579 RQIVESEKARAEYEA 593
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1057-1759 |
1.32e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1057 MVDLEERLKKEEKT---RQELEKAKRKLDAEttdlQDQIVELQAQIEELKFQLTKKEEELQAALARsdeetLQK-NNAL- 1131
Cdd:PRK04863 275 MRHANERRVHLEEAlelRRELYTSRRQLAAE----QYRLVEMARELAELNEAESDLEQDYQAASDH-----LNLvQTALr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1132 --KQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEA-------LKTELEDTLDTTAAQQELRSKREQEVAELKK 1202
Cdd:PRK04863 346 qqEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAaeeevdeLKSQLADYQQALDVQQTRAIQYQQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1203 A------IDEETKNHEAQIQEMR---QRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEH 1273
Cdd:PRK04863 426 AkqlcglPDLTADNAEDWLEEFQakeQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1274 KRKKLEA-QLQEFMARATEAERTKGE-------LAERSHKLQTELDNActmlEVAEKKGLKLAKEVDKLNSKLQDSEELR 1345
Cdd:PRK04863 506 REQRHLAeQLQQLRMRLSELEQRLRQqqraerlLAEFCKRLGKNLDDE----DELEQLQEELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1346 QEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQL---QMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDV 1422
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFedsQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1423 ELTSQcleEKTMAMDKMEKTKNRLQQEL-----DDLMVD--------LDHQRQ--IVSNLEKKQkkfDQLLAEEKTISAQ 1487
Cdd:PRK04863 662 ERLSQ---PGGSEDPRLNALAERFGGVLlseiyDDVSLEdapyfsalYGPARHaiVVPDLSDAA---EQLAGLEDCPEDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1488 Y---------------AEERDRAEA---------------------EAREKDTKAL-----SMARALEEALEAKEELERF 1526
Cdd:PRK04863 736 YliegdpdsfddsvfsVEELEKAVVvkiadrqwrysrfpevplfgrAAREKRIEQLraereELAERYATLSFDVQKLQRL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1527 NKQLR----------------AEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQL--------------------- 1569
Cdd:PRK04863 816 HQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladetladr 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1570 -EELEDELQATEDAKL-------------RLEVNMQAMKAQFDRdLQARDEQGEEKKRLL------VKQVREMEAELEDE 1629
Cdd:PRK04863 896 vEEIREQLDEAEEAKRfvqqhgnalaqlePIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAkqqafaLTEVVQRRAHFSYE 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1630 RKQRTLAVASkkklemDLNE-LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLkglea 1708
Cdd:PRK04863 975 DAAEMLAKNS------DLNEkLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL----- 1043
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1709 EILQLQEDHAASERARRHaeqeRDELADEISNSASGKSSLLEEKRRLEARI 1759
Cdd:PRK04863 1044 QDLGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1130-1343 |
1.59e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1130 ALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETK 1209
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1210 NHEAQIQEMRQR--------QATALEEL--SEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLE 1279
Cdd:COG4942 98 ELEAQKEELAELlralyrlgRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1280 AQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEE 1343
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1261-1731 |
1.76e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1261 VKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQD 1340
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1341 SEELRQ-EETRQKLN-LSTQIRQLEvdrntlleqqeEEEEARRNLEKQLQMVQSQMFETKKKLEEDLgsmeglEEVKRKL 1418
Cdd:COG4717 128 LPLYQElEALEAELAeLPERLEELE-----------ERLEELRELEEELEELEAELAELQEELEELL------EQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1419 QKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDH--QRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAE 1496
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1497 AEAREKDTKALSMA----------RALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMR 1566
Cdd:COG4717 271 LILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1567 TQLEELEDELQ--ATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLvKQVREMEAELEDERK--QRTLAVASKKK 1642
Cdd:COG4717 351 ELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGelEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1643 LEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDY--QRELEEARASRDEIftqskenEKKLKGLEAEILQLQEDHAAS 1720
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL-------KAELRELAEEWAALKLALELL 502
|
490
....*....|.
gi 1604804596 1721 ERARRHAEQER 1731
Cdd:COG4717 503 EEAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1072-1315 |
1.76e-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: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1072 QELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEetlqknnALKQVRELQAHLAELQEDLESe 1151
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-------LQAEIAEAEAEIEERREELGE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1152 kmcRSKAEKLKRDLSEELEALK--TELEDTLDTTAAQQELRSKREQEVAELKKAIdEETKNHEAQIQEMRQRQATALEEL 1229
Cdd:COG3883 91 ---RARALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1230 SEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTE 1309
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
....*.
gi 1604804596 1310 LDNACT 1315
Cdd:COG3883 247 AGAGAA 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1677-1951 |
1.88e-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: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1677 DYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSasgKSSLLEEKRRLE 1756
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE---KEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1757 ARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSaaqksenarqqmERQNKdLKAKLAELEgtvkskfkAS 1836
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLR-VKEKIGELE--------AE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1837 IAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR 1916
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270
....*....|....*....|....*....|....*
gi 1604804596 1917 ANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
999-1404 |
1.93e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 999 AKIKKMEEDILLLEDQNSKFLKekklLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMmVDLEERLKKEEKTRQELEKAK 1078
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1079 RKLDAETTDLQdQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQK-NNALKQVRELQAHLAELQEDLEsekmcrsk 1157
Cdd:COG4717 146 ERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELE-------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1158 aeklkrDLSEELEALKTELEDTLDTTAAQQELRSKREQE---------------------------------VAELKKAI 1204
Cdd:COG4717 217 ------EAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1205 DEETKNHEAQIQEMRQRQATALEELSEQLEQaKRFKSNLEKNKQSLENDNKELSCDVKTLQQA-----KTESEHKRKKLE 1279
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEEL-EELLAALGLPPDLSPEELLELLDRIEELQELlreaeELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1280 AQLQEFMARAT---------------EAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKlaKEVDKLNSKLQDSEEL 1344
Cdd:COG4717 370 QEIAALLAEAGvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEE 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1345 RQEETRQKLNLSTQIRQLEVDRN--TLLEQQEEEEEARRNLEKQ---LQMVQSQMFETKKKLEED 1404
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEwaaLKLALELLEEAREEYREE 512
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
867-1617 |
1.94e-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: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 867 QVTRQEEELQAKDEELVKVKERQLKVEN-ELVEMERKHQQLIEEKNILAEQLHA--------ETELFAEAEEMRvRLLSR 937
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANsELTEARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQNK-RLWDR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 938 KQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDeeeaarqklqldkvtaeAKIKKMEEDILLLEDQNSK 1017
Cdd:pfam15921 407 DTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQM-----------------AAIQGKNESLEKVSSLTAQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1018 FLKEKKLLEDRISEMTSQLTEEEEKAKNLGKvknkqemMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ------DQ 1091
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSD-------LTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1092 IVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKM--CRSKAEKLKRDLS-EE 1168
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLelQEFKILKDKKDAKiRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1169 LEALKT--ELEDTLDTTAAQQELRS------KREQEVAELKKA---IDEETKNHEAQIQEMRQRqATALEELSEQLE-QA 1236
Cdd:pfam15921 623 LEARVSdlELEKVKLVNAGSERLRAvkdikqERDQLLNEVKTSrneLNSLSEDYEVLKRNFRNK-SEEMETTTNKLKmQL 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1237 KRFKSNLEKNKQSLENDNKELSCDVKT---LQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNA 1313
Cdd:pfam15921 702 KSAQSELEQTRNTLKSMEGSDGHAMKVamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1314 CT-------MLEVAEKKGLKLAKEV-------DKLNSKLQDSEEL----RQEETRQKLNLSTQIRQLE---VDRNTLLEQ 1372
Cdd:pfam15921 782 ATeknkmagELEVLRSQERRLKEKVanmevalDKASLQFAECQDIiqrqEQESVRLKLQHTLDVKELQgpgYTSNSSMKP 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1373 QEEEEEARRNLEKQLQMVQSQM-FETKKKLEEDLGSMEGLEEVKRKLQkdvELTSQCLEEKTMAMDKME-KTKNRLQQEL 1450
Cdd:pfam15921 862 RLLQPASFTRTHSNVPSSQSTAsFLSHHSRKTNALKEDPTRDLKQLLQ---ELRSVINEEPTVQLSKAEdKGRAPSLGAL 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1451 DDLMVDLDHQRQIVSNLEKKQKKFdqLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQL 1530
Cdd:pfam15921 939 DDRVRDCIIESSLRSDICHSSSNS--LQTEGSKSSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPK 1016
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1531 RAEMEDLMSS--KDDVG--------KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdRD 1600
Cdd:pfam15921 1017 KSPVHSLLTSsaEGSIGsssqyrsaKTIHSPDSVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMI-RN 1095
|
810
....*....|....*..
gi 1604804596 1601 LQARDEQGEEKKRLLVK 1617
Cdd:pfam15921 1096 QEKRIQKVKDQEKMLLK 1112
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
874-1291 |
1.98e-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: 59.74 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 874 ELQAKDEELvkvKERQLKVENELVEMERKHQQLIEEKNILAEQLHAET---ELFAEAEEMRVRLLSRKQELeeilHDLES 950
Cdd:pfam05483 385 ELQKKSSEL---EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKiaeELKGKEQELIFLLQAREKEI----HDLEI 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 951 RVEEEEERNQSLQNEKKKMQSHIQDLeeqldeeeaarqklqldkvtaeaKIKKMEedillLEDQNSKFLKEKKLLEDRIS 1030
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDLKTELEKE-----------------------KLKNIE-----LTAHCDKLLLENKELTQEAS 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1031 EMTSQLTEEEEKAKNlgkVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKE 1110
Cdd:pfam05483 510 DMTLELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1111 EELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1190
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1191 SKREQ--------------EVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKN----KQSLEN 1252
Cdd:pfam05483 667 KISEEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEqssaKAALEI 746
|
410 420 430
....*....|....*....|....*....|....*....
gi 1604804596 1253 DNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATE 1291
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1089-1313 |
2.66e-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: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1089 QDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLEsekmcrskaeklkrDLSEE 1168
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1169 LEALKTELEDTLdtTAAQQELRSKREQEVAELKKAIDEETKNHEAqIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQ 1248
Cdd:COG3883 81 IEERREELGERA--RALYRSGGSVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1249 SLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNA 1313
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1060-1502 |
2.72e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1060 LEERLKKEektRQELEKAKRKLDaetTDLQDQIVELQAQIEELKfqltKKEEELQAALARSDEETLQKNNALKQVRELQA 1139
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1140 HLAELqEDLESEKMCRSKAEKLKRDLSEELEALKtELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMR 1219
Cdd:COG4717 117 ELEKL-EKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1220 QRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELscdvktlqQAKTESEHKRKKLEAQLQEFMARATEAERTkGEL 1299
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLLIAAALLALL-GLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1300 AERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNT----------L 1369
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLspeellelldR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1370 LEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQcLEEKTMAMDKMEKTKNRLQQE 1449
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1450 LDDLMVDLDHQrQIVSNLEKKQKKFDQLLAEEKTISAQYAE-ERDRAEAEAREK 1502
Cdd:COG4717 425 LDEEELEEELE-ELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQE 477
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1125-1782 |
2.74e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1125 LQKNNALKQVRELQAHLAEL---QEDLEsekmcrsKAEKlKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1201
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLeraHEALE-------DARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1202 kaiDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKE-LSCDVKTLQQAKTESEHKRKKLEA 1280
Cdd:COG4913 290 ---LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1281 QLQEFmarATEAERTKGELAERSHKLQTELDnactmlevaekkglKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIR 1360
Cdd:COG4913 367 LLAAL---GLPLPASAEEFAALRAEAAALLE--------------ALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1361 QLEVDRNTLleqQEEEEEARRNLEKQLQMVQSQM------FETKKKLEEDLGSMEG-LEEVKRKLQKDVELTSQcleekt 1433
Cdd:COG4913 430 SLERRKSNI---PARLLALRDALAEALGLDEAELpfvgelIEVRPEEERWRGAIERvLGGFALTLLVPPEHYAA------ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1434 mAMDKMEKTKNRLQqelddlmVDLDHQRQIVSNLEKKQKKFDQLLAEEKT--------ISAQYAEERDRAEAEarekDTK 1505
Cdd:COG4913 501 -ALRWVNRLHLRGR-------LVYERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAELGRRFDYVCVD----SPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1506 ALSMARaleealeakeelerfnkqlRAEMEDLMSSKddvGKNVHELEKSKRTLEQQV--EEMRTQLEELEDELQATEDAK 1583
Cdd:COG4913 569 ELRRHP-------------------RAITRAGQVKG---NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEEL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1584 LRLEVNMQAMKAQFDRDlqardeqgeEKKRLLVKQVREMEAELEDerkqrtlaVASkkkLEMDLNELEGQIEAANKGRDE 1663
Cdd:COG4913 627 AEAEERLEALEAELDAL---------QERREALQRLAEYSWDEID--------VAS---AEREIAELEAELERLDASSDD 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1664 avkqLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHaasERARRHAEQERDELADEISNSAS 1743
Cdd:COG4913 687 ----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAAL 759
|
650 660 670
....*....|....*....|....*....|....*....
gi 1604804596 1744 GKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRK 1782
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1160-1927 |
3.19e-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: 59.29 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1160 KLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAiDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRF 1239
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1240 KSnLEKNKQSLENDNKELSCDVKTLQQAKTEsehkrkkleaQLQEFMARATEAERTKGELAERSHKlQTELDNACTMLEV 1319
Cdd:TIGR00606 272 KA-LKSRKKQMEKDNSELELKMEKVFQGTDE----------QLNDLYHNHQRTVREKERELVDCQR-ELEKLNKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1320 AEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKK 1399
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1400 KLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK--FDQL 1477
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNslTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1478 LAEEKTISAQYAE--ERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSK 1555
Cdd:TIGR00606 500 KKEVKSLQNEKADldRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1556 RTLEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQgeekkrllvkqvremEAELEDerkqRTL 1635
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ---------------LSSYED----KLF 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1636 AVASKKKLEMDLNELEGQIEAANKgrdeavkQLRKLQAQMKDYQRELEEARASR-------DEIFTQSKENEKKLKGLEA 1708
Cdd:TIGR00606 630 DVCGSQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQS 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1709 EILQLQEDHAASERARRHAEQERDEL-------ADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFR 1781
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1782 KSNI-QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASiaaleAKILQLEDQLEQEAKERAA 1860
Cdd:TIGR00606 783 SAKVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEL-----DTVVSKIELNRKLIQDQQE 857
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1861 ANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRE 1927
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1011-1237 |
4.21e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1011 LEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLgkvknKQEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQD 1090
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELE-------SQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1091 QIVELQAQIEELKFQLTKKEEELQAALARSDEETLqknnaLKQVRELQAHLAELQEDLESE----KMCRSKAEKLKRDLS 1166
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL-----RAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1167 EELEALKTELEDTLDTTAAQ-QELRskreQEVAELKKAIDEETKNhEAQIQEMRQRQATA---LEELSEQLEQAK 1237
Cdd:COG3206 309 QEAQRILASLEAELEALQAReASLQ----AQLAQLEARLAELPEL-EAELRRLEREVEVArelYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1060-1606 |
4.36e-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: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1060 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQ--------IEELKFQLTKKEEELQAALARSD--EETLQK-- 1127
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRArlEALLAAlg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1128 ---NNALKQVRELQAHLAELQEDLESEkmcRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAI 1204
Cdd:COG4913 373 lplPASAEEFAALRAEAAALLEALEEE---LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1205 DEETKNHEAQIQ------EMRQRQA---TALEEL-----------SEQLEQAKRFksnLEKNKQSLENDNKELSCDVKTL 1264
Cdd:COG4913 450 AEALGLDEAELPfvgeliEVRPEEErwrGAIERVlggfaltllvpPEHYAAALRW---VNRLHLRGRLVYERVRTGLPDP 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1265 QQAKTES----------EHK-RKKLEAQLQEFMARA---------------TEAERTKGELAERSHKLQTELD------- 1311
Cdd:COG4913 527 ERPRLDPdslagkldfkPHPfRAWLEAELGRRFDYVcvdspeelrrhpraiTRAGQVKGNGTRHEKDDRRRIRsryvlgf 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1312 NACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTlleqqEEEEEARRNLEKQLQmvq 1391
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----ASAEREIAELEAELE--- 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1392 sqmfetkkKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK- 1470
Cdd:COG4913 679 --------RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAl 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1471 -QKKFDQLLAE--EKTISAQYAEERDRAEAEAREKDTKALSMARaleealeakeeleRFNKQLRAEMEDLMSSKDDVGkn 1547
Cdd:COG4913 751 lEERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMR-------------AFNREWPAETADLDADLESLP-- 815
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1548 vhelekskrtleqQVEEMRTQLEelEDEL-QATEDAKLRLEVNMQAMKAQFDRDL-QARDE 1606
Cdd:COG4913 816 -------------EYLALLDRLE--EDGLpEYEERFKELLNENSIEFVADLLSKLrRAIRE 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1379-1632 |
5.12e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1379 ARRNLEKQLQMVQSQMFETKKKLEEdlgsmegLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLmvdld 1458
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1459 hqrqivsnlekkQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLM 1538
Cdd:COG4942 89 ------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1539 SSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLvKQ 1618
Cdd:COG4942 157 ADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-AL 228
|
250
....*....|....
gi 1604804596 1619 VREMEAELEDERKQ 1632
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1444-1951 |
6.99e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1444 NRLQQELDDL------MVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAqyaeERDRAEAEAREKDTKALSMARAleeal 1517
Cdd:COG4913 228 DALVEHFDDLeraheaLEDAREQIELLEPIRELAERYAAARERLAELEY----LRAALRLWFAQRRLELLEAELE----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1518 eakeelerfnkQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQ-LEELEDELQATEDAKLRLEVNMQAMKAQ 1596
Cdd:COG4913 299 -----------ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1597 FdRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQrtlavaskkkLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMK 1676
Cdd:COG4913 368 L-AALGLPLPASAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1677 DYQRELEEARasrDEIFTQSKENEKKLKGLeAEILQLQEDHA----ASER------------------ARRHAEQERDEL 1734
Cdd:COG4913 437 NIPARLLALR---DALAEALGLDEAELPFV-GELIEVRPEEErwrgAIERvlggfaltllvppehyaaALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1735 ----------ADEISNSASGKSSLLEE--------KRRLEARIAQLEEELE--------------EEQGNMELLNDRFRK 1782
Cdd:COG4913 513 rlvyervrtgLPDPERPRLDPDSLAGKldfkphpfRAWLEAELGRRFDYVCvdspeelrrhpraiTRAGQVKGNGTRHEK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1783 --------------SNI-QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKF-KASIAALEAKILQ 1846
Cdd:COG4913 593 ddrrrirsryvlgfDNRaKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1847 LEDQLEQEAkeraAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRR---- 1922
Cdd:COG4913 673 LEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelr 748
|
570 580 590
....*....|....*....|....*....|....*.
gi 1604804596 1923 -----KLQRELDDATEA--SEGLTREVSSLKNRLRR 1951
Cdd:COG4913 749 alleeRFAAALGDAVERelRENLEERIDALRARLNR 784
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1527-1951 |
8.23e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1527 NKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFD-RDLQARD 1605
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1606 EQGEEKkrllVKQVREMEAELED-ERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEE 1684
Cdd:COG4717 149 EELEER----LEELRELEEELEElEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1685 ARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDE-----LADEISNSASGKSSLLEEKRRLEARI 1759
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1760 AQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKakLAELEGTVKSKFKASIAA 1839
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1840 LEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVmmqvedERRHADQYKEQMEKansRMKQLKRQLEEAEEEATRANA 1919
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGEL------EELLEALDEEELEE---ELEELEEELEELEEELEELRE 453
|
410 420 430
....*....|....*....|....*....|....
gi 1604804596 1920 TRRKLQRELDDATEASE--GLTREVSSLKNRLRR 1951
Cdd:COG4717 454 ELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
830-1453 |
8.34e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.75 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 830 KQQQLSALKVLQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERK---HQQL 906
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 907 IEEKNILAEQLHAETELFAEAEEMrvrllsrkqelEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAA 986
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEM-----------EQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 987 RQKLQLDKV--TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNkQEMMMVDLEERL 1064
Cdd:TIGR00606 570 PNKKQLEDWlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEEI 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1065 KKEEKTRQELE----------------------------KAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAA 1116
Cdd:TIGR00606 649 EKSSKQRAMLAgatavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1117 LARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRS---KR 1193
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKI 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1194 EQEVAELKKAIDEETKNheaQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEH 1273
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQ---QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1274 KRKKLEAQLQEFMARATEAERTKGE---LAERSHKLQTE----LDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQ 1346
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKEQdspLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1347 EETRQklnlstQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQsQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTS 1426
Cdd:TIGR00606 966 DGKDD------YLKQKETELNTVNAQLEECEKHQEKINEDMRLMR-QDIDTQKIQERWLQDNLTLRKRENELKEVEEELK 1038
|
650 660
....*....|....*....|....*...
gi 1604804596 1427 QCLEE-KTMAMDKMEKTKNRLQQELDDL 1453
Cdd:TIGR00606 1039 QHLKEmGQMQVLQMKQEHQKLEENIDLI 1066
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
870-1453 |
8.96e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 870 RQEEELQAKDEELVKVKER---QLKVENELVEMERKHQQLIEEKNILAEQLHAETelFAEAEEMRVRLLSRKQELEEILH 946
Cdd:pfam12128 287 ELNQLLRTLDDQWKEKRDElngELSAADAAVAKDRSELEALEDQHGAFLDADIET--AAADQEQLPSWQSELENLEERLK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 947 DLESRVEEEEERNQSLqnEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDI-LLLEDQNSKFLKEKKLL 1025
Cdd:pfam12128 365 ALTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1026 EDRISEMTSQL---TEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD---QIVELQAQI 1099
Cdd:pfam12128 443 KSRLGELKLRLnqaTATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSAL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EELKFQLTKKEEEL--------------------QAALARSD----------------------EETLQKNNALKQVREL 1137
Cdd:pfam12128 523 DELELQLFPQAGTLlhflrkeapdweqsigkvisPELLHRTDldpevwdgsvggelnlygvkldLKRIDVPEWAASEEEL 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1138 QAHLAELQEDLESEK-----------MCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDE 1206
Cdd:pfam12128 603 RERLDKAEEALQSARekqaaaeeqlvQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1207 ETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKsnleknkqslendnkelscdvktlQQAKTESEHKRKKLEAQLQEfm 1286
Cdd:pfam12128 683 RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK------------------------QAYWQVVEGALDAQLALLKA-- 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1287 arATEAERTkgELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETR-----------QKLNL 1355
Cdd:pfam12128 737 --AIAARRS--GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRL 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1356 STQIRQLEVD----RNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVK-----RKLQKDVELTS 1426
Cdd:pfam12128 813 ATQLSNIERAiselQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERL 892
|
650 660
....*....|....*....|....*..
gi 1604804596 1427 QCLEEktmAMDKMEKTKNRLQQELDDL 1453
Cdd:pfam12128 893 AQLED---LKLKRDYLSESVKKYVEHF 916
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
857-1290 |
1.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 857 RLFTKVKPLLQVTRQEEELQAKDEELvKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLS 936
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 937 RKQELEEILHDLEsrveeeEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQldkvTAEAKIKKMEEDILLLEDQNS 1016
Cdd:COG4717 168 LEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELE----EAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1017 KFLKEKKLLEDR--------ISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQElEKAKRKLDAETTDL 1088
Cdd:COG4717 238 AAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK-EAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1089 QDQivELQAQIEELKFQLTKKEEELQAALARsdeetlqknnaLKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEE 1168
Cdd:COG4717 317 EEE--ELEELLAALGLPPDLSPEELLELLDR-----------IEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1169 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQ 1248
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1604804596 1249 SLENDNkelscdvkTLQQAKTESEHKRKKLEAQLQEFMARAT 1290
Cdd:COG4717 464 QLEEDG--------ELAELLQELEELKAELRELAEEWAALKL 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1650-1902 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1650 LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFT--QSKENEKKLKGLEAEILQLQEDHAASERARRHA 1727
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1728 EQERDELADEISN--SASGKSSLLEEKRRLEARIAQleeeleeeqgnmelLNDRFRKSNIQVDNLNTELAgersaaqkse 1805
Cdd:COG3206 246 RAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAE--------------LSARYTPNHPDVIALRAQIA---------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1806 narqqmerqnkDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIvrrtEKKLKEVMMQVEDERRH 1885
Cdd:COG3206 302 -----------ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVAREL 366
|
250
....*....|....*..
gi 1604804596 1886 ADQYKEQMEKANSRMKQ 1902
Cdd:COG3206 367 YESLLQRLEEARLAEAL 383
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1081-1309 |
1.17e-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: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1081 LDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETL--QKNNALKQVRELQAHLAELQEDLESEkmcRSKA 1158
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEA---EARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1159 EKLKRDLSEELEALKTELEDtldttAAQQELRSKREQEVAELKKAIDEETKNHEaQIQEMRQRQATALEELSEQLEQAKr 1238
Cdd:COG3206 243 AALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHP-DVIALRAQIAALRAQLQQEAQRIL- 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1239 fksnleknkQSLENDNKELSCDVKTLQQAKTESEHKRKKL---EAQLQEFMARATEAERTKGELAERSHKLQTE 1309
Cdd:COG3206 316 ---------ASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1088-1874 |
1.29e-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: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1088 LQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVREL-QAHLAELQE-DLESEKMCRSKAEKLK--R 1163
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEEIQenK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1164 DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQI---QEMRQRQATALEELSEQLEQAKRFK 1240
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMIlafEELRVQAENARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1241 SNLEKNKQSLENDNKElscDVKTLQQAKTESEHKRKKLEAQLQEfmarateaERTKGELAERSHKLQTEldnacTMLEVA 1320
Cdd:pfam05483 225 QHLEEEYKKEINDKEK---QVSLLLIQITEKENKMKDLTFLLEE--------SRDKANQLEEKTKLQDE-----NLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1321 EKKGlKLAKEVDKLNSKLQDSEElRQEETRQKLNLSTQ-IRQLEVDRNTLLEQQEEEEEARrnlekqlQMVQSQMFETKK 1399
Cdd:pfam05483 289 EKKD-HLTKELEDIKMSLQRSMS-TQKALEEDLQIATKtICQLTEEKEAQMEELNKAKAAH-------SFVVTEFEATTC 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1400 KLEEDLGSMEGLEEvkrKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLA 1479
Cdd:pfam05483 360 SLEELLRTEQQRLE---KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1480 EEKTISAQYaeerdraeaEAREKDTKALSMarALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLE 1559
Cdd:pfam05483 437 KEQELIFLL---------QAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1560 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfDRDLQARDEqgeekkrllVKQVREMEAELEDERKQRTlavas 1639
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDE---------LESVREEFIQKGDEVKCKL----- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1640 kKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAA 1719
Cdd:pfam05483 569 -DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1720 serARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNME--------LLNDRFRKSNIQVDNLN 1791
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvaLMEKHKHQYDKIIEERD 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1792 TELAGERSAAQKSENARQQMERQNKDLKAKLaelegtvkskfkasiaaleakiLQLEDQLEQEAKERAAANKIVRRTEKK 1871
Cdd:pfam05483 725 SELGLYKNKEQEQSSAKAALEIELSNIKAEL----------------------LSLKKQLEIEKEEKEKLKMEAKENTAI 782
|
...
gi 1604804596 1872 LKE 1874
Cdd:pfam05483 783 LKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1528-1761 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1528 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdrdlqardeq 1607
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1608 gEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAankgrdeavkqlrkLQAQMKDYQRELEEARA 1687
Cdd:COG4942 100 -EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--------------RREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1688 SRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQ 1761
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1071-1733 |
1.35e-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: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1071 RQELEKAKRKLDAETTDLQDQIVELQA-QIEELKfqltKKEEELqaalaRSDEETlqknnALKQVRELQAHLAELQEDLE 1149
Cdd:pfam07111 43 GQGPGRRGRSLELEGSQALSQQAELISrQLQELR----RLEEEV-----RLLRET-----SLQQKMRLEAQAMELDALAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1150 SEKMCRSKAEKLKRDLSEElEALKTELEDtldttAAQQELrskreQEVAELkkaideetknHEAQIQEMRQRQATALEEL 1229
Cdd:pfam07111 109 AEKAGQAEAEGLRAALAGA-EMVRKNLEE-----GSQREL-----EEIQRL----------HQEQLSSLTQAHEEALSSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1230 SEQLEqakrfksNLEKNKQSLENDNkelSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAErshklQTE 1309
Cdd:pfam07111 168 TSKAE-------GLEKSLNSLETKR---AGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGE-----QVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1310 LDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETrQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRN---LEKQ 1386
Cdd:pfam07111 233 PEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRV-QSLTHMLALQEEELTRKIQPSDSLEPEFPKKCrslLNRW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1387 LQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVelTSQCLEEKTmamdkmektknrLQQELDDLMVDLDHQRQIVSN 1466
Cdd:pfam07111 312 REKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQV--TSQSQEQAI------------LQRALQDKAAEVEVERMSAKG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1467 LEKKQKKFDQLLAEEKTISAQYAEE-RDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRA--EMEDLMSSKDD 1543
Cdd:pfam07111 378 LQMELSRAQEARRRQQQQTASAEEQlKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKGLMARKVA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1544 VGKNVHELEKSKRTLEQQVEEMRTQLEELEDElqatedaKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREME 1623
Cdd:pfam07111 458 LAQLRQESCPPPPPAPPVDADLSLELEQLREE-------RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1624 AELedERKQRTLAVASkKKLEMDLNELEGQIEAANKGRDEAVKQLR---------------KLQAQMKDYQRELEEARAS 1688
Cdd:pfam07111 531 QEL--QRAQESLASVG-QQLEVARQGQQESTEEAASLRQELTQQQEiygqalqekvaevetRLREQLSDTKRRLNEARRE 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1689 RDEIF----------TQSKENEKKLKGLEAEilqlQEDHAASERARRHAEQERDE 1733
Cdd:pfam07111 608 QAKAVvslrqiqhraTQEKERNQELRRLQDE----ARKEEGQRLARRVQELERDK 658
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1952 |
1.37e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1714 QEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTE 1793
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1794 LAGERSAAQKSENARQQMERQNKdLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLK 1873
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1874 EVMMQVEDERRhadQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRRG 1952
Cdd:COG4942 178 ALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1195-1640 |
1.52e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1195 QEVAELKKAIDEEtKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLENDnKELSCDVKTLQQAKTESEHK 1274
Cdd:COG4717 71 KELKELEEELKEA-EEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1275 RKKLEaQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLK-LAKEVDKLNSKLQDSEELRQEETRQKL 1353
Cdd:COG4717 145 PERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1354 NLSTQIRQLEVDRNTLleqqeeEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEV-----------KRKLQKDV 1422
Cdd:COG4717 224 ELEEELEQLENELEAA------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1423 ELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREK 1502
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1503 DTKA------LSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKnvHELEKSKRTLEQQVEEMRTQLEELEDEL 1576
Cdd:COG4717 378 EAGVedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 1577 QATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKK----RLLVKQVREMEAELEDERKQRTLAVASK 1640
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELEELKAELRELAEEwaalKLALELLEEAREEYREERLPPVLERASE 523
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
928-1510 |
1.53e-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: 56.75 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 928 EEMRVRLLSRKQELEeilhdlesrveeeeERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKlqldkVTAEAKIKKMEed 1007
Cdd:pfam10174 140 EEMELRIETQKQTLG--------------ARDESIKKLLEMLQSKGLPKKSGEEDWERTRRI-----AEAEMQLGHLE-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1008 iLLLEDQNSKFLKEKKLLEDRisemtSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEktrQELEKAKRKLDAETTD 1087
Cdd:pfam10174 199 -VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1088 LQDQIVELQA----------QIEELKFQLTKKEEELQAALARSDE------------ETLQKNNALKQVRE--LQAHLAE 1143
Cdd:pfam10174 270 REEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1144 LQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAqqelrskREQEVAELKKAID---EETKNHEAQIQEMRQ 1220
Cdd:pfam10174 350 LRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGLKE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1221 RQA----------TALEELSEQLEQAKRFKSNLEKNKqslENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARAT 1290
Cdd:pfam10174 423 RVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1291 EAERTKGELAERSHKLQTELDNactmLEVAEKKGLKlakEVDKLNSKLQDSEELrQEETRQKLNLSTQIRQLEVDRNTLL 1370
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKS----LEIAVEQKKE---ECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQEVARYK 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1371 EQQEEEEEARRNLEKQLQMVQSQMFETKKKLE--EDLGSMEGLEEVKRKLQKDvelTSQCLEEKTMAM-------DKMEK 1441
Cdd:pfam10174 572 EESGKAQAEVERLLGILREVENEKNDKDKKIAelESLTLRQMKEQNKKVANIK---HGQQEMKKKGAQlleearrREDNL 648
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1442 TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMA 1510
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1182-1413 |
1.84e-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: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1182 TTAAQQELRSKREQEVAELKKAIdEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLEndnkelscdv 1261
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEI-AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1262 KTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDS 1341
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1342 EELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEE 1413
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1068-1238 |
1.93e-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: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1068 EKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELK--FQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQ 1145
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1146 EDLES--EKMCRSKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELRSKREQeVAELKKAIDEETKNHEAQIQEMRQRQ 1222
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQ-IAALRAQLQQEAQRILASLEAELEAL 325
|
170
....*....|....*.
gi 1604804596 1223 ATALEELSEQLEQAKR 1238
Cdd:COG3206 326 QAREASLQAQLAQLEA 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
790-1318 |
1.96e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 790 FFRTGVLahleEERDL--KITDIIIYFQSVCRgylARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWW 856
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 857 RLFTKVKpLLQ--VTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQL-IEEKNILAEQLhaetelfAEAEEMRVR 933
Cdd:COG4913 285 FAQRRLE-LLEaeLEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREI-------ERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 934 LLSRKQELEEILHDLESRVEEEEernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLED 1013
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1014 QNSKFLKEkklLEDRISEMTSQLTEEEEKAKNLG---KVKNKQEM---------------MMVDlEERLKK------EEK 1069
Cdd:COG4913 434 RKSNIPAR---LLALRDALAEALGLDEAELPFVGeliEVRPEEERwrgaiervlggfaltLLVP-PEHYAAalrwvnRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1070 TRQELekakRKLDAETTDLQDQIVELQAQ--IEELKFQLTKKEEELQAALARS-------DEETL--------------- 1125
Cdd:COG4913 510 LRGRL----VYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAELGRRfdyvcvdSPEELrrhpraitragqvkg 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1126 -----QKN-------------NALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELE---DTLDTTA 1184
Cdd:COG4913 586 ngtrhEKDdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1185 AQQELRSKrEQEVAELKKAIDEetknhEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTL 1264
Cdd:COG4913 666 AEREIAEL-EAELERLDASSDD-----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1265 qqAKTESEHKRKKLEAQLQEFMARATEAERTKgELAERSHKLQTELDNACTMLE 1318
Cdd:COG4913 740 --EDLARLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNRAEEELE 790
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1529-1861 |
2.50e-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: 55.46 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1529 QLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFDRDLQARDEQG 1608
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1609 EEKKRLLVK---QVREMEAELEDERKQ-RTLAVASK------KKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDY 1678
Cdd:pfam19220 107 EELRIELRDktaQAEALERQLAAETEQnRALEEENKalreeaQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1679 QRELEEARASRDEIFTQSKENEKKLKGLEAeilQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEAR 1758
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEG---QLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1759 IAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQ-----------NKDLKAKLAELEG 1827
Cdd:pfam19220 264 LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraeleeraemlTKALAAKDAALER 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1604804596 1828 -------------TVKSKFKASIAALEAKILQLEDQLEQEAKERAAA 1861
Cdd:pfam19220 344 aeeriaslsdriaELTKRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
881-1452 |
2.58e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.90 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 881 ELVKVKERQLKVENELVEMERKHQqliEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQ 960
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK---RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 961 SLqneKKKMQSHIQDLEEQLDEEEAARQ-KLQLDKVTAEAKIKKMEEDILLLEDQNSK--FLKEKKLLEDRISEMtSQLT 1037
Cdd:pfam05557 80 LK---KKYLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQRAELELQSTNSELeeLQERLDLLKAKASEA-EQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1038 EEEEKAKNLGKVKNKQemmMVDLEERLKKEEKTRQELEKAKRKLdAETTDLQDqivELQAQIEELKFQLTKKEEELqaaL 1117
Cdd:pfam05557 156 QNLEKQQSSLAEAEQR---IKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEK---ELERLREHNKHLNENIENKL---L 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1118 ARSDEETLQKNnaLKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEEL---EALKTELEDTLDTTAAQQELRSKRE 1194
Cdd:pfam05557 226 LKEEVEDLKRK--LEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1195 QEVAELKKAIDE---ETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKN----KQSLENDNKELSCDVKTLQQA 1267
Cdd:pfam05557 304 SSARQLEKARREleqELAQYLKKIEDLNKK----LKRHKALVRRLQRRVLLLTKErdgyRAILESYDKELTMSNYSPQLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1268 K--TESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKlaKEVDKLNSKLQDSEELR 1345
Cdd:pfam05557 380 EriEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELER 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1346 QEETRQKLNLSTQIRQLEVDRNTLLEQQeeeeearrnleKQLQMVQSQMFETKKKLEEDLGSM----EGLEEVKRKLQKD 1421
Cdd:pfam05557 458 QRLREQKNELEMELERRCLQGDYDPKKT-----------KVLHLSMNPAAEAYQQRKNQLEKLqaeiERLKRLLKKLEDD 526
|
570 580 590
....*....|....*....|....*....|.
gi 1604804596 1422 VElTSQCLEEKTMAMDkmEKTKNRLQQELDD 1452
Cdd:pfam05557 527 LE-QVLRLPETTSTMN--FKEVLDLRKELES 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
920-1496 |
2.82e-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: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 920 ETELFAEAEEMrvrllsrkQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEeaaRQKLQLDKVTAEA 999
Cdd:COG4913 220 EPDTFEAADAL--------VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE---YLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1000 KIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTE-EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAK 1078
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1079 RKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARsdeetlqknnALKQVRELQAHLAELQEDLESEKMCRS-- 1156
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE----------AEAALRDLRRELRELEAEIASLERRKSni 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1157 --KAEKLKRDLSEELEALKTEL-----------EDTLDTTAAQQELRSKR------EQEVAELKKAIDE----------- 1206
Cdd:COG4913 439 paRLLALRDALAEALGLDEAELpfvgelievrpEEERWRGAIERVLGGFAltllvpPEHYAAALRWVNRlhlrgrlvyer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1207 ----------------------ETKNHEAQ---IQEMRQRQATALEELSEQLEQAKR-------FKSNL---EKNKQS-- 1249
Cdd:COG4913 519 vrtglpdperprldpdslagklDFKPHPFRawlEAELGRRFDYVCVDSPEELRRHPRaitragqVKGNGtrhEKDDRRri 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1250 -----LENDNKELscdVKTLQQaktesehKRKKLEAQLQEFMARATEAERTKGELAERSHKLQ-------TELDNACTML 1317
Cdd:COG4913 599 rsryvLGFDNRAK---LAALEA-------ELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVASAER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1318 EVAEKKGLKLA-----KEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQS 1392
Cdd:COG4913 669 EIAELEAELERldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1393 QMFEtkKKLEEDLGSmEGLEEVKRKLQKDVE-LTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLD--------HQRQI 1463
Cdd:COG4913 749 ALLE--ERFAAALGD-AVERELRENLEERIDaLRARLNRAEEELERAMRAFNREWPAETADLDADLEslpeylalLDRLE 825
|
650 660 670
....*....|....*....|....*....|....*...
gi 1604804596 1464 VSNLEKKQKKFDQLLAEEKT-----ISAQYAEERDRAE 1496
Cdd:COG4913 826 EDGLPEYEERFKELLNENSIefvadLLSKLRRAIREIK 863
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1415-1702 |
5.32e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1415 KRKLQKDVeltsqcLEEKTMA-MDKMEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQL 1477
Cdd:PHA02562 152 RRKLVEDL------LDISVLSeMDKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1478 LAEEKTISAQYAEERDRAEAEAREKDTKALSMaraleealeakeelerfnKQLRAEMEDLMSSKDDVGKNVHELEKSKR- 1556
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSAAL------------------NKLNTAAAKIKSKIEQFQKVIKMYEKGGVc 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1557 -TLEQQVEEMRTQLEELEDelqatedaklrlevNMQAMKAQFDRDLQARDEqgeekkrllvkqvremEAELEDErkqrtL 1635
Cdd:PHA02562 288 pTCTQQISEGPDRITKIKD--------------KLKELQHSLEKLDTAIDE----------------LEEIMDE-----F 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1636 AVASKKKLEM--DLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKK 1702
Cdd:PHA02562 333 NEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1644-1874 |
6.54e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1644 EMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEdhAASERA 1723
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE--ELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1724 RrhAEQERDELADEISN--SASGKSSLLEekrRLEAriaqleeeleeeqgnMELLNDRFRKSNIQVDNLNTELAGERSAA 1801
Cdd:COG3883 93 R--ALYRSGGSVSYLDVllGSESFSDFLD---RLSA---------------LSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1802 qksENARQQMERQNKDLKAKLAELEGTVKSKfKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKE 1874
Cdd:COG3883 153 ---EAKLAELEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1270-1945 |
7.45e-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: 54.46 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1270 ESEHKRKKLEAQLQEFMA-RATEAERTKGE-LAERSHKLQTELDNACTM------LEVAEKKGLKLAKEVDK-LNSKL-- 1338
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIQAiAGIMKIRPEFTkLQQEFNTLESAELRLSHLhfgyksDETLIASRQEERQETSAeLNQLLrt 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1339 ------QDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLE 1412
Cdd:pfam12128 295 lddqwkEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVT 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1413 E--------VKRKLQKDVELTSQCLE--------EKTMAMDKMEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFD 1475
Cdd:pfam12128 375 AkynrrrskIKEQNNRDIAGIKDKLAkireardrQLAVAEDDLQALESELREQLEAGKLEFnEEEYRLKSRLGELKLRLN 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1476 QLLAEEKTISAQyaEERDRAEAEAREKDTKAlsmaraleealeakeelerfnkqlRAEMEDLMSSKDDVGKNVHELEKSK 1555
Cdd:pfam12128 455 QATATPELLLQL--ENFDERIERAREEQEAA------------------------NAEVERLQSELRQARKRRDQASEAL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1556 RTLEQQVEEMRTQLEELEDELQA----------TEDAKLRLEVNMQAMKAQFDR-DLQARDEQGEEKKRLLVKQVRemea 1624
Cdd:pfam12128 509 RQASRRLEERQSALDELELQLFPqagtllhflrKEAPDWEQSIGKVISPELLHRtDLDPEVWDGSVGGELNLYGVK---- 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1625 eLEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASrdeiFTQSKENEKKLK 1704
Cdd:pfam12128 585 -LDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLF 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1705 G-LEAEILQLQEdhaASERARRHAEQERDELADEISNSASGKSSLLEEKRR--LEARIAQLeeeleeeQGNMELLNDRfr 1781
Cdd:pfam12128 660 DeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL-- 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1782 ksNIQVDNLNTELAGERSAAQKSENA-RQQMERqnkDLKAKlaELEGTVKSKFKASIAALEAKIlqledqlEQEAKERAA 1860
Cdd:pfam12128 728 --DAQLALLKAAIAARRSGAKAELKAlETWYKR---DLASL--GVDPDVIAKLKREIRTLERKI-------ERIAVRRQE 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1861 ankiVRRTEKKLKEVMMQvederrHADQYKEQMEKANSRMK----QLKRQLEEAEEEATRANATRRKLQRELDDATEASE 1936
Cdd:pfam12128 794 ----VLRYFDWYQETWLQ------RRPRLATQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
....*....
gi 1604804596 1937 GLTREVSSL 1945
Cdd:pfam12128 864 GLRCEMSKL 872
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1001-1228 |
7.96e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.52 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1001 IKKMEEDILLLE-------DQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQE 1073
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE-EQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1074 LEKA-KRKLDAETTDLQDQIVELQAQIEELKFQLTKkeeelqaaLARSDEE--TLQKNNAL--KQVRELQAHLAELQEDL 1148
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIE--------VAETEERvfKLEKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1149 esekmcrSKAEKLKRD-LSEELEalktELEDTLDTTAAQQELRSKREQEVAELKKAIDE-ETKNHEAQIQ-------EMR 1219
Cdd:PLN02939 288 -------SKLSPLQYDcWWEKVE----NLQDLLDRATNQVEKAALVLDQNQDLRDKVDKlEASLKEANVSkfssykvELL 356
|
....*....
gi 1604804596 1220 QRQATALEE 1228
Cdd:PLN02939 357 QQKLKLLEE 365
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
868-1508 |
8.44e-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: 54.37 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 868 VTRQEEELQAKDEELVKVKE----RQLKVENELVEMErkhQQLIEEKNILAEQLHAETELfAEAEEMRVRLLSRKQ-ELE 942
Cdd:pfam07111 68 ISRQLQELRRLEEEVRLLREtslqQKMRLEAQAMELD---ALAVAEKAGQAEAEGLRAAL-AGAEMVRKNLEEGSQrELE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 943 EIlhdlesrveeeeernQSLQNEK--KKMQSHiqdleeQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQnskflK 1020
Cdd:pfam07111 144 EI---------------QRLHQEQlsSLTQAH------EEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----K 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1021 EKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQemmmVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIE 1100
Cdd:pfam07111 198 EAELLRKQLSKTQEELEAQVTLVESLRKYVGEQ----VPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1101 ELKFQLTKKEEELQAALARSD----EETLQKNNALKQVRELQAHLaelqedlesekMCRSKAEKLK-RDLSEELEalkte 1175
Cdd:pfam07111 274 SLTHMLALQEEELTRKIQPSDslepEFPKKCRSLLNRWREKVFAL-----------MVQLKAQDLEhRDSVKQLR----- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1176 ledtlDTTAAQQELRSKREQEVAELKKAIDEETKnhEAQIQEMrqrqatALEELSEQLEQAKRFKSNLEKNKQSLENDNK 1255
Cdd:pfam07111 338 -----GQVAELQEQVTSQSQEQAILQRALQDKAA--EVEVERM------SAKGLQMELSRAQEARRRQQQQTASAEEQLK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1256 ELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERT----KGELAERSHKLQTELDnACTMLEVAEKKGLKLAKEV 1331
Cdd:pfam07111 405 FVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhtiKGLMARKVALAQLRQE-SCPPPPPAPPVDADLSLEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1332 dklnsklqdsEELRQEETR--QKLNLSTQIRQLEVDRNTLLEQQEEEEEAR--RNLEKQLQMVQSQMFETKKKLEEDL-G 1406
Cdd:pfam07111 484 ----------EQLREERNRldAELQLSAHLIQQEVGRAREQGEAERQQLSEvaQQLEQELQRAQESLASVGQQLEVARqG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1407 SMEGLEE---VKRKLQKDVELTSQCLEEktmamdKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKt 1483
Cdd:pfam07111 554 QQESTEEaasLRQELTQQQEIYGQALQE------KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK- 626
|
650 660
....*....|....*....|....*
gi 1604804596 1484 isaQYAEERDRAEAEAREKDTKALS 1508
Cdd:pfam07111 627 ---ERNQELRRLQDEARKEEGQRLA 648
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1592-1738 |
8.58e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1592 AMKAQFDR--DLQARDEQGEEKKRLLV---KQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVK 1666
Cdd:COG1579 1 AMPEDLRAllDLQELDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1667 QLRKLQA--QMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEI 1738
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1037-1249 |
9.11e-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: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1037 TEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAA 1116
Cdd:COG3883 16 PQIQAKQKELSELQAELE----AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1117 L------------------ARSDEETLQKNNALKQVRELQAHLAELQEDLesekmcRSKAEKLKrdlsEELEALKTELED 1178
Cdd:COG3883 92 AralyrsggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKAD------KAELEAKK----AELEAKLAELEA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1179 TLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQS 1249
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1175-1866 |
9.74e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1175 ELEDTLDTTAAQqelRSKREQEVAELKKAidEETKNHEAQIQEMRQRQATALEELSEQLeqaKRFKSNLEKNKQSLENDN 1254
Cdd:PRK01156 139 EMDSLISGDPAQ---RKKILDEILEINSL--ERNYDKLKDVIDMLRAEISNIDYLEEKL---KSSNLELENIKKQIADDE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1255 KELSCDVKTLQQAKTESEHKRKK---LEAQLQEFMARATEAERTKGELAERSHKLQTEldnactmlevaEKKGLKLAKEV 1331
Cdd:PRK01156 211 KSHSITLKEIERLSIEYNNAMDDynnLKSALNELSSLEDMKNRYESEIKTAESDLSME-----------LEKNNYYKELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1332 DKLNSKLQDSEELRQEETRQKLNLSTQIrqleVDRNTLLeqqeeeeearRNLEKQLQMVQSQMfetkKKLEEdlgsmegl 1411
Cdd:PRK01156 280 ERHMKIINDPVYKNRNYINDYFKYKNDI----ENKKQIL----------SNIDAEINKYHAII----KKLSV-------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1412 eevkrkLQKDVEltsqcleektmAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEE 1491
Cdd:PRK01156 334 ------LQKDYN-----------DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1492 RDRAEAEAREkdtkalsmaraleealeakeelerfnkqLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEE 1571
Cdd:PRK01156 397 LKIQEIDPDA----------------------------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEM 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1572 LEDE---------LQATEDAKLRLEVNMQAMKAQFD-----RDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAV 1637
Cdd:PRK01156 449 LNGQsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKireieIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESAR 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1638 ASKKKLEMDLNELEGQIEAANKGRDEAVK-QLRKLQAQMKDYQR--------ELEEARASRDEIFTQSKENEKKLKGLEA 1708
Cdd:PRK01156 529 ADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNalavisliDIETNRSRSNEIKKQLNDLESRLQEIEI 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1709 EIlqlQEDHAASERARRHAEQErdeladeiSNSASGKSSLLEEKRRLEARIAQLEeeleeeqgnmellnDRFRKSNIQVD 1788
Cdd:PRK01156 609 GF---PDDKSYIDKSIREIENE--------ANNLNNKYNEIQENKILIEKLRGKI--------------DNYKKQIAEID 663
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 1789 NLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSkFKASIAALEAKILQLEDQLEQEAKERAAANKIVR 1866
Cdd:PRK01156 664 SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI-LRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1379-1907 |
1.14e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1379 ARRNLEKQLQMVQ--SQMFETKKKLEEDLGSMEGLEEVKRKLqkDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVD 1456
Cdd:COG4913 240 AHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1457 LDHQRQIVSNLEKK--QKKFDQLlaeektisAQYAEERDRAEAEAREKDTKAlsmaraleealeakeelERFNKQLRAEM 1534
Cdd:COG4913 318 LDALREELDELEAQirGNGGDRL--------EQLEREIERLERELEERERRR-----------------ARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1535 EDLMSSKDDVGKNV--------------HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRD 1600
Cdd:COG4913 373 LPLPASAEEFAALRaeaaallealeeelEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1601 LQARDEQ-----------GEEKK--------------RLLV-----KQVREMEAELEDERKQRTLAVASKKKLEMDLNEL 1650
Cdd:COG4913 453 LGLDEAElpfvgelievrPEEERwrgaiervlggfalTLLVppehyAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1651 EGQIE-----AANKGRDEAVKQLRKL--------QAQMKDYQREL---------EEARASRDEIFTQSK-----ENEKKL 1703
Cdd:COG4913 533 PDSLAgkldfKPHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAItragqvkgnGTRHEKDDRRRIRSRyvlgfDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1704 KGLEAEILQLQEDHAASERARRHAEQERDEladeisnsasgksslLEEKRRLEARIAQleeeleeeqgnmellndrFRKS 1783
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDA---------------LQERREALQRLAE------------------YSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1784 NIQVDNLNTELA---GERSAAQKSENARQQMERQNKDLKAKLAELEGTVKsKFKASIAALEAKILQLEDQLEQEAKERAA 1860
Cdd:COG4913 660 EIDVASAEREIAeleAELERLDASSDDLAALEEQLEELEAELEELEEELD-ELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1861 ANKIVR-----RTEKKLKEVMMQvEDERRHADQYKEQMEKANSRMKQLKRQL 1907
Cdd:COG4913 739 AEDLARlelraLLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1706-1948 |
1.27e-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: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1706 LEAEILQLQEDHAASERARRHAEQERDELAdeisnsasgkssLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKsnI 1785
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQ--R 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1786 QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAaankiv 1865
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRA------ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1866 rRTEKKLKEVMMQVEDErrhADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDateasegLTREVSSL 1945
Cdd:COG4913 363 -RLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIASL 431
|
...
gi 1604804596 1946 KNR 1948
Cdd:COG4913 432 ERR 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1126-1352 |
1.31e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1126 QKNNALKQVRELQAHLAELQEDLESekmcrskaeklkrdLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID 1205
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA--------------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1206 EETKNHEAQIQEMRQ--RQATALEEL--SEQLEQakrFKSNLEKNKQSLENDNKELscdvKTLQQAKTESEHKRKKLEAQ 1281
Cdd:COG3883 83 ERREELGERARALYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1282 LQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQK 1352
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1550-1710 |
1.73e-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: 51.46 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1550 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQGEEKKrllVKQVREMEAELEDE 1629
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN---NKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1630 RKQRtlavaskKKLEMDLNELEGQIEAANKgrdeavkQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAE 1709
Cdd:COG1579 102 KRRI-------SDLEDEILELMERIEELEE-------ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
.
gi 1604804596 1710 I 1710
Cdd:COG1579 168 L 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1020-1424 |
1.86e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAettdlQDQIVELQAQI 1099
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEK-----LLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EELKFQLTKKEEELQAALARSDEEtlqkNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLK-RDLSEELEALKTELED 1178
Cdd:COG4717 135 EALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1179 TLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEK-----------NK 1247
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllalLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1248 QSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKL 1327
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1328 AKEVDKLNSKLQDSEELRQ--EETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEA--RRNLEKQLQMVQSQMFETKKKLEE 1403
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEE 450
|
410 420
....*....|....*....|.
gi 1604804596 1404 DLGSMEGLEEVKRKLQKDVEL 1424
Cdd:COG4717 451 LREELAELEAELEQLEEDGEL 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1399-1874 |
2.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1399 KKLEEDLGSMEGLEEVKRKLQKDveltsqcLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQ------RQIVSNLEKKQK 1472
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEE-------LEELEEELEELEAELEELREELEKLEKLLQLLplyqelEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1473 KFDQLLAEEKTIsAQYAEERDRAEAEAREKDTKAlsmaraleealeaKEELERFNKQLRAEMEDLMSSKDDVGKNVHELE 1552
Cdd:COG4717 147 RLEELEERLEEL-RELEEELEELEAELAELQEEL-------------EELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1553 KSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKR-------------LLVKQV 1619
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1620 REMEAELEDERKQRTLAVASKKKLEMdlNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIftqsken 1699
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL------- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1700 ekKLKGLEAEILQL-QEDHAASERARRHAEQERDELADeisnsasgkssLLEEKRRLEARIAQLEEELEEEQGNMELlnd 1778
Cdd:COG4717 364 --QLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQE-----------LKEELEELEEQLEELLGELEELLEALDE--- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1779 rfrksniqvDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGtvkskfKASIAALEAKILQLEDQLEQEAKER 1858
Cdd:COG4717 428 ---------EELEEELEELEEELEELEEELEELREELAELEAELEQLEE------DGELAELLQELEELKAELRELAEEW 492
|
490
....*....|....*....
gi 1604804596 1859 AAAN---KIVRRTEKKLKE 1874
Cdd:COG4717 493 AALKlalELLEEAREEYRE 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1541-1761 |
4.19e-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: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1541 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA----------TEDAKLRLEvNMQAMKAQFdRDLQARDEQGEE 1610
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQ-QLSELESQL-AEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1611 KKRLLVKQVREMEAELEDERKQRTLAvaskkKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQREL-EEARASR 1689
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQ-----QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1690 DEIFTQSKENEKKLKGLEAEILQLQEDHAA-SERARRHAEQERD-ELADEISNsasgksSLLeeKRRLEARIAQ 1761
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYE------SLL--QRLEEARLAE 381
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1609-1758 |
4.32e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1609 EEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIE--------AANKGRD----EAVKQLRKLQAQMK 1676
Cdd:COG1842 22 EDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEAQAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1677 DYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLqedhAASERARRHAEQERDELADEISNSASGKSSLLEEK-RRL 1755
Cdd:COG1842 102 ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL----KARAKAAKAQEKVNEALSGIDSDDATSALERMEEKiEEM 177
|
...
gi 1604804596 1756 EAR 1758
Cdd:COG1842 178 EAR 180
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1486-1858 |
4.78e-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: 51.43 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1486 AQYAEERDRaEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1565
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1566 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKqVREMEAELederkqRTLAvaskKKLEM 1645
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK-LQQTEEEL------RSLS----KEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1646 DLNELEGQIEAANKGRDEAVKQLRKL-QAQMKDYQRE--LEEARASRDEIFTqskeNEKKLKGLEAEILQL--QEDHAAS 1720
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNA----SERKVEGLGEELSSMaaQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1721 E--RARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGER 1798
Cdd:pfam07888 273 ElhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1799 --SAAQKSENARQQMErqnkdLKAKLAELEGTvKSKFKASIAALEAKILQLEDQLEQEAKER 1858
Cdd:pfam07888 353 dcNRVQLSESRRELQE-----LKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1379-1761 |
5.45e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1379 ARRNLEKQLQMvQSQMFETKKKLEEdlgSMEGLEEVKRKLQKDVEltsqclEEKTMAMDkMEKTKNRLQQelddLMVDLD 1458
Cdd:PRK04863 281 RRVHLEEALEL-RRELYTSRRQLAA---EQYRLVEMARELAELNE------AESDLEQD-YQAASDHLNL----VQTALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1459 HQRQI---VSNLEKKQKKfdqlLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEME 1535
Cdd:PRK04863 346 QQEKIeryQADLEELEER----LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1536 DLMSSKDDVGKNVHELEKskrtLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFDRDLQARDEQGEEKKRLL 1615
Cdd:PRK04863 422 ALERAKQLCGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIAGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1616 VKQV-REMeaeLEDERKQRTLAvASKKKLEMDLNELEGQIE---AANKGRDEAVKQLRK---LQAQMKDYQRELEEARAS 1688
Cdd:PRK04863 494 AWDVaREL---LRRLREQRHLA-EQLQQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKnldDEDELEQLQEELEARLES 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1689 RDEIFTQSKEN----EKKLKGLEAEILQL----QEDHAASERARRHAEQERDELADE------ISNSASGKSSLLEEKRR 1754
Cdd:PRK04863 570 LSESVSEARERrmalRQQLEQLQARIQRLaaraPAWLAAQDALARLREQSGEEFEDSqdvteyMQQLLERERELTVERDE 649
|
....*..
gi 1604804596 1755 LEARIAQ 1761
Cdd:PRK04863 650 LAARKQA 656
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1648-1951 |
7.02e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1648 NELEGQIEAANKGRDeavkqlrkLQAQMKDYQRELEEARASRDEIFTQSKENE---KKLKGLEAEILQLQEDHAASERAr 1724
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1725 rhaeqerdelADEISNSASGKSSLleekRRLEARIAQLEEELEEEQGNmelLNDrfrkSNIQVDNLNTelAGERSAAQKS 1804
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQND---LAE----YNSQLVSLQT--QPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1805 ENAR--QQMERQNKDLKAKLAELEGTVKSKFKASIAALEAKIL----------QLEDqLEQEAKERAAANkiVRRTEKKL 1872
Cdd:PRK11281 167 ANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDlqrkslegntQLQD-LLQKQRDYLTAR--IQRLEHQL 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1873 KEVMMQVEDERRhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANatrRKLQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:PRK11281 244 QLLQEAINSKRL--TLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLDR 317
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
905-1286 |
7.47e-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: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 905 QLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEE 984
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 985 AARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLgkvknkqEMMMVDLEERL 1064
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1065 KKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfqltKKEEELQAALarsdeetlqknnalKQVRELQAHLAEL 1144
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEALL--------------EELRSLQERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1145 QEdlesekmcrsKAEKLKRDLSE---------------ELEALKTELEdTLDTTAAQQELRSKREQEVAELKKAIDEETK 1209
Cdd:pfam07888 250 ER----------KVEGLGEELSSmaaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1210 NHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHkrkkLEAQLQEFM 1286
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQ----LQAEKQELL 391
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1025-1180 |
8.19e-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: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1025 LEDRISEMTSQLTEEEEKAKnlGKVKNKQEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQDQIVELQAQIEELKF 1104
Cdd:COG2433 378 IEEALEELIEKELPEEEPEA--EREKEHEERELTEEEEEIRRLEEQVERLE-------AEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 1105 QLTKKEEELQAALARSDEetlqknnalkqVRELQAHLAELQEDLESEkmcRSKAEKLKRDLSEELEALKTELEDTL 1180
Cdd:COG2433 449 ELSEARSEERREIRKDRE-----------ISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
898-1323 |
8.99e-06 |
|
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: 50.46 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 898 EMERKHQQLIEEKNILAEQLHAETELFAEAEEM--------RVRLLSRKQ--ELEEILHDLESRVEEEEERNQSLQNEKK 967
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGddsgtpggKKYLLLQKQleQLQEENFRLETARDDYRIKCEELEKEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 968 KMQSHIQdleeqldeeeaarqklQLDKVTAEAKIKKMEEDILLLEDQNSKFLKE-----KKLLEDrISEMTSQLTEEEEk 1042
Cdd:pfam05622 98 ELQHRNE----------------ELTSLAEEAQALKDEMDILRESSDKVKKLEAtvetyKKKLED-LGDLRRQVKLLEE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1043 aKNLGKVKNKqemmmVDLEERLKKEEKTRQELEKAKRKLdaetTDLQDQIVELQAQIEELKFQLTKKEEELqAALARSDE 1122
Cdd:pfam05622 160 -RNAEYMQRT-----LQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKL-EALQKEKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1123 ETLQKNNALKQVRElQAHLAELQED-LESEKMCRSKAEKLKRDLSEELeaLKTELEDTLdttaaqqeLRSKREQEVAELK 1201
Cdd:pfam05622 229 RLIIERDTLRETNE-ELRCAQLQQAeLSQADALLSPSSDPGDNLAAEI--MPAEIREKL--------IRLQHENKMLRLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1202 KAIDEETKnheaqiqemrqrqataLEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTE-------SEHK 1274
Cdd:pfam05622 298 QEGSYRER----------------LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEqgskaedSSLL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1604804596 1275 RKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKK 1323
Cdd:pfam05622 362 KQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRK 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1528-1744 |
1.03e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1528 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ 1607
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1608 GEEKKRL-----------LVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMK 1676
Cdd:COG3883 99 GGSVSYLdvllgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 1677 DYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASG 1744
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
867-1346 |
1.10e-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: 50.51 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 867 QVTRQEEELQAKDEELVKVKERqlkveneLVEMERKHQQLieekNILAEQLHAETELFAEAEEmRVRLLSRKQELEE--- 943
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEA----EQLRQNLEKQQSSLAEAEQ-RIKELEFEIQSQEqds 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 944 -ILHDLESRVeeeeERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQlDKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1022
Cdd:pfam05557 187 eIVKNSKSEL----ARIPELEKELERLREHNKHLNENIENKLLLKEEVE-DLKRKLEREEKYREEAATLELEKEKLEQEL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1023 KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMM---VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQI 1099
Cdd:pfam05557 262 QSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKeenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EEL---KFQLTKKEEELQAALARSDEETLQKN---NALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALK 1173
Cdd:pfam05557 342 RRLqrrVLLLTKERDGYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1174 TELedTLDTTAAQQELRSKREQEVAELKKAIDEetknHEAQIQEMRQRQatalEELSEQLEqakrfksnleknKQSLEND 1253
Cdd:pfam05557 422 REL--QALRQQESLADPSYSKEEVDSLRRKLET----LELERQRLREQK----NELEMELE------------RRCLQGD 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1254 NKELSCDVKTLQQAKT-ESEHKRKKLEAQLQEfmaratEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVD 1332
Cdd:pfam05557 480 YDPKKTKVLHLSMNPAaEAYQQRKNQLEKLQA------EIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
490
....*....|....
gi 1604804596 1333 KLNSKLQDSEELRQ 1346
Cdd:pfam05557 554 SAELKNQRLKEVFQ 567
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
949-1139 |
1.12e-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: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 949 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDIlllEDQNSKFLKEKKLLEDR 1028
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1029 ISEM---------TSQLTEEE------EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIV 1093
Cdd:COG3883 92 ARALyrsggsvsyLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1604804596 1094 ELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQA 1139
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1321-1946 |
1.22e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1321 EKKGLKLAKEVDKLNSKLQDSEELRQEETRQKL---NLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQM--- 1394
Cdd:PRK01156 165 ERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLeleNIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALnel 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1395 ---FETKKKLEEDLGSMEGleEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMvDLDHQRQIVSNLEKKQ 1471
Cdd:PRK01156 245 sslEDMKNRYESEIKTAES--DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1472 KKFDQL---LAEEKTISAQYAEERDRAEaearEKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNV 1548
Cdd:PRK01156 322 NKYHAIikkLSVLQKDYNDYIKKKSRYD----DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1549 HELEKSKRTLEQQVEEMRTQLEELEDE---LQATEDA----KLRLEVNMQAMKAQFDRDLQARDeQGEEKKRLLVKQVRE 1621
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKvssLNQRIRAlrenLDELSRNMEMLNGQSVCPVCGTT-LGEEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1622 meaelederkqrtlavaSKKKLEMDLNELEGQIEAAnkgrDEAVKQLRKLQAQMKdyQRELEEARASrdeiftqskenEK 1701
Cdd:PRK01156 477 -----------------KKSRLEEKIREIEIEVKDI----DEKIVDLKKRKEYLE--SEEINKSINE-----------YN 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1702 KLKGLEAEIlqlqEDHAASERARRHAEQERDELADEIsnsasgKSSLLEEkrrLEARiaqleeeleeeqgNMELLNDRFR 1781
Cdd:PRK01156 523 KIESARADL----EDIKIKINELKDKHDKYEEIKNRY------KSLKLED---LDSK-------------RTSWLNALAV 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1782 KSNIQVDNLNTElagersaaqksenaRQQMERQNKDLKAKLAELEGT---VKSKFKASIAALEAKILQLEDQLeQEAKER 1858
Cdd:PRK01156 577 ISLIDIETNRSR--------------SNEIKKQLNDLESRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NEIQEN 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1859 AAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGL 1938
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
....*...
gi 1604804596 1939 TREVSSLK 1946
Cdd:PRK01156 722 NETLESMK 729
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
996-1201 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 996 TAEAKIK--KMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEErLKKEEKTRQE 1073
Cdd:COG3206 193 EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1074 LEKAKRKLDAETTDLQD---QIVELQAQIEELKFQLtKKEEELQAALARSDEETLQknnalKQVRELQAHLAELQEDLES 1150
Cdd:COG3206 272 LAELEAELAELSARYTPnhpDVIALRAQIAALRAQL-QQEAQRILASLEAELEALQ-----AREASLQAQLAQLEARLAE 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1151 EKMCRSKAEKLKRDlseeLEALKTELEDTLdttAAQQELRSKREQEVAELK 1201
Cdd:COG3206 346 LPELEAELRRLERE----VEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
678-702 |
1.30e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.30e-05
10 20
....*....|....*....|....*
gi 1604804596 678 YKESLTKLMATLRNTNPNFVRCIIP 702
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
908-1123 |
1.43e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 908 EEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDE--EEA 985
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 986 ARQKLQLDKVTAEA-KIKKMEEDILLLEDQN-SKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEER 1063
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1064 LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfqltKKEEELQAALARSDEE 1123
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAE 235
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1550-1828 |
1.53e-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: 50.12 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1550 ELEKSKRTLEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARdeQGEEKKRLL-----------V 1616
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELerirqeeiameI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1617 KQVREME--------------AELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQREL 1682
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1683 EEARASRDEIFTQsKENEKKLKGLEAEILQlQEDHAASERARRHAEQERDEladeisnsasGKSSLLEEKRR---LEARI 1759
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEK-RDRKRAEEQRRKILEKELEE----------RKQAMIEEERKrklLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1760 AQLEEELEEEQGNMELLNDRFRKSNI----QVDNLNTELAGERSAAQKSENARQQMeRQNKDLKAKLAELEGT 1828
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
940-1430 |
1.62e-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: 50.44 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 940 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaarQKLQLDKVTAEA-------KIKKMEEDILLLE 1012
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---------QINDLEDVADKAisnddpeEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1013 DQNSKFLKEKKLLEDRISEMTSQLTE-EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD------AET 1085
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIEKDKTSlEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDeikeksPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1086 TDLQDQIVELQAQIEEL--------KFQLTKK-----------------------------EEELQAALARSDEET---- 1124
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMETFnishdddkDHHIISKkhdenisdirekslkiiedfseesdindiKKELQKNLLDAQKHNsdin 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1125 ------------LQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEE--LEALKTELEDTLD--------- 1181
Cdd:TIGR01612 1343 lylneianiyniLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDinLEECKSKIESTLDdkdidecik 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1182 -TTAAQQELRSKREQEVAELKKAID------------EETKNHEAQIQEMRQRQATA-----LEELSEQLEQAKRFKSNL 1243
Cdd:TIGR01612 1423 kIKELKNHILSEESNIDTYFKNADEnnenvlllfkniEMADNKSQHILKIKKDNATNdhdfnINELKEHIDKSKGCKDEA 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1244 EKNKQSLEND---------------NKELSCDVKT-LQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQ 1307
Cdd:TIGR01612 1503 DKNAKAIEKNkelfeqykkdvtellNKYSALAIKNkFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIE 1582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1308 TELDN----------ACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLS-TQIRQLEVDRNTLLEQQEEE 1376
Cdd:TIGR01612 1583 DDAAKndksnkaaidIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQdTELKENGDNLNSLQEFLESL 1662
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1377 EEARRNLE---KQLQMVQSQMFETKKKLEE-----DLGSMEGLEEVKRKLQKDVELTSQCLE 1430
Cdd:TIGR01612 1663 KDQKKNIEdkkKELDELDSEIEKIEIDVDQhkknyEIGIIEKIKEIAIANKEEIESIKELIE 1724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
873-1105 |
1.83e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 873 EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEAEEMRVRLLSRKQELEEILHDLESRV 952
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 953 EEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLdkvtAEAKIKKMEEDillLEDQNSKFLKEK-KLLEDRISE 1031
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEELRKE---LEELEKKYSEEEyEELREEYLE 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1032 MTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLdAETTDLQDQIVELQAQIEELKFQ 1105
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL-ERVEELREKVKKYKALLKERALS 743
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
989-1716 |
2.04e-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: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 989 KLQLDKVTAeaKIKKMEEDILLLEDQNSKFLKEKklLEDRISEMTSQLTEE--EEKAKNLGKVKNKQEmmmvDLEERLKK 1066
Cdd:TIGR01612 702 KSKIDKEYD--KIQNMETATVELHLSNIENKKNE--LLDIIVEIKKHIHGEinKDLNKILEDFKNKEK----ELSNKIND 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1067 EEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfQLTKKEEELQAALARSDEETLQKNNALKQVRElqAHLAELQE 1146
Cdd:TIGR01612 774 YAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAK-QNYDKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1147 DLESEKMCRSKAEKLKRDLSEELEALKTELEDtldttaaqqELRSKREQEVAELKKAIDEETKNHEAQIQEMrqrqaTAL 1226
Cdd:TIGR01612 851 FINFENNCKEKIDSEHEQFAELTNKIKAEISD---------DKLNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTL 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1227 EELSEQLEQAKRFKSNLEK--NKQSLENDnkELSCDVKTLQQAKTESEHKRKKLEAQLQEfmarateaertkgelaersh 1304
Cdd:TIGR01612 917 KKVDEYIKICENTKESIEKfhNKQNILKE--ILNKNIDTIKESNLIEKSYKDKFDNTLID-------------------- 974
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1305 kLQTELDNACTMLEvaekkglklakevdkLNSKLQDSEELRQEETRQKLNLSTQirqlevDRNTLLEQQEEEEEARRNLE 1384
Cdd:TIGR01612 975 -KINELDKAFKDAS---------------LNDYEAKNNELIKYFNDLKANLGKN------KENMLYHQFDEKEKATNDIE 1032
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1385 KQLQMVQSQMFETKKKLEEDLGSMegLEEVKRKLQKDVE-LTSQCLEEKTMAMDKMEKTKNRLqqelddlmvdldhqrqi 1463
Cdd:TIGR01612 1033 QKIEDANKNIPNIEIAIHTSIYNI--IDEIEKEIGKNIElLNKEILEEAEINITNFNEIKEKL----------------- 1093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1464 vsnlekKQKKFDQLLAEEktiSAQYAEERDRAEAEAREKDTKalsmaraleealeakeelerfnkqlraemedlmsskdd 1543
Cdd:TIGR01612 1094 ------KHYNFDDFGKEE---NIKYADEINKIKDDIKNLDQK-------------------------------------- 1126
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1544 VGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQARDEQGEekkrlLVKQVR 1620
Cdd:TIGR01612 1127 IDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIA 1200
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1621 EMEAELEDERKQRTLAVA---------------SKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMkDYQRELEEA 1685
Cdd:TIGR01612 1201 EIEKDKTSLEEVKGINLSygknlgklflekideEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETF 1279
|
730 740 750
....*....|....*....|....*....|....
gi 1604804596 1686 RASRDEI---FTQSKENEKKLKGLEAEILQLQED 1716
Cdd:TIGR01612 1280 NISHDDDkdhHIISKKHDENISDIREKSLKIIED 1313
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1088-1757 |
2.62e-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: 49.44 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1088 LQDQIVELQAQIEELKFQLTKKEEELQAALAR-----SDEetLQKNNALKqvRELQAHLAELQEDLesekmcrskaeklk 1162
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSiktfwSPE--LKKERALR--KEEAARISVLKEQY-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1163 RDLSEELEALKTELEDTLDTTAAQQELRSKREQEV------AELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQa 1236
Cdd:pfam10174 63 RVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1237 krFKSNLEKNKQSLENDNKELSCDVKTLQ-----QAKTESEHKRKK----LEAQLQEFMARATEAERTKGELAERSHK-- 1305
Cdd:pfam10174 142 --MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREELHRrn 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1306 -----------LQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEEtrqklnlstqIRQLEVDRN------- 1367
Cdd:pfam10174 220 qlqpdpaktkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEE----------IKQMEVYKShskfmkn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1368 ---TLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKN 1444
Cdd:pfam10174 290 kidQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1445 RLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAK 1520
Cdd:pfam10174 370 DLTEEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1521 EELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ------ATEDAKLR-LEVNMQAM 1593
Cdd:pfam10174 450 RIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1594 KAQFDRdLQARD------EQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKL-------EMDLNELEGQIEAANKG 1660
Cdd:pfam10174 530 KEECSK-LENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLlgilrevENEKNDKDKKIAELESL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1661 RDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKlkglEAEILQLQEDHAASERARrhaeQERDELADEISn 1740
Cdd:pfam10174 609 TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTR----QELDATKARLS- 679
|
730
....*....|....*..
gi 1604804596 1741 saSGKSSLLEEKRRLEA 1757
Cdd:pfam10174 680 --STQQSLAEKDGHLTN 694
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1011-1863 |
3.05e-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: 49.28 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1011 LEDQNSKFLKEKKLledrISEMTSQLTEEEEKAKNLGKVKNKQEMmmvdLEERLKKEEKTRQELEKAKRKLDAETTDLQD 1090
Cdd:TIGR01612 885 LNDYEKKFNDSKSL----INEINKSIEEEYQNINTLKKVDEYIKI----CENTKESIEKFHNKQNILKEILNKNIDTIKE 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1091 QIVELQAQIEELKFQLTKKEEELQAA---LARSDEETlqKNNALKQ-VRELQAHLAELQEDL------ESEKMCRS---K 1157
Cdd:TIGR01612 957 SNLIEKSYKDKFDNTLIDKINELDKAfkdASLNDYEA--KNNELIKyFNDLKANLGKNKENMlyhqfdEKEKATNDieqK 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1158 AEKLKRDLSEELEALKTELEDTLDttaaqqelrskreqevaELKKAIDEETKNHEAQIQEMRQRQATALEELSEQL---- 1233
Cdd:TIGR01612 1035 IEDANKNIPNIEIAIHTSIYNIID-----------------EIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLkhyn 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1234 ------EQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQefmarateaertkgelaershKLQ 1307
Cdd:TIGR01612 1098 fddfgkEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIN---------------------DLE 1156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1308 TELDNACTMLEVAEkkglkLAKEVDKLNSKLqDSEELRQEETRQKLNlstQIRQLEVDRNTLLEQQEEEEEARRNLEKql 1387
Cdd:TIGR01612 1157 DVADKAISNDDPEE-----IEKKIENIVTKI-DKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGK-- 1225
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1388 qMVQSQMFETKKKLEEDLGSMEG----LEEVKRKLQK-DVELTSQCLEEKTMAMDKMEKTKNRlqqelDDLMVDLDHQRQ 1462
Cdd:TIGR01612 1226 -LFLEKIDEEKKKSEHMIKAMEAyiedLDEIKEKSPEiENEMGIEMDIKAEMETFNISHDDDK-----DHHIISKKHDEN 1299
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1463 IvSNLEKKQKKFDQLLAEEKTISAQYAE-ERDRAEAEAREKDTKalsmarALEEALEAKEELERFN--KQLRAEMEDLMS 1539
Cdd:TIGR01612 1300 I-SDIREKSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDIN------LYLNEIANIYNILKLNkiKKIIDEVKEYTK 1372
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1540 SKDDVGKNVH-ELEKSKrTLEQQVEEmRTQLEELEDELQATEDAK---------LRLEVNMQAMKAQFDRDLQARDEQGE 1609
Cdd:TIGR01612 1373 EIEENNKNIKdELDKSE-KLIKKIKD-DINLEECKSKIESTLDDKdidecikkiKELKNHILSEESNIDTYFKNADENNE 1450
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1610 EKKrLLVKQVremeaELEDERKQRTLAVA---SKKKLEMDLNELEGQIEAANKGRDEA---VKQLRKLQAQMKDYQRELE 1683
Cdd:TIGR01612 1451 NVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVT 1524
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1684 E------ARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEA 1757
Cdd:TIGR01612 1525 EllnkysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEN 1604
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1758 ------RIAQLEEELEEEQGNMELLNDRFrkSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgTVKS 1831
Cdd:TIGR01612 1605 fenkflKISDIKKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD-ELDS 1681
|
890 900 910
....*....|....*....|....*....|..
gi 1604804596 1832 KFKASIAALEAKILQLEDQLEQEAKERAAANK 1863
Cdd:TIGR01612 1682 EIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
823-1238 |
3.22e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 823 ARKAFAKKQQQLSALKVLQRNCAAYLK-----LRHWQWWRLFTKVKPLL-QVTRQEEELQAKDEELVKVKERQLKVENEL 896
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEkleklLQLLPLYQELEALEAELaELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 897 VEMERKHQQLIEEKNILAEQlhAETELFAEAEEMRVRLLSRKQELEEI---LHDLESRVEEEEERNQSLQNEKKKMQSHI 973
Cdd:COG4717 173 AELQEELEELLEQLSLATEE--ELQDLAEELEELQQRLAELEEELEEAqeeLEELEEELEQLENELEAAALEERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 974 QDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLedQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVknkq 1053
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL--LFLLLAREKASLGKEAEELQALPALEELEEEELEEL---- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1054 emmmvdLEERLKKEEKTRQELEKAKRKLdAETTDLQDQIVELQAQIEeLKFQLTKKEEELQAALARSDEETLQKNNALKQ 1133
Cdd:COG4717 325 ------LAALGLPPDLSPEELLELLDRI-EELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1134 VRELQAHLAELQEDLES------EKMCRSKAEKLK---RDLSEELEALKTELEDTLdttaaqqelrskreQEVAELKKAI 1204
Cdd:COG4717 397 YQELKEELEELEEQLEEllgeleELLEALDEEELEeelEELEEELEELEEELEELR--------------EELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....
gi 1604804596 1205 DEETKNHEaqIQEMRQRQATALEELSEQLEQAKR 1238
Cdd:COG4717 463 EQLEEDGE--LAELLQELEELKAELRELAEEWAA 494
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
866-1123 |
3.29e-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: 48.97 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 866 LQVTRQE------EELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETElfAEAEEMRVRLLSRKQ 939
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA--REMERVRLEEQERQQ 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 940 ELEEILHDLESRveeeeernqslqnekkkmqshiqdleeqldeeeaARQKLQLDKvtaeakikkMEEDILLLEDQNskfl 1019
Cdd:pfam17380 461 QVERLRQQEEER----------------------------------KRKKLELEK---------EKRDRKRAEEQR---- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 keKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaettDLQDQIveLQAQI 1099
Cdd:pfam17380 494 --RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM--RKATE 563
|
250 260
....*....|....*....|....
gi 1604804596 1100 EELKFQLTKKEEELQAALARSDEE 1123
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVESEKA 587
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1041-1152 |
3.96e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1041 EKAK-NLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLtkkEEELQAALA- 1118
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKe 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1604804596 1119 ------------RSDEETLQKNNALKQVRELQAHLAELQEDLESEK 1152
Cdd:PRK00409 582 akkeadeiikelRQLQKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
883-1904 |
4.06e-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: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 883 VKVKERQLKVENELVEMERKHQQLIEEKNILAEQLhAETELFAEAEEMRVR---LLSRKQELEEILHD--------LESR 951
Cdd:TIGR01612 605 LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQVPEHLKNKdkiYSTIKSELSKIYEDdidalyneLSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 952 VEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarqklqlDKVTaeAKIKKMEEDILLLEDQNSKFLKEKklLEDRISE 1031
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKI-------------------DKEY--DKIQNMETATVELHLSNIENKKNE--LLDIIVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1032 MTSQLTEE--EEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfQLTKK 1109
Cdd:TIGR01612 741 IKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAK-QNYDK 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1110 EEELQAALARSDEETLQKNNALKQVRElqAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDtldttaaqqEL 1189
Cdd:TIGR01612 816 SKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD---------DK 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1190 RSKREQEVAELKKAIDEETKNHEAQIQEMrqrqaTALEELSEQLEQAKRFKSNLEK--NKQSLENDnkELSCDVKTLQQA 1267
Cdd:TIGR01612 885 LNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTLKKVDEYIKICENTKESIEKfhNKQNILKE--ILNKNIDTIKES 957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1268 KTESEHKRKKLEAQLQEfmaRATEAERTKGELAERSHKLQ-TELDNACTMLE--VAEKKGLKLAKEVDK----LNSKLQD 1340
Cdd:TIGR01612 958 NLIEKSYKDKFDNTLID---KINELDKAFKDASLNDYEAKnNELIKYFNDLKanLGKNKENMLYHQFDEkekaTNDIEQK 1034
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1341 SEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEeaRRNLEKQLQMVQSQMFETKKKLE----EDLGSMEGLEEVKR 1416
Cdd:TIGR01612 1035 IEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELL--NKEILEEAEINITNFNEIKEKLKhynfDDFGKEENIKYADE 1112
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1417 --KLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLD-----------------HQRQIVSNLEKKQKKFDQL 1477
Cdd:TIGR01612 1113 inKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEdvadkaisnddpeeiekKIENIVTKIDKKKNIYDEI 1192
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1478 ----------------LAEEKTISAQYA------------EERDRAE--AEAREKDTKALSMARALEEALEAKEELErfn 1527
Cdd:TIGR01612 1193 kkllneiaeiekdktsLEEVKGINLSYGknlgklflekidEEKKKSEhmIKAMEAYIEDLDEIKEKSPEIENEMGIE--- 1269
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1528 KQLRAEMEDLMSSKDDV----------GKNVHEL-EKSKRTLEQQVEEmrTQLEELEDELQA--TEDAKLRLEVNMQAMK 1594
Cdd:TIGR01612 1270 MDIKAEMETFNISHDDDkdhhiiskkhDENISDIrEKSLKIIEDFSEE--SDINDIKKELQKnlLDAQKHNSDINLYLNE 1347
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1595 AQFDRDLQARDeqgeeKKRLLVKQVREMEAELEDERKQRTLAVASKKKL------EMDLNELEGQIEAANKGRD--EAVK 1666
Cdd:TIGR01612 1348 IANIYNILKLN-----KIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLikkikdDINLEECKSKIESTLDDKDidECIK 1422
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1667 QLRKLQAQMkdyqreLEEaRASRDEIFTQSKENEKKL----KGLE------AEILQLQEDHAASERARRHAE-QERDELA 1735
Cdd:TIGR01612 1423 KIKELKNHI------LSE-ESNIDTYFKNADENNENVlllfKNIEmadnksQHILKIKKDNATNDHDFNINElKEHIDKS 1495
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1736 DEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLN--DRFRKSNIQVDNLNTELAGERS-AAQKSENARQQME 1812
Cdd:TIGR01612 1496 KGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNkfAKTKKDSEIIIKEIKDAHKKFIlEAEKSEQKIKEIK 1575
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1813 RQNKDLKAKLAELEGTVKS--KFKASIAALEAKILQLED--------QLEQEAKERAAANKIVRRTEKKLKE-------- 1874
Cdd:TIGR01612 1576 KEKFRIEDDAAKNDKSNKAaiDIQLSLENFENKFLKISDikkkindcLKETESIEKKISSFSIDSQDTELKEngdnlnsl 1655
|
1130 1140 1150
....*....|....*....|....*....|..
gi 1604804596 1875 --VMMQVEDERRHADQYKEQMEKANSRMKQLK 1904
Cdd:TIGR01612 1656 qeFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1786-1933 |
4.37e-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: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1786 QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTvkskfkASIAALEAKILQLEDQLEQEAKERAAANKIV 1865
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1866 RRTEKKLKEVMMQVEDE-RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRK---LQRELDDATE 1933
Cdd:COG3206 294 IALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1486-1951 |
4.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1486 AQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEdlmsskddvgknvhELEKSKRTLEQQVEEM 1565
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1566 RTQLEELEDELQATEDAKLRLEVNMQamKAQFDRDLQARDEQGEEKKRLLvKQVREMEAELEDERKQRTlavaskKKLEM 1645
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELE-EELEELEAELAELQEELE------ELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1646 DLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARR 1725
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1726 HAEQERDE-----LADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSA 1800
Cdd:COG4717 266 GSLLSLILtiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1801 AQKSENARQQMERQNKDLkaKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVE 1880
Cdd:COG4717 346 IEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1881 DERRhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKL--QRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:COG4717 424 ALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAA 494
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1142-1453 |
4.46e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1142 AELQEDLESEKMCRSKAEKLKR--DLSEELEALKTELEDTLDTTAAQQelrsKREQEVAELKKAID---EETKNHEAQIQ 1216
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALNKqkLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQLAqapAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1217 EMRQRQATALEELSEQLEQAkRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEA---QLQEFMARATEAE 1293
Cdd:PRK11281 105 ALKDDNDEETRETLSTLSLR-QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAnsqRLQQIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1294 RTKGEL-AERSHKLQTELD--NACTMLEVAEKKGlklakevdklNSKLQDSEELRQEEtrqklnLSTQIRQLEVDRNTLl 1370
Cdd:PRK11281 184 VGGKALrPSQRVLLQAEQAllNAQNDLQRKSLEG----------NTQLQDLLQKQRDY------LTARIQRLEHQLQLL- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1371 eqqeEEEEARRNL---EKQLQMVQSQmfetkkkleEDLGSMEGLEEVKRKLQKDVELtSQCLEEKTMAMDKMEKTKNRLQ 1447
Cdd:PRK11281 247 ----QEAINSKRLtlsEKTVQEAQSQ---------DEAARIQANPLVAQELEINLQL-SQRLLKATEKLNTLTQQNLRVK 312
|
....*.
gi 1604804596 1448 QELDDL 1453
Cdd:PRK11281 313 NWLDRL 318
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1313-1536 |
4.59e-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: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1313 ACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQS 1392
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1393 QMFETKKKLEEDLGSmegLEEVKRKLQK-------DVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVS 1465
Cdd:COG4942 91 EIAELRAELEAQKEE---LAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1466 NLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMED 1536
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1211-1503 |
4.98e-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: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1211 HEAQIQEmRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKtlQQAKTESEHKRKKLEaqlqefmaRAT 1290
Cdd:pfam17380 280 HQKAVSE-RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQERMAME--------RER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1291 EAERTKGELAERshklqteldnactmlEVAEKKGLKLAKEVDKLNS--KLQDSEELRQEETRQKLNLSTQIRQLEVDRNT 1368
Cdd:pfam17380 349 ELERIRQEERKR---------------ELERIRQEEIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1369 LLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEedlgsMEGLEEVKRKLQKDVELTSQCLEE---KTMAMDKMEKTKNR 1445
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERARE-----MERVRLEEQERQQQVERLRQQEEErkrKKLELEKEKRDRKR 488
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1446 LQQELDDLM-VDLDHQRQIVSNLEKKQKKFDQLLAEEKTisAQYAEERDRAEAEAREKD 1503
Cdd:pfam17380 489 AEEQRRKILeKELEERKQAMIEEERKRKLLEKEMEERQK--AIYEEERRREAEEERRKQ 545
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1133-1723 |
5.29e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1133 QVRELQAHLAELQEDLES----EKMCRSKAEKLKRDLS--EELEALKTELEDTLDTTAAQQ-ELRSKREQEVAELKKaID 1205
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQqqraERLLAEFCKRLGKNLDdeDELEQLQEELEARLESLSESVsEARERRMALRQQLEQ-LQ 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1206 EETKNHEAQIQEMRQRQAtALEELSEQLEQAkrfksnlEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEF 1285
Cdd:PRK04863 593 ARIQRLAARAPAWLAAQD-ALARLREQSGEE-------FEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1286 MARAT-EAERTKGeLAER-SHKLQTELDNACTMLEVAEKKGL------------------KLAKE-------------VD 1332
Cdd:PRK04863 665 SQPGGsEDPRLNA-LAERfGGVLLSEIYDDVSLEDAPYFSALygparhaivvpdlsdaaeQLAGLedcpedlyliegdPD 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1333 KLNSKLQDSEELRQEETRQklnlsTQIRQLEVDRntLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLgsmegle 1412
Cdd:PRK04863 744 SFDDSVFSVEELEKAVVVK-----IADRQWRYSR--FPEVPLFGRAAREKRIEQLRAEREELAERYATLSFDV------- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1413 evkRKLQKDVELTSQCL---------EEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKT 1483
Cdd:PRK04863 810 ---QKLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1484 IsaqyAEER--DRAEaEAREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLmsskDDVGKNVHELEKSKRTLEQQ 1561
Cdd:PRK04863 887 L----ADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF----EQLKQDYQQAQQTQRDAKQQ 957
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1562 ------VEEMRTQL------EELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDEQGEEKKRLLVK------QVREME 1623
Cdd:PRK04863 958 afalteVVQRRAHFsyedaaEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQLAQYNQVLASlkssydAKRQML 1036
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1624 AELEDERKQRTL---------AVASKKKLEMDLNELEGQIEAANKGR-------DEAVKQLRKLQAQMKDYQRELEEARA 1687
Cdd:PRK04863 1037 QELKQELQDLGVpadsgaeerARARRDELHARLSANRSRRNQLEKQLtfceaemDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
650 660 670
....*....|....*....|....*....|....*...
gi 1604804596 1688 SRDEIFTQSKEN--EKKLKGLEAEILQLQEDHAASERA 1723
Cdd:PRK04863 1117 GWCAVLRLVKDNgvERRLHRRELAYLSADELRSMSDKA 1154
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1606-1760 |
5.71e-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: 46.60 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1606 EQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIE--------AANKGRD----EAVKQLRKLQA 1673
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaALTKGNEelarEALAEKKSLEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1674 QMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEdHAASERARRHAEQERDELadeisnSASGKSSLLEekr 1753
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKA-RLKAAKAQEAVQTSLGSL------STSSATDSFE--- 167
|
....*..
gi 1604804596 1754 RLEARIA 1760
Cdd:pfam04012 168 RIEEKIE 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
980-1123 |
7.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 980 LDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKaknLGKVKNKQEMMmvD 1059
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEYE--A 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1060 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEE 1123
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
918-1139 |
8.76e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 918 HAETELFAEAEEMRvRLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLDKVTA 997
Cdd:COG3883 13 FADPQIQAKQKELS-ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 998 EAKIKKMEE-------------------DILLLEDQNSKFLKEKKLLeDRISEMTSQLTEEEEKAKNlgKVKNKQEmmmv 1058
Cdd:COG3883 78 EAEIEERREelgeraralyrsggsvsylDVLLGSESFSDFLDRLSAL-SKIADADADLLEELKADKA--ELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1059 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQ 1138
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
.
gi 1604804596 1139 A 1139
Cdd:COG3883 231 A 231
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1059-1302 |
9.18e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.84 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1059 DLEERLK-KEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKnnalkqvREL 1137
Cdd:pfam00038 29 LLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1138 QAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALKTEledtldttaaqqelrskREQEVAELKKAIDEETKNHE---AQ 1214
Cdd:pfam00038 102 ENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVEmdaAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1215 IQEMrqrqATALEELSEQLE-QAKRFKSNLEKNKQS-LENDNKELSCDVKTLQQAKTE-SEHKR--KKLEAQLQEFMARA 1289
Cdd:pfam00038 165 KLDL----TSALAEIRAQYEeIAAKNREEAEEWYQSkLEELQQAAARNGDALRSAKEEiTELRRtiQSLEIELQSLKKQK 240
|
250
....*....|...
gi 1604804596 1290 TEAERTKGELAER 1302
Cdd:pfam00038 241 ASLERQLAETEER 253
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1663-1877 |
1.01e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1663 EAVKQLRKLQAQMKDYQRELEEARASRDEIftqskeNEKKLKglEAEILQLQEdhaasERAR-RHAEQERDELA---DEI 1738
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEEL------EAAALQ--PGEEEELEE-----ERRRlSNAEKLREALQealEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1739 SNSASGKSSLLEE-KRRLEaRIAQleeeleeEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQME-RQN- 1815
Cdd:COG0497 236 SGGEGGALDLLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEeRLAl 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1816 -------------------KDLKAKLAELEGtvkskFKASIAALEAKILQLEDQLEQEAKE-----RAAANKIVRRTEKK 1871
Cdd:COG0497 308 lrrlarkygvtveellayaEELRAELAELEN-----SDERLEELEAELAEAEAELLEAAEKlsaarKKAAKKLEKAVTAE 382
|
....*.
gi 1604804596 1872 LKEVMM 1877
Cdd:COG0497 383 LADLGM 388
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
870-1258 |
1.09e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 870 RQEEELQAKDEELVKVKERQLKVENELVEMERKHQQL------IEEKNILAEQLHAETE-LFAEAEEMRVRLLSRKQELE 942
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksIESLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 943 EILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDillledqnskFLKEK 1022
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINH----------YNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1023 KLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVD-LEERLKKEEKTRQELEKAKRKLdAETTDLQDQIVELQAQIEE 1101
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKS 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1102 LKFQL--TKKEEELQAALARS--DEETLQK--NNALKQVRELQAHLAELQEDLESEKmcrSKAEKLKRDLSEELEALKTE 1175
Cdd:PRK01156 558 LKLEDldSKRTSWLNALAVISliDIETNRSrsNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1176 LEDTLDTTAAQQELRSKRE---QEVAElKKAIDEETKNHEAQIQEMRQRqataLEELSEQLEQAKRFKSNLEKNKQSLEN 1252
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDnykKQIAE-IDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRARLESTIEILRT 709
|
....*.
gi 1604804596 1253 DNKELS 1258
Cdd:PRK01156 710 RINELS 715
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1099-1244 |
1.10e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1099 IEELKFQLTKKEEELqaalarsdEETLQKNNALKqvRELQAHLAELQEDLEsekmcrsKAEKLKRDLSEELEALKTELED 1178
Cdd:PRK00409 504 IEEAKKLIGEDKEKL--------NELIASLEELE--RELEQKAEEAEALLK-------EAEKLKEELEEKKEKLQEEEDK 566
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 1179 TLdttaaqQELRSKREQEVAELKKAIDE------------ETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLE 1244
Cdd:PRK00409 567 LL------EEAEKEAQQAIKEAKKEADEiikelrqlqkggYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
872-1206 |
1.23e-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: 47.16 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 872 EEELQAKDEELVKVkerqLKVENELVEMERKHQQLIEE-KNILAE---QLHAETELFAEAEEmrvrllsrkqELEEILHD 947
Cdd:pfam06160 92 EELLDDIEEDIKQI----LEELDELLESEEKNREEVEElKDKYRElrkTLLANRFSYGPAID----------ELEKQLAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 948 LESRVEEEEERNQSLQNEK-----KKMQSHIQDLEEQLDEEEAARQKL------QLDKVtaEAKIKKMEEDILLLEDQNs 1016
Cdd:pfam06160 158 IEEEFSQFEELTESGDYLEarevlEKLEEETDALEELMEDIPPLYEELktelpdQLEEL--KEGYREMEEEGYALEHLN- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1017 kFLKEKKLLEDRISEMTSQL--TEEEEKAKNLGKVKNKQEMMMVDLEerlkKEEKTRQELEKAKRKLDAETTDLQDQIVE 1094
Cdd:pfam06160 235 -VDKEIQQLEEQLEENLALLenLELDEAEEALEEIEERIDQLYDLLE----KEVDAKKYVEKNLPEIEDYLEHAEEQNKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1095 LQAQIEELK--FQLTKKEEELQAALArsdeetlqknnalKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEAL 1172
Cdd:pfam06160 310 LKEELERVQqsYTLNENELERVRGLE-------------KQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEI 376
|
330 340 350
....*....|....*....|....*....|....
gi 1604804596 1173 KTELEDTLDTTAAQQELRSKREQEVAELKKAIDE 1206
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDELEAREKLDEFKLELRE 410
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1321-1904 |
1.30e-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: 47.04 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1321 EKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEvdrntlleqqEEEEEARRNLEKQLQMVQSQ---MFET 1397
Cdd:pfam05557 19 KQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLE----------KREAEAEEALREQAELNRLKkkyLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1398 KKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL 1477
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1478 LAEEKTISAQYAEERDRAEaEAREKDTKALSMARALEEAleakeelerfnKQLRAEMEDLMSSKDDVGKNVHELEKSKRT 1557
Cdd:pfam05557 169 EQRIKELEFEIQSQEQDSE-IVKNSKSELARIPELEKEL-----------ERLREHNKHLNENIENKLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1558 LEQQvEEMRTQLEELEDELQATEdAKLRLEVNMQAMKAQFDR---DLQARDEQGEEKKRLLVKQVREMEAELEDERKQRT 1634
Cdd:pfam05557 237 LERE-EKYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1635 LavaskkkLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARA---SRDEIFTQSKENEKKLKGLEAEIL 1711
Cdd:pfam05557 315 E-------LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1712 QLQEDHAASERARRHAEQERDELadeisnsASGKSSLLEEKRRLEARIAQleeeleeeqgnmELLNDRfRKSNIQVDNLN 1791
Cdd:pfam05557 388 MTQKMQAHNEEMEAQLSVAEEEL-------GGYKQQAQTLERELQALRQQ------------ESLADP-SYSKEEVDSLR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1792 TELagersaaQKSENARQQMERQNKDLKAKLA--ELEGTVK-SKFK----ASIAALEAKiLQLEDQLEQEAKERAAANKI 1864
Cdd:pfam05557 448 RKL-------ETLELERQRLREQKNELEMELErrCLQGDYDpKKTKvlhlSMNPAAEAY-QQRKNQLEKLQAEIERLKRL 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1604804596 1865 VRRTEKKLKEV----MMQVEDERRHADQYKEQMEKANSRMKQLK 1904
Cdd:pfam05557 520 LKKLEDDLEQVlrlpETTSTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1326-1946 |
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 1604804596 1326 KLAKEVDKLNS-KLQDSEELRQEETRQKLNlstqirqlevdrntlleqqeeeeeaRRNLEKQLQMVQSQMFETKKKleeD 1404
Cdd:pfam05483 82 KLYKEAEKIKKwKVSIEAELKQKENKLQEN-------------------------RKIIEAQRKAIQELQFENEKV---S 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1405 LGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRL--QQELDDLMVDLDHqrqivsNLEKKQKKFDQL--LAE 1480
Cdd:pfam05483 134 LKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEyeREETRQVYMDLNN------NIEKMILAFEELrvQAE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1481 EKTISAQYAEERDRAEAEAREKDTKALSMARALEEALEAKEELERFNKqlraeMEDLMSSKDDVGKNVHELEKSKRTLEQ 1560
Cdd:pfam05483 208 NARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK-----MKDLTFLLEESRDKANQLEEKTKLQDE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1561 QVEEMRTQLEELEDELqatEDAKLRLEVNMQAMKAqFDRDLQArdeqgeeKKRLLVKQVREMEAELEDERKQRTLAVASK 1640
Cdd:pfam05483 283 NLKELIEKKDHLTKEL---EDIKMSLQRSMSTQKA-LEEDLQI-------ATKTICQLTEEKEAQMEELNKAKAAHSFVV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1641 KKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEAR-----------------ASRDEIFTQSKENEK-- 1701
Cdd:pfam05483 352 TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeveleelkkilAEDEKLLDEKKQFEKia 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1702 -KLKGLEAEILQLQEDHaaserarrhaEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRF 1780
Cdd:pfam05483 432 eELKGKEQELIFLLQAR----------EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1781 RKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEG---TVKSKFKASIAALEAKILQLEDQLEQEAKE 1857
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDeleSVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1858 RAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQ----MEKANSRMKQLKRQLEEAEEEATRANATRRKL-------QR 1926
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalKKKGSAENKQLNAYEIKVNKLELELASAKQKFeeiidnyQK 661
|
650 660
....*....|....*....|
gi 1604804596 1927 ELDDATEASEGLTREVSSLK 1946
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAK 681
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
996-1234 |
1.69e-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: 46.67 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 996 TAEAKIKKMEEDILLLEDQNSKFLKEKKL-LEDRISEMTSQLTEEEEK--------------AKNLGKVKNKQEMMMVDL 1060
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEEEAAPPLLDaAPETPPKLPEHLDNVEEKvekaqslaklvdqyKELVASERIVFQQELVSI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1061 EERLKKEEKTRQELEKAKrkLDAETTDLQDQIVELQAQIEELKfqlTKKEEELQAALARSDEEtlQKNNALKQVRELQAH 1140
Cdd:pfam09731 267 FPDIIPVLKEDNLLSNDD--LNSLIAHAHREIDQLSKKLAELK---KREEKHIERALEKQKEE--LDKLAEELSARLEEV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1141 LA--ELQEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDEETKNHEAQIQEM 1218
Cdd:pfam09731 340 RAadEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNEL 418
|
250
....*....|....*.
gi 1604804596 1219 rqrqATALEELSEQLE 1234
Cdd:pfam09731 419 ----LANLKGLEKATS 430
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
861-1181 |
1.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 861 KVKPLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLH-AETELFAEAEEMRVRLLSRKQ 939
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 940 ELEEIlhdlesrveeeeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDqnskfL 1019
Cdd:PTZ00121 1676 KAEEA---------------KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE-----A 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 KEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEkTRQELEKAKRKLDAETTDLQDQIVELQAQI 1099
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-LDEEDEKRRMEVDKKIKDIFDNFANIIEGG 1814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1100 EELKFQLTKKEEELQAALarsDEETLQKNNALKQVRELQAHL----AELQEDLESEKMCRSKAEKLKRDLSEELEALKTE 1175
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAI---KEVADSKNMQLEEADAFEKHKfnknNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
....*.
gi 1604804596 1176 LEDTLD 1181
Cdd:PTZ00121 1892 KIDKDD 1897
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1940 |
1.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1528 KQLRAEMEDLMSSKDDVGK--NVHELEKSKRTLEQQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMKAQFDRDLQ 1602
Cdd:COG4717 105 EELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1603 ARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRD-EAVKQLRKLQAQMKDYQRE 1681
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1682 LEEARASRDEI-----------FTQSKENEKKLKGLEAEILQLQEDHAASERarrhAEQERDELADEISNSASGKSSLLE 1750
Cdd:COG4717 265 GGSLLSLILTIagvlflvlgllALLFLLLAREKASLGKEAEELQALPALEEL----EEEELEELLAALGLPPDLSPEELL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1751 EKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNkDLKAKLAELEGTVK 1830
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE-ELEEQLEELLGELE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1831 SKFKA-SIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLEE 1909
Cdd:COG4717 420 ELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
410 420 430
....*....|....*....|....*....|.
gi 1604804596 1910 AEEEATRANATRRKLQRELDDATEASEGLTR 1940
Cdd:COG4717 500 ELLEEAREEYREERLPPVLERASEYFSRLTD 530
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1471-1739 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1471 QKKFDQLLAEEKTISAQyaeERDRAEAEAREKDTKALSMARALEEALEAKEELERfnKQLRAEMEDLMSSKDDVGKNVHE 1550
Cdd:TIGR00606 172 KQKFDEIFSATRYIKAL---ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1551 LEKSKRTLeQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDER 1630
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1631 KQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLK--GLEA 1708
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVieRQED 405
|
250 260 270
....*....|....*....|....*....|.
gi 1604804596 1709 EILQLQEDHAASERARRHAEQERDELADEIS 1739
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1638-1842 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1638 ASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQ--SKENEKKLKGLEAEILQLQE 1715
Cdd:cd22656 114 EAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKEIKDLQKELEKLNE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1716 DHAASerarrhAEQERDELADEISNsasgksslLEEKRRLEARIaqleeeleeeQGNMELLNDrfrksniQVDNLNTELA 1795
Cdd:cd22656 194 EYAAK------LKAKIDELKALIAD--------DEAKLAAALRL----------IADLTAADT-------DLDNLLALIG 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1604804596 1796 GERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEA 1842
Cdd:cd22656 243 PAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1043-1289 |
2.23e-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: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1043 AKNLGKVKNKQEMMMVDLEERLKkEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQaalarsde 1122
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLA-DATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTE-------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1123 etlqknnalKQVRELQAHLAELQEDLESEkmcrskaekLKRDLSEELEALKTELEDtldttaAQQELRSKREQEVAELKK 1202
Cdd:cd22656 153 ---------KDQTALETLEKALKDLLTDE---------GGAIARKEIKDLQKELEK------LNEEYAAKLKAKIDELKA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1203 AI--DEETKNHEAQIQEMRQRQATALEELSEQLEQAKR-----------FKSNLEKNKQSLENDNKELSCDVKTLQQAKt 1269
Cdd:cd22656 209 LIadDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPaleklqgawqaIATDLDSLKDLLEDDISKIPAAILAKLELE- 287
|
250 260
....*....|....*....|
gi 1604804596 1270 ESEHKRKKLEAQLQEFMARA 1289
Cdd:cd22656 288 KAIEKWNELAEKADKFRQNA 307
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1024-1205 |
2.64e-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: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1024 LLEDRISEMTSQLTEEEEKAKNLGK-VKNKQEMMMVDLEERLKKE-----EKTRQELEKAKRKLDAETTDLQDQiveLQA 1097
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQeLVDRLEKETEALRERLQKDleevrAKLEPYLEELQAKLGQNVEELRQR---LEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1098 QIEELKFQLTKKEEELQAALARSDEETlqKNNALKQVRELQAHLAELQEDLesekmcRSKAEKLKRDLSEELEALKTELE 1177
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLAPYGEEL--RERLEQNVDALRARLAPYAEEL------RQKLAERLEELKESLAPYAEEVQ 149
|
170 180
....*....|....*....|....*...
gi 1604804596 1178 DTLDTTAaqQELRSKREQEVAELKKAID 1205
Cdd:pfam01442 150 AQLSQRL--QELREKLEPQAEDLREKLD 175
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1161-1331 |
3.53e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1161 LKRDLSEELEALKTELEDTLDttAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFK 1240
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1241 SNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMA-RATEA---------ERTKGELAERSHKLQTEl 1310
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEEAkeillekveEEARHEAAVLIKEIEEE- 181
|
170 180
....*....|....*....|.
gi 1604804596 1311 dnactmlevAEKKGLKLAKEV 1331
Cdd:PRK12704 182 ---------AKEEADKKAKEI 193
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1087-1707 |
3.70e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1087 DLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLS 1166
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1167 EELEALK--TELEDTLDTTAAQQELRSKRE-QEVAELKKAID---EETKNHEAQIQ--EMRQRQATALEELSEQLEQAKR 1238
Cdd:PRK01156 267 MELEKNNyyKELEERHMKIINDPVYKNRNYiNDYFKYKNDIEnkkQILSNIDAEINkyHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1239 FKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDnactmle 1318
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ------- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1319 vaekkglKLAKEVDKLNSKLqDSEELRQEETRQKLNLSTQIRQLEVDRNTLleqqeeeeearrnLEKQLQMVQSQMFETK 1398
Cdd:PRK01156 420 -------DISSKVSSLNQRI-RALRENLDELSRNMEMLNGQSVCPVCGTTL-------------GEEKSNHIINHYNEKK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1399 KKLEEDLGSMEglEEVKRKLQKDVELTSQcleEKTMAMDKMEKTKNRLQQeLDDLMVDLDHQRQIVSNLEKKQKKFDQLL 1478
Cdd:PRK01156 479 SRLEEKIREIE--IEVKDIDEKIVDLKKR---KEYLESEEINKSINEYNK-IESARADLEDIKIKINELKDKHDKYEEIK 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1479 AEEKTISAQYAEERdraeaeaREKDTKALSMARAleealeakeelerfnkqlrAEMEDLMSSKDDVGKNVHELEKSKRTL 1558
Cdd:PRK01156 553 NRYKSLKLEDLDSK-------RTSWLNALAVISL-------------------IDIETNRSRSNEIKKQLNDLESRLQEI 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1559 EQQVEEMRT----QLEELEDELQATEDAKLRLEVNMQAMkaqfdrdlqardeqgeEKKRLLVKQVREMEAELEDERKQRT 1634
Cdd:PRK01156 607 EIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILI----------------EKLRGKIDNYKKQIAEIDSIIPDLK 670
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1635 LAVASKKKLEMDLNELEGQIEAANKGRDEavkqLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLE 1707
Cdd:PRK01156 671 EITSRINDIEDNLKKSRKALDDAKANRAR----LESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLK 739
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1618-1808 |
3.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1618 QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSK 1697
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1698 ENEKKLKGLEA--------------------------EILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEE 1751
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1752 KRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENAR 1808
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
865-1323 |
3.86e-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: 45.60 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 865 LLQVTRQEEELQAKDEELVKVKERQLKVENEL-----------VEMERKHQQLIEEKNILAEqlhAETELFAEA------ 927
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAgtllhf 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 928 --------EEMRVRLLSRKQELEEILHdlESRVEEEEERNQSLQNEKKKMQS-HIQDLEEQLDEEEAARQKLQLDKVTAE 998
Cdd:pfam12128 540 lrkeapdwEQSIGKVISPELLHRTDLD--PEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 999 AKIKKMEEDILLLEDQnskflkekklLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVD----LEERLKKEEKTRQEL 1074
Cdd:pfam12128 618 EKQAAAEEQLVQANGE----------LEKASREETFARTALKNARLDLRRLFDEKQSEKDKknkaLAERKDSANERLNSL 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1075 EKAKRKLDaetTDLQDQIVELQAQIEELKFQLTKK----EEELQAALARSDEETLQKNNALKqvrelqAHLAELQEDLES 1150
Cdd:pfam12128 688 EAQLKQLD---KKHQAWLEEQKEQKREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKR 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1151 EKMCRSKAEKLKRDLSEELEALKTELEDTldttaaqqelrSKREQEVAELKKAIDE----ETKNHEAQIQEMRQRQATAL 1226
Cdd:pfam12128 759 DLASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQ 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1227 EELSEQLEQAKRFKSNLEKNKQSLENdnkelscdvktlQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKL 1306
Cdd:pfam12128 828 QQLARLIADTKLRRAKLEMERKASEK------------QQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQL 895
|
490
....*....|....*..
gi 1604804596 1307 QTELDNACTMLEVAEKK 1323
Cdd:pfam12128 896 EDLKLKRDYLSESVKKY 912
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1052 |
4.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 867 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAE----------AEEMRV---- 932
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrQPPLALllsp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 933 ----RLLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDI 1008
Cdd:COG4942 129 edflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1604804596 1009 LLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNK 1052
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1105-1367 |
4.55e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1105 QLTKKEEELQAALARSDEETlqknnalkqVRELQAHLAELQEDLESEKmcRSKA--------EKLKRDLSEELEALKTEL 1176
Cdd:PRK10929 27 QITQELEQAKAAKTPAQAEI---------VEALQSALNWLEERKGSLE--RAKQyqqvidnfPKLSAELRQQLNNERDEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1177 EdTLDTTAAQQELrskrEQEVAELKKAIDEETknHEAQIQEMRQRQ-ATALEELSEQLEQAKRFKSNLEKNKQSLENDNK 1255
Cdd:PRK10929 96 R-SVPPNMSTDAL----EQEILQVSSQLLEKS--RQAQQEQDRAREiSDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1256 ELSCDVKTLQQAKTeSEHKRKKLEAQLQEFMAR-ATEAERTKGELAERSHklqTELDnactmlevAEKKGLKlakevDKL 1334
Cdd:PRK10929 169 PLAQAQLTALQAES-AALKALVDELELAQLSANnRQELARLRSELAKKRS---QQLD--------AYLQALR-----NQL 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1604804596 1335 NSKLQDSEELRQEETR----QKLNLSTQI-RQLEVDRN 1367
Cdd:PRK10929 232 NSQRQREAERALESTEllaeQSGDLPKSIvAQFKINRE 269
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1039-1311 |
4.56e-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: 44.57 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1039 EEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKfqltkkeEELQAALA 1118
Cdd:pfam09311 15 QEQEAETRDQVKKLQEMLR-QANDQLEKTMKDKKELEDKMNQLSEETSNQVSTLAKRNQKSETLL-------DELQQAFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1119 RSDEETLQKNNALKQVRELQA-HLAELQEDLESEKMCRSKAEKLKR-------DLSEELEALKTEL-EDTLDTTAAQQEL 1189
Cdd:pfam09311 87 QAKRNFQDQLAVLMDSREQVSdELVRLQKDNESLQGKHSLHVSLQQaekfdmpDTVQELQELVLKYrEELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1190 RSKREQEVAELKKAIDEEtKNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKT 1269
Cdd:pfam09311 167 EEKLKAEILFLKEQIQAE-QCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQLEDLQTTKG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1604804596 1270 EsehkrkkLEAQLQEFMARATEAERTKGELAERSHKLQTELD 1311
Cdd:pfam09311 246 S-------LETQLKKETNEKAAVEQLVFEEKNKAQRLQTELD 280
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1681-1898 |
5.13e-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: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1681 ELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISnsasgksslleekrRLEARIA 1760
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1761 QLeeeleeeqgnMELLNDRFR---KSNIQVDNLN--------TELAGERSAAQKSENARQQMERQNKDLKAKLAELegtv 1829
Cdd:COG3883 83 ER----------REELGERARalyRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAK---- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604804596 1830 KSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANS 1898
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1598-1939 |
5.75e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1598 DRDLQARDEQGEEKKRLLVKQVR--EMEAELED-ERKQRTL----------------AVASKKKLEM---DLNELEGQIE 1655
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRlvEMARELEElSARESDLeqdyqaasdhlnlvqtALRQQEKIERyqeDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1656 AANKGRDEAVKQLRKLQAQmkdyqreLEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARR-------HAE 1728
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcglpdlTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1729 QERDELADEISNSASGKSSLLEEKRRLeaRIAQLEEeleeeqgnmellnDRFRKSNIQVdnlnTELAGERSAAQKSENAR 1808
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQKL--SVADAAR-------------RQFEKAYELV----CKIAGEVERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1809 QQMeRQNKDLKAKLAELEgtvkskfkasiaALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMmQVEDERRHADQ 1888
Cdd:COG3096 499 ELL-RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEELLAELEA 564
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1889 YKEQMEkansrmkqlkrqleeaeEEATRANATRRKLQRELDDATEASEGLT 1939
Cdd:COG3096 565 QLEELE-----------------EQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1285-1511 |
5.93e-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: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1285 FMARATEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIRQLEV 1364
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1365 DRNTLleqQEEEEEARRNLEKQLQMVQSQMFETKKKLeedLGSMEGLEEVKRKLQKDVELTSQCLEEktmaMDKMEKTKN 1444
Cdd:COG4942 91 EIAEL---RAELEAQKEELAELLRALYRLGRQPPLAL---LLSPEDFLDAVRRLQYLKYLAPARREQ----AEELRADLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1445 RLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAEAEAREKDTKALSMAR 1511
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
861-1261 |
5.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 861 KVKPLLQVTRQEEELQA---KDEELVKVKERQLKVENELVEMERKHQ----QLIEEKNILAEQLHAETELFAEAEEMRVR 933
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMalrKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 934 LLSRKQELEEILHDLESRVEEEEERNQSLQNEKKKMQshiqdleEQLDEEEAARQKLQLDKVTAEAKiKKMEEDILLLED 1013
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-------EAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAE 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1014 QNSKFLKEKKLLEDRISEMTSQLTEEEEKaknlgkvKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDqiv 1093
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEED-------KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--- 1783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1094 ELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQahLAELQEDLESEKMCRSKAEKLKRDLSEElEALK 1173
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME--DSAIKEVADSKNMQLEEADAFEKHKFNK-NNEN 1860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1174 TELEDTLDTTAAQQELRSKREQEVAELK--KAIDEETKNHEAQIQEMRQRQAtalEELSEQLEQAKRFKSNLEKNKQSLE 1251
Cdd:PTZ00121 1861 GEDGNKEADFNKEKDLKEDDEEEIEEADeiEKIDKDDIEREIPNNNMAGKNN---DIIDDKLDKDEYIKRDAEETREEII 1937
|
410
....*....|
gi 1604804596 1252 NDNKELSCDV 1261
Cdd:PTZ00121 1938 KISKKDMCIN 1947
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1064-1330 |
6.11e-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: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1064 LKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALArsDEETLQKNNAlkqvrELQAHLAE 1143
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVR--EKTSLSASVA-----SLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1144 LQE--DLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ-----------EVAELKKAIDEETKN 1210
Cdd:pfam15905 134 LTRvnELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQvtqknlehskgKVAQLEEKLVSTEKE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1211 HEAQIQEMrQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFmarAT 1290
Cdd:pfam15905 214 KIEEKSET-EKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL---ES 289
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1604804596 1291 EAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKE 1330
Cdd:pfam15905 290 EKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1421-1640 |
7.01e-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: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1421 DVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERDRAEAEA 1499
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1500 REKDT----KALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1575
Cdd:COG3883 97 RSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604804596 1576 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASK 1640
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1013-1803 |
7.17e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1013 DQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKqemMMVDLEERLKKeeKTRQELE--------------KAK 1078
Cdd:TIGR01612 486 DENSKQDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNI---IGFDIDQNIKA--KLYKEIEaglkesyelaknwkKLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1079 RKLDAETTDLQDQIVELQAQIEELKFQLTKKEEE------LQAALARSDEETLQKNNALKQVRELQ-------AHLAELQ 1145
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinkLKLELKEKIKNISDKNEYIKKAIDLKkiiennnAYIDELA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1146 --------EDLES-EKMCRSKAEKLKRDLSEELEALKTEL-----EDTLDTT---AAQQELRSKREQEVAELKKAIDEET 1208
Cdd:TIGR01612 641 kispyqvpEHLKNkDKIYSTIKSELSKIYEDDIDALYNELssivkENAIDNTedkAKLDDLKSKIDKEYDKIQNMETATV 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1209 KNHEAQIQEMRQRQATALEELSEQLEqaKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLeAQLQEFMAR 1288
Cdd:TIGR01612 721 ELHLSNIENKKNELLDIIVEIKKHIH--GEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKI-SEIKNHYND 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1289 ATEAERTKGELAERSHKLQTELDNACTMLE------VAEKKGLK--LAKEVDKLNSKLQDSEELRQEETRQKLNLSTQIR 1360
Cdd:TIGR01612 798 QINIDNIKDEDAKQNYDKSKEYIKTISIKEdeifkiINEMKFMKddFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIK 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1361 QlEVDRNTLleqqeeeeearRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLqKDVELTSQCLEEktmAMDKME 1440
Cdd:TIGR01612 878 A-EISDDKL-----------NDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEK---FHNKQN 941
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1441 KTKNRLQQELDDLmvdldhqrQIVSNLEKKQK-KFDQLLAEEKTISAQYAEERDRAEAEAREKD-TKALSMARALEEALE 1518
Cdd:TIGR01612 942 ILKEILNKNIDTI--------KESNLIEKSYKdKFDNTLIDKINELDKAFKDASLNDYEAKNNElIKYFNDLKANLGKNK 1013
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1519 AKEELERFNKQLRAeMEDLMSSKDDVGKNVHELEKSKRT------------LEQQVEEMRTQ-LEELE------------ 1573
Cdd:TIGR01612 1014 ENMLYHQFDEKEKA-TNDIEQKIEDANKNIPNIEIAIHTsiyniideiekeIGKNIELLNKEiLEEAEinitnfneikek 1092
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1574 ------DELQATEDAKLRLEVN-----MQAMKAQFDRDLQARdeqgEEKKRLLVKQVREMEAELEDERK--QRTLAVASK 1640
Cdd:TIGR01612 1093 lkhynfDDFGKEENIKYADEINkikddIKNLDQKIDHHIKAL----EEIKKKSENYIDEIKAQINDLEDvaDKAISNDDP 1168
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1641 KKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDyQRELEEARA-------SRDEIFTQSKENEKK-----LKGLEA 1708
Cdd:TIGR01612 1169 EEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEVKGinlsygkNLGKLFLEKIDEEKKksehmIKAMEA 1247
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1709 EILQLQEDHAASERARRHAEQERDELAD----EISNSASGKSSLLEEKrrleariaQLEEELEEEQGNMELLNDRFRKSN 1784
Cdd:TIGR01612 1248 YIEDLDEIKEKSPEIENEMGIEMDIKAEmetfNISHDDDKDHHIISKK--------HDENISDIREKSLKIIEDFSEESD 1319
|
890
....*....|....*....
gi 1604804596 1785 IqvDNLNTELAGERSAAQK 1803
Cdd:TIGR01612 1320 I--NDIKKELQKNLLDAQK 1336
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1504-1677 |
7.25e-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: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1504 TKALSMARALEEALEAKEELERFNKQ-----LRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1578
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQREeeleeLQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1579 TEDAKLRL---EVNMQAMKAQFD---RDLQARDEQGEEKKRLLVKQVRemeaELEDERKQRTLavASKKKLE--MDLNEL 1650
Cdd:pfam05667 389 KKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYR----ALKEAKSNKED--ESQRKLEeiKELREK 462
|
170 180
....*....|....*....|....*..
gi 1604804596 1651 EGQIEAANKGRDEAVKQlrkLQAQMKD 1677
Cdd:pfam05667 463 IKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1022-1173 |
7.25e-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: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1022 KKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD----AETTDLQDQIVELQA 1097
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 1098 QIEELKFQLTKKEEELQAAlarsdEETLQKNNALKQvrELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEALK 1173
Cdd:smart00787 219 EIMIKVKKLEELEEELQEL-----ESKIEDLTNKKS--ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1084-1230 |
7.26e-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: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1084 ETTDLQDQIVELQAQIEELKFQLTKKE---EELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEK 1160
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 1161 L-------KRDLsEELEALKTELEDTLDTTAAQQE-LRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELS 1230
Cdd:pfam00529 132 LapiggisRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
999-1235 |
7.40e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 999 AKIKKMEEDILLLEDQNSKFLKEKKLLEDRISEMTS-QLTEEEEkaknlgkvknkqemmmVDLEE---RLKKEEKTRQEL 1074
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELEAaALQPGEE----------------EELEEerrRLSNAEKLREAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1075 EKAKRKLDAETTDLQDQIVELQAQIEELkfqlTKKEEELQAALARSDEetlqknnALKQVRELQAHLAELQEDLES---- 1150
Cdd:COG0497 229 QEALEALSGGEGGALDLLGQALRALERL----AEYDPSLAELAERLES-------ALIELEEAASELRRYLDSLEFdper 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1151 -----EKMcrSKAEKLKR---DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETknheAQIQEMRQRQ 1222
Cdd:COG0497 298 leeveERL--ALLRRLARkygVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----EKLSAARKKA 371
|
250
....*....|....
gi 1604804596 1223 ATALEE-LSEQLEQ 1235
Cdd:COG0497 372 AKKLEKaVTAELAD 385
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1616-1905 |
7.48e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1616 VKQVREMEAELEDERKQRTLAVASKKKLEMDLNE----LEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDE 1691
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEelkeLAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1692 IFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNsasgksslLEEKRRLEARIAQLEEELEEEQG 1771
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLS--------PEEEKELVEKIKELEKELEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1772 NMELlndrfrksNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKsKFKASIAALEAKILQLEDQL 1851
Cdd:COG1340 155 ALEK--------NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1604804596 1852 EQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQyKEQMEKANSRMKQLKR 1905
Cdd:COG1340 226 DELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1067-1344 |
7.52e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1067 EEKTRQELEKAKRKLDAETTD------LQDQIVELQAQIEE-----------LKFQLTKKEEELQAALARSD--EETLQK 1127
Cdd:PLN03229 457 ELALNEMIEKLKKEIDLEYTEaviamgLQERLENLREEFSKansqdqlmhpvLMEKIEKLKDEFNKRLSRAPnyLSLKYK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1128 NNALKQVRELQAhlaelqedlESEKmcRSKAEKLKR-------------DLSEELEALKTELEDTLDTTAAqqELRSKRE 1194
Cdd:PLN03229 537 LDMLNEFSRAKA---------LSEK--KSKAEKLKAeinkkfkevmdrpEIKEKMEALKAEVASSGASSGD--ELDDDLK 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1195 QEVAELKKAIDEET----KNHEAQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQ--------SLENDNKELSCDV- 1261
Cdd:PLN03229 604 EKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKiervirssDLKSKIELLKLEVa 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1262 KTLQQAKTESEHKRKKLEAQLQEFMARATEAErtkgELAERSHKLQTELDNActmLEVAEKKGLKLAKEVDKLNSKLQDS 1341
Cdd:PLN03229 684 KASKTPDVTEKEKIEALEQQIKQKIAEALNSS----ELKEKFEELEAELAAA---RETAAESNGSLKNDDDKEEDSKEDG 756
|
...
gi 1604804596 1342 EEL 1344
Cdd:PLN03229 757 SRV 759
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1090-1335 |
7.80e-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: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1090 DQIV---ELQAQIEELKFQLTKKEeelQAALARSDEETLQKNNA-LKQVRELQ-AHLAELQEDLES-EKMCRSKAEKLKR 1163
Cdd:NF012221 1532 DNVVatsESSQQADAVSKHAKQDD---AAQNALADKERAEADRQrLEQEKQQQlAAISGSQSQLEStDQNALETNGQAQR 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1164 D-LSEELEALKTELE------DTLDTTAAQQELRSK--REQEVAELKKAIDEE---TKNH-EAQIQEMRQRQATALEELS 1230
Cdd:NF012221 1609 DaILEESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1231 EQLEQAKRFKSNLEKNKQSLENDnkelscdvktLQQAKTESEhkRKKLEAQLQEfmARATEAErTKGELAERSHKLQTEL 1310
Cdd:NF012221 1689 DAVAKSEAGVAQGEQNQANAEQD----------IDDAKADAE--KRKDDALAKQ--NEAQQAE-SDANAAANDAQSRGEQ 1753
|
250 260
....*....|....*....|....*....
gi 1604804596 1311 DNACTMLEV----AEKKGLKLaKEVDKLN 1335
Cdd:NF012221 1754 DASAAENKAnqaqADAKGAKQ-DESDKPN 1781
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
938-1131 |
7.80e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 938 KQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLDKVTAEAKIKKMEEDILLLEDQ--N 1015
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1016 SKFLKEKKLLEDRISEMTSQLTEEEEKAKNLgkvknkqemmMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVEL 1095
Cdd:COG1579 85 VRNNKEYEALQKEIESLKRRISDLEDEILEL----------MERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1604804596 1096 QAQIEELKFQLTKKEEELQAALARSDEETLQKNNAL 1131
Cdd:COG1579 155 EAELEELEAEREELAAKIPPELLALYERIRKRKNGL 190
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1550-1951 |
8.07e-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: 44.57 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1550 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmQAMKAQFDRDLQARDEQGEEKKRLL--VKQVREMEAELE 1627
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRarIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1628 DERKQRTLAVASKKKLEMD--LNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQR-ELEEARASRDEIFTQSKENEKKLK 1704
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIkaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqQSSIEEQRRLLQTLHSQEIHIRDA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1705 GLEAEILQLQEDHAASERARRHAEQERDELADEISNSASgksSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSN 1784
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC---KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1785 IQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgtVKSKFKASIAALEAKILQLEDQLEQEAKERA----- 1859
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE--QIHLQETRKKAVVLARLLELQEEPCPLCGSCihpnp 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1860 ----------------AANKIVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQleeaeeeATRANATRRK 1923
Cdd:TIGR00618 516 arqdidnpgpltrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPN 588
|
410 420
....*....|....*....|....*...
gi 1604804596 1924 LQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1417-1897 |
8.14e-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: 44.57 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1417 KLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAEEKTISAQYAEERDRAE 1496
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1497 AEARekdtkalsmaraleealeakeeLERFNKQLRAEMEDLMSSkddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1576
Cdd:TIGR00618 254 EQLK----------------------KQQLLKQLRARIEELRAQ-----EAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1577 QATEDAKLRLEVNMQAM-KAQFDRDLQARDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKK---LEMDLNELEG 1652
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtLTQHIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1653 QIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERD 1732
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1733 ELADEISNSASGKSSLLEEKRRLEARIAqleeELEEEQGNMELLNDRFRKSNIQVDNLNtELAGERSAAQKSENARQQME 1812
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPARQDID-NPGPLTRRMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1813 RQNKDLKAKLAELegtvkskfKASIAALEAKILQLEDQLEQEAKER----AAANKIVRRTEKKLKEVMMQVEDERRHADQ 1888
Cdd:TIGR00618 542 TSEEDVYHQLTSE--------RKQRASLKEQMQEIQQSFSILTQCDnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
....*....
gi 1604804596 1889 YKEQMEKAN 1897
Cdd:TIGR00618 614 QHALLRKLQ 622
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1590-1969 |
9.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1590 MQAMKAQFDRDLQARDEQ----GEEKKRLLVKQVREMEAELEDERKQrtlaVASKKKLEMDLNELEGQIEAANKGRDEAV 1665
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1666 KQLRKLQaQMKDYQRELEEARASRDEIftqsKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGK 1745
Cdd:COG4717 116 EELEKLE-KLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1746 ----SSLLEEKRRLEARIAQLEEELEEEQGNMELLNDrfrksniQVDNLNTELAGERSAAQKSENARQQM---------- 1811
Cdd:COG4717 191 eeelQDLAEELEELQQRLAELEEELEEAQEELEELEE-------ELEQLENELEAAALEERLKEARLLLLiaaallallg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1812 --------ERQNKDLKAKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDER 1883
Cdd:COG4717 264 lggsllslILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1884 RHADQYKEQMEKANSRMKQLKRQLEEAEEEA--TRANATRRKLQRELDDATEASEGLTREVSSLKNRLRRGGPVSSFSSS 1961
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
....*...
gi 1604804596 1962 RSGRRNLN 1969
Cdd:COG4717 424 ALDEEELE 431
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1002-1308 |
9.83e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1002 KKMEEDILLLedqnSKFLKEKKLLEDRISEMTSQLTEeeekaknlgkvknkQEMMMVDLEERLKKEEKTRQELEKakrKL 1081
Cdd:PHA02562 153 RKLVEDLLDI----SVLSEMDKLNKDKIRELNQQIQT--------------LDMKIDHIQQQIKTYNKNIEEQRK---KN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1082 DAETTDLQDQIVELQAQIEELKFQLtkkeEELQAALARSDEETLQKNNALKQVRELQAhlaelqeDLESEKMCRSKAEKL 1161
Cdd:PHA02562 212 GENIARKQNKYDELVEEAKTIKAEI----EELTDELLNLVMDIEDPSAALNKLNTAAA-------KIKSKIEQFQKVIKM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1162 KRDlSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDEETKnheaQIQEMRQRqataLEELSEQLEQAKRFKS 1241
Cdd:PHA02562 281 YEK-GGVCPTCTQQISEG-------PDRITKIKDKLKELQHSLEKLDT----AIDELEEI----MDEFNEQSKKLLELKN 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1242 NLEKNKQSLENDNKElscdVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQT 1308
Cdd:PHA02562 345 KISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1025-1109 |
9.99e-04 |
|
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: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1025 LEDRISEMTSQLTEEEEKAKNLGKVKNkqEMMMVDLEERLK----------KEEKTRQELEKAKRKLDAETTDLQDQIVE 1094
Cdd:cd23165 11 LNARLHELKEELKAKKKELENLEDASD--ELELADDDEPVPykigevfvhlSLEEAQERLEKAKEELEEEIEKLEEEIDE 88
|
90
....*....|....*
gi 1604804596 1095 LQAQIEELKFQLTKK 1109
Cdd:cd23165 89 IEEEMKELKVQLYAK 103
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1702-1861 |
1.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1702 KLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLndrfr 1781
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1782 KSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEG---TVKSKFKASIAALEAKILQLEDQLEQEAKER 1858
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAelaELEAELEEKKAELDEELAELEAELEELEAER 165
|
...
gi 1604804596 1859 AAA 1861
Cdd:COG1579 166 EEL 168
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1241-1503 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1241 SNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAERTKGELAERSHKLQTELDNActmleVA 1320
Cdd:pfam15905 41 LNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAA-----VR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1321 EKKGLKLAKEV-DKLNSKLQDSEELRQ----EETRQKlNLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMF 1395
Cdd:pfam15905 116 EKTSLSASVASlEKQLLELTRVNELLKakfsEDGTQK-KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1396 ETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFD 1475
Cdd:pfam15905 195 HSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS 274
|
250 260
....*....|....*....|....*...
gi 1604804596 1476 QLLAEEKTISAQYAEERDRAEAEAREKD 1503
Cdd:pfam15905 275 KQIKDLNEKCKLLESEKEELLREYEEKE 302
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1549-1945 |
1.20e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1549 HELEKSKRTL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQfdRDLQARDEQGEEkkrlLVKQ 1618
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQ--EKIERYQEDLEE----LTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1619 VREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDeaVKQLRKLQAQMKdyQRELEEARA-------SRDE 1691
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALD--VQQTRAIQYQQA--VQALEKARAlcglpdlTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1692 IFTQSKENEKKLKGLEAEILQLQEDHAASERARR---HAEQERDELADEISNSASGKS--SLLEEKRRLEARIAQleeel 1766
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTarELLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1767 eeeqgnmellndrfrksniqVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgtvkskfkasiaALEAKILQ 1846
Cdd:COG3096 514 --------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1847 LEDQLEQEAKERAAANKIVRRTEKKLKEVMMQVEDERRHADQYKeqmeKANSRMKQLKRQLEEAEEEATRANATR----- 1921
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMqqlle 637
|
410 420
....*....|....*....|....*.
gi 1604804596 1922 --RKLQRELDDATEASEGLTREVSSL 1945
Cdd:COG3096 638 reREATVERDELAARKQALESQIERL 663
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1444-1878 |
1.20e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1444 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLaeEKTISAQYAEERDRAEAEAREKDTKALsMARALEEALEAKEEL 1523
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRARLLLLALAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1524 ERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQA 1603
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1604 RDEQGEEKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELE 1683
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1684 EARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLE 1763
Cdd:COG5278 326 AALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1764 EELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEGTVKSKFKASIAALEAK 1843
Cdd:COG5278 406 AAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
410 420 430
....*....|....*....|....*....|....*
gi 1604804596 1844 ILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMMQ 1878
Cdd:COG5278 486 EAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1441-1687 |
1.22e-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: 43.60 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1441 KTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQLLAE-EKTISAQYAEERD-RAEAEAREKDTKALSmARALEEALE 1518
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRIRAlEQELAALEAELAELE-KEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1519 AKEELERFNKQLRA--------EMEDLMSSKDdvgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnm 1590
Cdd:COG4942 99 LEAQKEELAELLRAlyrlgrqpPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1591 qamkaqfdrdlqardeqgEEKKRLlvkqvREMEAELEDERKQRTLAVASKKKLemdLNELEGQIEAANKGRDEAVKQLRK 1670
Cdd:COG4942 171 ------------------AERAEL-----EALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*..
gi 1604804596 1671 LQAQMKDYQRELEEARA 1687
Cdd:COG4942 225 LEALIARLEAEAAAAAE 241
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1571-1872 |
1.25e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1571 ELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQGEEKKrllvkqvremeaelEDERKQRTLAVASKkklemdLNEL 1650
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAA--------------EARAAKDKDAVAAA------LARV 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1651 EGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKlkgleAEILqlqedhAASERAR-RHAEQ 1729
Cdd:PRK05035 496 KAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKK-----AAVA------AAIARAKaKKAAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1730 ErDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDrfRKSNIqvdnlntELAGERSAAQKSenARQ 1809
Cdd:PRK05035 565 Q-AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP--KKAAV-------AAAIARAKAKKA--EQQ 632
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604804596 1810 QMERQNKDLKAKLAELEGTVkSKFKASIAALEAKilQLEDQLEQEAKERAAANKIVRRTEKKL 1872
Cdd:PRK05035 633 ANAEPEEPVDPRKAAVAAAI-ARAKARKAAQQQA--NAEPEEAEDPKKAAVAAAIARAKAKKA 692
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1550-1735 |
1.26e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1550 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqaRDEQGEEKKRLLVKQVREMEAELEDE 1629
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1630 RKQRTLAVASKKKLEmdlnelegqiEAANKGRDEAVKqlrKLQAQMKdyqRELEEARASRDEIFTQSKENEKKLKGLEAE 1709
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 1604804596 1710 ILQLQEDHAASERARRHAEQERDELA 1735
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1494-1951 |
1.31e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1494 RAEAEAREKDTKALSmaraleealeakeelerfnkqLRAEmedLMSSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELE 1573
Cdd:PRK04863 276 RHANERRVHLEEALE---------------------LRRE---LYTSRR-------QLAAEQYRLVEMARELAELNEAES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1574 DELQATEDAKLRLEVNMQAMKAQ-----FDRDLQARDEQGEEKkrllvKQVREMEAELEDERkqrtlavaskkklemdln 1648
Cdd:PRK04863 325 DLEQDYQAASDHLNLVQTALRQQekierYQADLEELEERLEEQ-----NEVVEEADEQQEEN------------------ 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1649 elEGQIEAANKGRDEavkqlrkLQAQMKDYQRELEEA--RASRDEIFTQSKENEKKLKGLEA-EILQLQEDHAASERARR 1725
Cdd:PRK04863 382 --EARAEAAEEEVDE-------LKSQLADYQQALDVQqtRAIQYQQAVQALERAKQLCGLPDlTADNAEDWLEEFQAKEQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1726 HAEQERDELADEISnSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNdRFRKSNIQVDNLNtELAGERSAAQKSE 1805
Cdd:PRK04863 453 EATEELLSLEQKLS-VAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR-RLREQRHLAEQLQ-QLRMRLSELEQRL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1806 NARQQMERQNKDLKaKLAELEGTVKSKFKASIAALEAKILQLEDQLEQEAKERAAankivrrTEKKLKEVMMQVEDERRH 1885
Cdd:PRK04863 530 RQQQRAERLLAEFC-KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA-------LRQQLEQLQARIQRLAAR 601
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604804596 1886 ADQYKEqmekANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:PRK04863 602 APAWLA----AQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1664-1951 |
1.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1664 AVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAE---QERDELADEISN 1740
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1741 SASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNiqvdnlntelagersAAQKSENARQQMERQNKDLKA 1820
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---------------ELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1821 KLAELEGTvKSKFKASIAALEAKILQLEDQLEQeakeraaankiVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANsRM 1900
Cdd:PRK03918 308 ELREIEKR-LSRLEEEINGIEERIKELEEKEER-----------LEELKKKLKELEKRLEELEERHELYEEAKAKKE-EL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1901 KQLKRQLeeaeeeatrANATRRKLQRELDDATEASEGLTREVSSLKNRLRR 1951
Cdd:PRK03918 375 ERLKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1080-1243 |
1.33e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1080 KLDAETTDLQDQIVELQAQIEELKfqLTKKEEELQAALARSDE--ETLQ-----KNNALKQVRELQAHLAELQEdleSEK 1152
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQlyDILErevkaRKYVEKNSDTLPDFLEHAKE---QNK 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1153 MCRSKAEKLK-------------RDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHE---AQIQ 1216
Cdd:PRK04778 328 ELKEEIDRVKqsytlneselesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEklsEMLQ 407
|
170 180 190
....*....|....*....|....*....|..
gi 1604804596 1217 EMRQRQATA---LEELSEQLEQAKRF--KSNL 1243
Cdd:PRK04778 408 GLRKDELEArekLERYRNKLHEIKRYleKSNL 439
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1059-1361 |
1.40e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1059 DLEERLKKEEKTRQELEKAKRKLDAettdLQDQIVELQAQIEELKFQLtkkeEELQAALARSDEEtlqknnalkqvrelq 1138
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEE----LRADEAERARELDLLRFQL----EELEAAALQPGEE--------------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1139 ahlaelqEDLESEKMCRSKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELrskreQEVAElkkaideetknHEAQIQE 1217
Cdd:COG0497 209 -------EELEEERRRLSNAEKLREALQEALEALSGGEGGALDLlGQALRAL-----ERLAE-----------YDPSLAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1218 MRQRqataLEELSEQLEQAKRfksNLEKNKQSLENDNKELscdvktlqqaktesehkrkkleAQLQEFMARATEAER--- 1294
Cdd:COG0497 266 LAER----LESALIELEEAAS---ELRRYLDSLEFDPERL----------------------EEVEERLALLRRLARkyg 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1295 -TKGELAERSHKLQTELDNactmLEVAEKKGLKLAKEVDKLNSKLQD-SEELRQEetRQK--LNLSTQIRQ 1361
Cdd:COG0497 317 vTVEELLAYAEELRAELAE----LENSDERLEELEAELAEAEAELLEaAEKLSAA--RKKaaKKLEKAVTA 381
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1012-1208 |
1.45e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1012 EDQNSKFLKEKKLLEdRISEMTSQLTEEEEKAKnlGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1091
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1092 IVELQAQIEELK----FQL----------------TKKEEELQAALARSD----------------------------EE 1123
Cdd:PRK05771 116 IKELEQEIERLEpwgnFDLdlslllgfkyvsvfvgTVPEDKLEELKLESDvenveyistdkgyvyvvvvvlkelsdevEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1124 TLQKNNALKQVRELQAHLAELQEDLESEKmcrSKAEKLKRDLSEELEALKTELEDTLdtTAAQQELRSKREQEVAELKKA 1203
Cdd:PRK05771 196 ELKKLGFERLELEEEGTPSELIREIKEEL---EEIEKERESLLEELKELAKKYLEEL--LALYEYLEIELERAEALSKFL 270
|
....*
gi 1604804596 1204 IDEET 1208
Cdd:PRK05771 271 KTDKT 275
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1393-1951 |
1.57e-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: 43.67 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1393 QMFETKKKLEEDLGSMEG----LEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTK-NRLQQELDDLMVDLDHQRQIVSNL 1467
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFgyksDETLIASRQEERQETSAELNQLLRTLDDQWKEKrDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1468 EKKQKKFDQLLAEEKtisAQYAEERD--RAEAEAREKDTKALSMAraleealeAKEELERFNKQLRAEMEDLmssKDDVG 1545
Cdd:pfam12128 328 EDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKALTGK--------HQDVTAKYNRRRSKIKEQN---NRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1546 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT--------EDAKLRLEVNMQAMKAQFDrDLQARDEQgEEKKRLLVK 1617
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQleagklefNEEEYRLKSRLGELKLRLN-QATATPEL-LLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1618 QVREMEAELEDERKQR---TLAVASKKKLEMDLNELEGQIEAA---NKGRDEAVKQ---------LRKLQAQMKDYQREL 1682
Cdd:pfam12128 472 RIERAREEQEAANAEVerlQSELRQARKRRDQASEALRQASRRleeRQSALDELELqlfpqagtlLHFLRKEAPDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1683 EEARASR--------DEIFTQSKENEKKLKG--LEAEILQLQEDHAASERARRHAEQERDELADEISNSAsgksslleek 1752
Cdd:pfam12128 552 GKVISPEllhrtdldPEVWDGSVGGELNLYGvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA---------- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1753 rRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKS--------ENARQQMERQNKDLK----- 1819
Cdd:pfam12128 622 -AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAlaerkdsaNERLNSLEAQLKQLDkkhqa 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1820 -----------------AKLAELEGTVKSK---FKASIAALE----AKILQLEDQLEQEAKERAAANKIVRRTEKKLKEV 1875
Cdd:pfam12128 701 wleeqkeqkreartekqAYWQVVEGALDAQlalLKAAIAARRsgakAELKALETWYKRDLASLGVDPDVIAKLKREIRTL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1876 MMQVEDERR------------------HADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAtrrKLQRELDDATEASEG 1937
Cdd:pfam12128 781 ERKIERIAVrrqevlryfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRA---KLEMERKASEKQQVR 857
|
650
....*....|....
gi 1604804596 1938 LTREVSSLKNRLRR 1951
Cdd:pfam12128 858 LSENLRGLRCEMSK 871
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1051-1284 |
1.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1051 NKQEMMMVDLEERLKKEEKTRQELEKAKRKLD---AETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQK 1127
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDelnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1128 NNALKQVRELQAHLAELQEDLESekmcRSKAEKLKRDLSEELEALKTELEDTLDTTAAQQEL--RSKR-EQEVAELKKAI 1204
Cdd:COG1340 81 DELNEKLNELREELDELRKELAE----LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1205 DEETKNHE--AQIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQL 1282
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
..
gi 1604804596 1283 QE 1284
Cdd:COG1340 237 KE 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
864-1303 |
1.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 864 PLLQVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLieeKNILAEQLHAEtelFAEAEEMRVRLLSRK-QELE 942
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAF---SRFIGSHLAVA---FEADPEAELRQLNRRrVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 943 EILHDLESrveeeeeRNQSLQNEKKKmqshiqdleeqldeeeaARQKLQLdkvtaeakIKKMEEDILLLEDQNskflkek 1022
Cdd:PRK04863 851 RALADHES-------QEQQQRSQLEQ-----------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1023 klLEDRISEMTSQLTEEEEKAKNlgkvknkqemmmvdleerLKKEEKTRQELEKAKRKLDAEttdlqdqivelQAQIEEL 1102
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKRF------------------VQQHGNALAQLEPIVSVLQSD-----------PEQFEQL 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1103 KFQLTKKEEELQAALARSDeetlqknnALKQVRELQAHLA--ELQEDLESEKmcrSKAEKLKRDLsEELEALKTELEDTL 1180
Cdd:PRK04863 941 KQDYQQAQQTQRDAKQQAF--------ALTEVVQRRAHFSyeDAAEMLAKNS---DLNEKLRQRL-EQAEQERTRAREQL 1008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1181 DTTAAQ--------QELRSKR---EQEVAELKKAIDEETKNHEAqiqEMRQRQATALEELSEQLEQAKRFKSNLEKNKQS 1249
Cdd:PRK04863 1009 RQAQAQlaqynqvlASLKSSYdakRQMLQELKQELQDLGVPADS---GAEERARARRDELHARLSANRSRRNQLEKQLTF 1085
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1250 LE----NDNKELSCDVKTLQQAKTESEHKRKKLEAQLQefMARATEAER--TKGELAERS 1303
Cdd:PRK04863 1086 CEaemdNLTKKLRKLERDYHEMREQVVNAKAGWCAVLR--LVKDNGVERrlHRRELAYLS 1143
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
867-1483 |
1.82e-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: 43.50 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 867 QVTRQEEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLHAETELFAEA-EEMRVRLLSRKQELEEIL 945
Cdd:TIGR01612 1170 EIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKiDEEKKKSEHMIKAMEAYI 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 946 HDLESrveeEEERNQSLQNE-------KKKMQS-----------HIQDLEEQLDEEEAARQKLQLDKVTAEAK----IKK 1003
Cdd:TIGR01612 1250 EDLDE----IKEKSPEIENEmgiemdiKAEMETfnishdddkdhHIISKKHDENISDIREKSLKIIEDFSEESdindIKK 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1004 -MEEDILLLEDQNSKF---------------LKEKKLLEDRISEMTSQLteeEEKAKNLgkvknKQEMmmvDLEERLKKE 1067
Cdd:TIGR01612 1326 eLQKNLLDAQKHNSDInlylneianiynilkLNKIKKIIDEVKEYTKEI---EENNKNI-----KDEL---DKSEKLIKK 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1068 EKTRQELEKAKRKLDAeTTDLQDqIVELQAQIEELKFQLTKKEEELQAALARSDEET----------------------L 1125
Cdd:TIGR01612 1395 IKDDINLEECKSKIES-TLDDKD-IDECIKKIKELKNHILSEESNIDTYFKNADENNenvlllfkniemadnksqhilkI 1472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1126 QKNNAlkqVRELQAHLAELQEDLESEKMCRSKAEKLKRDLS---EELEALKTELEDTLDTTAAqQELRSKREQ------- 1195
Cdd:TIGR01612 1473 KKDNA---TNDHDFNINELKEHIDKSKGCKDEADKNAKAIEknkELFEQYKKDVTELLNKYSA-LAIKNKFAKtkkdsei 1548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1196 ---EVAELKKAIDEETKNHEAQIQEMRQRQATALEELseqleqAKRFKSN-----LEKNKQSLENDNKELSCDVKTLQQA 1267
Cdd:TIGR01612 1549 iikEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDA------AKNDKSNkaaidIQLSLENFENKFLKISDIKKKINDC 1622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1268 KTESEhkrkKLEAQLQEFMARATEAERTkgELAERSHKLQTELDNactmLEVAEKKGLKLAKEVDKLNSKLQDSE-ELRQ 1346
Cdd:TIGR01612 1623 LKETE----SIEKKISSFSIDSQDTELK--ENGDNLNSLQEFLES----LKDQKKNIEDKKKELDELDSEIEKIEiDVDQ 1692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1347 EETRQKLNLSTQIRQLEV-DRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLEEDLGSMEGLEEvkrKLQKDVELT 1425
Cdd:TIGR01612 1693 HKKNYEIGIIEKIKEIAIaNKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYE---EFIELYNII 1769
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604804596 1426 SQCLE---EKTMAMDKMEKTKNRLQQElddLMVDLDHQRQIVSNLEK-KQKKFDQLLAEEKT 1483
Cdd:TIGR01612 1770 AGCLEtvsKEPITYDEIKNTRINAQNE---FLKIIEIEKKSKSYLDDiEAKEFDRIINHFKK 1828
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
872-1423 |
1.86e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 872 EEELQAKDEELVKVKERQLKVENELVEMERKHQQLIEEKNILAEQLhaeTELFAEAEEMRvRLLSRKQELEEILHDLESR 951
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY---NNLKSALNELS-SLEDMKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 952 VEEEEERN---QSLQNEKKKMQS--------HIQDLEEQLDEEEAARQKLQ---LDKVTAEAKIKKMEEdillLEDQNSK 1017
Cdd:PRK01156 265 LSMELEKNnyyKELEERHMKIINdpvyknrnYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1018 FLKEKKLLED---RISEM-------TSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTD 1087
Cdd:PRK01156 341 YIKKKSRYDDlnnQILELegyemdyNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1088 LQDQIVELQAQIEELkfqltkkeeelqaalaRSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRdLSE 1167
Cdd:PRK01156 421 ISSKVSSLNQRIRAL----------------RENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSR-LEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1168 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELSEQLEQAKRFKS----NL 1243
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkleDL 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1244 EKNKQSLENDNKELS-CDVKTLQQAKTESEHKRKKLEAQLQEFMARATEAErtkgelaERSHKLQTELDNACTMLEVAEK 1322
Cdd:PRK01156 564 DSKRTSWLNALAVISlIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK-------SYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1323 KGLKLAKEVDKLNSKLQDseeLRQEetrqklnlSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQLQMVQSQMFETKKKLE 1402
Cdd:PRK01156 637 EIQENKILIEKLRGKIDN---YKKQ--------IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
570 580
....*....|....*....|.
gi 1604804596 1403 EDLGSMEGLEEVKRKLQKDVE 1423
Cdd:PRK01156 706 ILRTRINELSDRINDINETLE 726
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1059-1149 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1059 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQ 1138
Cdd:pfam11932 17 QALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERELV 96
|
90
....*....|.
gi 1604804596 1139 AHLAELQEDLE 1149
Cdd:pfam11932 97 PLMLKMLDRLE 107
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1548-1949 |
2.25e-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: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1548 VHELEKSKrTLEQQVEEMRTQLEELEDELQATEDAKLR----LEVN---MQAMKAQFDRdLQARDEQGEEKKRLLVKQVR 1620
Cdd:pfam05701 31 IQTVERRK-LVELELEKVQEEIPEYKKQSEAAEAAKAQvleeLESTkrlIEELKLNLER-AQTEEAQAKQDSELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1621 EME------------AELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQLRklqaqmkdyqreleearas 1688
Cdd:pfam05701 109 EMEqgiadeasvaakAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAE------------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1689 rdEIFTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDELA----DEISNSASGKSSLLEEKRRLEARIAQLEE 1764
Cdd:pfam05701 170 --EAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareQDKLNWEKELKQAEEELQRLNQQLLSAKD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1765 ELEEEQGNMELLNDrfrksniqvdnLNTELAGERSAAQKSENARQQMERQ-NKDLKAKLA----ELEgtvksKFKASI-- 1837
Cdd:pfam05701 248 LKSKLETASALLLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALAsakkELE-----EVKANIek 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1838 AALEAKILQ-----LEDQLEQEAKERAAankiVRRTEKKLKEVMMQVEDERRHADQ----YKEQMEKANSRMKQLKRQLE 1908
Cdd:pfam05701 312 AKDEVNCLRvaaasLRSELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQ 387
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1604804596 1909 EAEEEATRANATRRKLQRELDDATEASEGLTREVSSLKNRL 1949
Cdd:pfam05701 388 QAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRL 428
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1609 |
2.89e-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: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1391 QSQMFETKKKLEEDLGSMEGLEEVKRKLQKDVELTSQCLEEKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1470
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1471 QKK-------FDQLLAeektiSAQYAEERDRAEAEAR--EKDTKALSMARALEealeakeelerfnKQLRAEMEDLMSSK 1541
Cdd:COG3883 95 LYRsggsvsyLDVLLG-----SESFSDFLDRLSALSKiaDADADLLEELKADK-------------AELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604804596 1542 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQGE 1609
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1653-1933 |
2.92e-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: 42.80 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1653 QIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASR----DEIFTQSKENEKKLKGLEAEILQLQEDhaasERARRHAE 1728
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1729 QERDELADEISNSASGKSSLLEEKRRLEaRIAQLEEELEEEQgnmELLNDRFRKSNIQVDNLNtELAGERSAAQKSENAR 1808
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVK---ILEEERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1809 QQMERQNKDLKAKLAELEGTVK-SKFKASIAALEAKILQLEDQLEQEAKERAAANKIVRRTEKKLKEVMmqVEDERRHAD 1887
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM--IEEERKRKL 517
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1604804596 1888 QYKEQMEKANSRMKQLKRQLEEAEEEATRANATRRKLQRELDDATE 1933
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1057-1152 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1057 MVDLEERLKKEEKTRQELEKAKRKLDAET-TDLQDQIVELQAQIEELKFQLtKKEEELQAALARSDEETLQKNNALKqvr 1135
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARW-EAEKELIEEIQELKEELEQRYGKIP--- 488
|
90
....*....|....*..
gi 1604804596 1136 ELQAHLAELQEDLESEK 1152
Cdd:COG0542 489 ELEKELAELEEELAELA 505
|
|
| CCDC90-like |
pfam07798 |
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ... |
1138-1237 |
3.13e-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: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1138 QAHLAELQEDLES-EK----MCRSKAEKLKRDLseelEALKTELEDTLDTTAAQQELrskreqEVAELKKAIDEETKNHE 1212
Cdd:pfam07798 56 KADLAELRSELQIlEKsefaALRSENEKLRREL----EKLKQRLREEITKLKADVRL------DLNLEKGRIREELKAQE 125
|
90 100
....*....|....*....|....*
gi 1604804596 1213 AQIQEMRQRQATALEELSEQLEQAK 1237
Cdd:pfam07798 126 LKIQETNNKIDTEIANLRTQIESVK 150
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1657-1740 |
3.17e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1657 ANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEI---FTQSKENEKKLKGLEAEILQLQEDHAASERARRHAEQERDE 1733
Cdd:PRK05431 19 AKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEIKALEAELDELEAELEE 98
|
....*..
gi 1604804596 1734 LADEISN 1740
Cdd:PRK05431 99 LLLRIPN 105
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
1035-1120 |
4.03e-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: 41.95 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1035 QLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD----------QIVELQAQIEELKF 1104
Cdd:smart00435 278 SMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKekkkeekkkkQIERLEERIEKLEV 357
|
90
....*....|....*.
gi 1604804596 1105 QLTKKEEELQAALARS 1120
Cdd:smart00435 358 QATDKEENKTVALGTS 373
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
996-1222 |
4.29e-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: 41.75 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 996 TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRisemtsQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELE 1075
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQA------RQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1076 KAKRKLDAETTDLQDQIVELQAQIEELKFQLTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEKMCR 1155
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604804596 1156 SKAEKLKRdLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDEETKnHEAQIQEMRQRQ 1222
Cdd:TIGR02794 211 AKAEAEAA-AAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK-YAAIIQQAIQQN 275
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1025-1172 |
4.67e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1025 LEDRISEMTSQLTEE---EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIVELQAQIEE 1101
Cdd:PRK04863 518 LRMRLSELEQRLRQQqraERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1102 LKfQLTKKEEELQAALARSDEetlQKNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSEELEAL 1172
Cdd:PRK04863 598 LA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1528-1729 |
4.75e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1528 KQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFDRDLQARDEQ 1607
Cdd:COG1340 53 KELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDK-LRKEIERLEWRQQTEVLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1608 GEEKKRLLVK-------------------QVREMEAELEDERKQRTLAVASKKKLEMDLNELEGQIEAANKGRDEAVKQL 1668
Cdd:COG1340 132 PEEEKELVEKikelekelekakkalekneKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1669 RKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAEILQLQEdHAASERARRHAEQ 1729
Cdd:COG1340 212 DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR-EKEKEELEEKAEE 271
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1064-1384 |
4.87e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1064 LKKEEKTRQELEKAKR-KLDAETTDLQDQIVELQAQIEELKfQLTKKEEELQAAL--ARSDEETLQKNNALKQVRELQAH 1140
Cdd:PRK10246 535 LEKEVKKLGEEGAALRgQLDALTKQLQRDESEAQSLRQEEQ-ALTQQWQAVCASLniTLQPQDDIQPWLDAQEEHERQLR 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1141 LAELQEDLESEKmcrSKAEKLKRDLSEELEALKTELEDTLDTTA-------AQQELRSKREQEVAELkkaidEETKNHEA 1213
Cdd:PRK10246 614 LLSQRHELQGQI---AAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSW-----QQRQNELT 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1214 QIQEMRQRQATALEELSEQLEQAKRFKSNLEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEAQL----------- 1282
Cdd:PRK10246 686 ALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFdtalqasvfdd 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1283 QEFMARATEAERTKGELAERSHKLQTELDNACTMLEVAEK----------KGLKLAKEVDKLNSKL-QDSEELRQEETRQ 1351
Cdd:PRK10246 766 QQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQalaqhqqhrpDGLDLTVTVEQIQQELaQLAQQLRENTTRQ 845
|
330 340 350
....*....|....*....|....*....|...
gi 1604804596 1352 KlNLSTQIRQLEVDRNTLLEQQEEEEEARRNLE 1384
Cdd:PRK10246 846 G-EIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1094-1280 |
4.98e-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: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1094 ELQAQIEELKfqlTKKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEkmcrskaEKLKRDLSEELEALK 1173
Cdd:pfam15665 11 EHEAEIQALK---EAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQH-------ERMKRQALTEFEQYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1174 TELED-TLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMRQRQATALEELS-------EQLEQAKRFKSN--- 1242
Cdd:pfam15665 81 RRVEErELKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRakhrqeiQELLTTQRAQSAssl 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1604804596 1243 ------LEKNKQSLENDNKELSCDVKTLQQAKTESEHKRKKLEA 1280
Cdd:pfam15665 161 aeqeklEELHKAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQA 204
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1786-1951 |
5.15e-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: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1786 QVDNLNTELAGERSAAQKSENARQQMERQNKDLKAKLAELEgtvkskfkASIAALEAKILQLEDQLEQEA--KERAAANK 1863
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE--------ARIKKYEEQLGNVRNNKEYEAlqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1864 IVRRTEKKLKEVMMQVEDERRHADQYKEQMEKANSRMKQLKRQLeeaeeeATRANATRRKLQRELDDATEASEGLTREVS 1943
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL------DEELAELEAELEELEAEREELAAKIPPELL 177
|
....*...
gi 1604804596 1944 SLKNRLRR 1951
Cdd:COG1579 178 ALYERIRK 185
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
998-1164 |
5.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 998 EAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--ISEMTSQLTEEEEKaknLGKVKNKqemmMVDLEERLKKEEKTRQELE 1075
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvCPTCTQQISEGPDR---ITKIKDK----LKELQHSLEKLDTAIDELE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1076 KakrKLDaETTDLQDQIVELQAQIEELKFQLT---KKEEELQAALARSDEETLQKNNALKQVRELQAHLAELQEDLESEK 1152
Cdd:PHA02562 327 E---IMD-EFNEQSKKLLELKNKISTNKQSLItlvDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
170
....*....|..
gi 1604804596 1153 MCRSKAEKLKRD 1164
Cdd:PHA02562 403 YHRGIVTDLLKD 414
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
999-1179 |
6.44e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.77 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 999 AKIKKMEEDILLLEdQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAK 1078
Cdd:PRK06669 2 PKVIFKRSNVINKE-KLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1079 RKLDAETTDLQDQIVELQAQIEELKFQL-TKKEEELQAALARSDEETLQKNNAlkqvrELQAHLAELQEDLesekmcRSK 1157
Cdd:PRK06669 81 EELLKKTDEASSIIEKLQMQIEREQEEWeEELERLIEEAKAEGYEEGYEKGRE-----EGLEEVRELIEQL------NKI 149
|
170 180
....*....|....*....|..
gi 1604804596 1158 AEKLKRDLSEELEALKTELEDT 1179
Cdd:PRK06669 150 IEKLIKKREEILESSEEEIVEL 171
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1021-1703 |
6.45e-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: 41.86 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1021 EKKLLEDRISEMTSQLTEEE----------EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD 1090
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEqrlrqqqnaeRLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1091 QIVELQAQIEElkfqLTKKEE---ELQAALARSDEETlqkNNALKQVRELQAHLAELQEDLESEKMCRSKAEKLKRDLSE 1167
Cdd:COG3096 586 QLEQLRARIKE----LAARAPawlAAQDALERLREQS---GEALADSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1168 ELEALkteledTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQIQEMR---QRQATALEELS---EQLEQAKRFKS 1241
Cdd:COG3096 659 QIERL------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYFSALygpARHAIVVPDLSavkEQLAGLEDCPE 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1242 NL---EKNKQS-----LENDNKELSCDVKTLQQAKTESEHK------RKKLEAQLQEFMARATEAERTKGELAERSHKLQ 1307
Cdd:COG3096 733 DLyliEGDPDSfddsvFDAEELEDAVVVKLSDRQWRYSRFPevplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQ 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1308 tELDNACTMLeVAEkkGLKLAKEVDKlnsklqdSEELRQeetrqklnLSTQIRQLEVDRNTLLEQQEEEEEARRNLEKQL 1387
Cdd:COG3096 813 -RLHQAFSQF-VGG--HLAVAFAPDP-------EAELAA--------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQL 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1388 QMVQSQMFETKKKLEEDLGsmEGLEEVKRKLQkdveltsQCLEektmAMDKMEKTKNRLQQeLDDlmvdldhqrqIVSNL 1467
Cdd:COG3096 874 QLLNKLLPQANLLADETLA--DRLEELREELD-------AAQE----AQAFIQQHGKALAQ-LEP----------LVAVL 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1468 EKKQKKFDQLlaeektisaqyAEERDRAEAEAREKDTKALSMAraleealEAKEELERFNKQLRAEMedLMSSKDDVGKN 1547
Cdd:COG3096 930 QSDPEQFEQL-----------QADYLQAKEQQRRLKQQIFALS-------EVVQRRPHFSYEDAVGL--LGENSDLNEKL 989
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1548 VHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQaMKAQFDRDLQA----RDEQGEEKKRLlvkQVREME 1623
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQ-TLQELEQELEElgvqADAEAEERARI---RRDELH 1065
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1624 AELEDERKQRtlavaskkklemdlNELEGQIEAANKGRDEAVKQLRKLQAQMKDYQRELEEARASRDEIFTQSKEN--EK 1701
Cdd:COG3096 1066 EELSQNRSRR--------------SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNdvER 1131
|
..
gi 1604804596 1702 KL 1703
Cdd:COG3096 1132 RL 1133
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1021-1215 |
6.95e-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: 41.58 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1021 EKKLLEDRISEMTSQLTEE-EEKAKNLGKVKNKQEMMMVDLEERLKK---EEKTRQELEKAKRKLDAETTDLQDQIVELQ 1096
Cdd:pfam13166 262 GQPLPAERKAALEAHFDDEfTEFQNRLQKLIEKVESAISSLLAQLPAvsdLASLLSAFELDVEDIESEAEVLNSQLDGLR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1097 AQIEELKFQLTKKEEelqaaLARSDEETLQKNNALKQVRELQAHLAELQEDLESEKmcRSKAEKLKRDLSEELEALKTEL 1176
Cdd:pfam13166 342 RALEAKRKDPFKSIE-----LDSVDAKIESINDLVASINELIAKHNEITDNFEEEK--NKAKKKLRLHLVEEFKSEIDEY 414
|
170 180 190
....*....|....*....|....*....|....*....
gi 1604804596 1177 EDTLDTTAAQQELRSKREQEVAELKKAIDEETKNHEAQI 1215
Cdd:pfam13166 415 KDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQL 453
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1003-1142 |
7.02e-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: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1003 KMEEDILLLEDQNSKFLKEKKLLEDRISEMTSQLTEEEEKAKNLGKVkNKQEMMMVDLEERLkkeEKTRQELEKAKRKLD 1082
Cdd:pfam15294 144 KLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEI-SDLEEKMAALKSDL---EKTLNASTALQKSLE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1083 AETTDLQDQIVELQAQIEELKFQLTKKEEelQAALARSDEETLQKNNalKQVRELQAHLA 1142
Cdd:pfam15294 220 EDLASTKHELLKVQEQLEMAEKELEKKFQ--QTAAYRNMKEMLTKKN--EQIKELRKRLS 275
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1528-1858 |
8.65e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1528 KQLRAEMEDLMSSKDDVGKNVHE--------LEKSKRTLE-----QQV--------EEMRTQLEELEDELQATEDAKLRL 1586
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEalqsalnwLEERKGSLErakqyQQVidnfpklsAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1587 EVNMQAMKAQFDRDLQARDEQGE-EKKRLLVKQVREMEAELEDERKQrtlavaskkklemdLNELEGQIEAANKGRDEAV 1665
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQEqDRAREISDSLSQLPQQQTEARRQ--------------LNEIERRLQTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1666 kqlrklQAQMKDYQRELEEARASRDEI-FTQ-SKENEKKLKGLEAEILQLQEDHAASE----------RARRHAEQ--ER 1731
Cdd:PRK10929 172 ------QAQLTALQAESAALKALVDELeLAQlSANNRQELARLRSELAKKRSQQLDAYlqalrnqlnsQRQREAERalES 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1732 DE-LADEISNSASGKSSLLEEKRRLEARIAQLEEEleeeqgnMELLNDRFRKSNIQVDNLNTELAGERSAAQ--KSENAR 1808
Cdd:PRK10929 246 TElLAEQSGDLPKSIVAQFKINRELSQALNQQAQR-------MDLIASQQRQAASQTLQVRQALNTLREQSQwlGVSNAL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1809 QQMerqnkdLKAKLAELEGTVKS-KFKASIAALEAKILQLEDQLEQEAKER 1858
Cdd:PRK10929 319 GEA------LRAQVARLPEMPKPqQLDTEMAQLRVQRLRYEDLLNKQPQLR 363
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
873-1133 |
9.00e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 873 EELQakDEELVKVKERQLKVENELVEMERKHQQLIEEK----NILAEQLHAETELFAEAEEmrVRLLSRKQELEEILHDL 948
Cdd:PRK05771 23 EALH--ELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklRSYLPKLNPLREEKKKVSV--KSLEELIKDVEEELEKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 949 ESRVEEEEERNQSLQNEKKKMQSHIQDleeqldeeeaarqklqldkvtaeakIKKME----EDILLLEDQNSKFL----- 1019
Cdd:PRK05771 99 EKEIKELEEEISELENEIKELEQEIER-------------------------LEPWGnfdlDLSLLLGFKYVSVFvgtvp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1020 KEKKLLEDRISEMTSQLTEEEEKAKN----LGKVKNKQEmmmvdLEERLKKEEKTRQELEkAKRKLDAETTDLQDQIVEL 1095
Cdd:PRK05771 154 EDKLEELKLESDVENVEYISTDKGYVyvvvVVLKELSDE-----VEEELKKLGFERLELE-EEGTPSELIREIKEELEEI 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1604804596 1096 QAQIEELKFQL---TKKEEELQAALARSDEETLQKNNALKQ 1133
Cdd:PRK05771 228 EKERESLLEELkelAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| Use1 |
pfam09753 |
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ... |
1117-1233 |
9.75e-03 |
|
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport.
Pssm-ID: 462882 [Multi-domain] Cd Length: 245 Bit Score: 40.00 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1117 LARSdeETLQKNNALKQVRELQAHLAELQEDLESEKMCRSK--AEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKRE 1194
Cdd:pfam09753 10 LSRC--ERLAKEDRSDNQWRLEKYVKALEEMLEELQKERDKpsKDVLN-EYSERVEFLKGLLEAEKLSSPEEKALANQFL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1604804596 1195 QEVAELKKAIDEETKNHEAQIQEMRQRQATALE-ELSEQL 1233
Cdd:pfam09753 87 APGFAESPRSPEESSERESASKELRQKTKAKYQsELRKEL 126
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1278-1946 |
9.78e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1278 LEAQLQEFMaraTEAERTKGELAERSHKLQTELDNACTMLEVAEKKGLKLAKEVDKLNSKLQDSEELRQEETrQKLNLST 1357
Cdd:pfam10174 1 LQAQLRDLQ---RENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEEN-QHLQLTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1358 QIRQLEVdrntlleqqeeeeEARRNLEkqlQMVQSQMFETKKKLEEDLGSMEGLEEVKRKLQ-------KDVELTSQCLE 1430
Cdd:pfam10174 77 QALQDEL-------------RAQRDLN---QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQseherqaKELFLLRKTLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1431 EKTMAMDKMEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQL------------LAEEKTISAQYAEERDRAEAE 1498
Cdd:pfam10174 141 EMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIaeaemqlghlevLLDQKEKENIHLREELHRRNQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1499 AREKDTKALSMARALEEALEAKEELERFNKQLRAEMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1578
Cdd:pfam10174 221 LQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1579 TEDAKLRLEVNMQAMKAQFDRDLQARDEQGE----EKKRLLVKQVREMEAELEDERKQRTLAVASKKKLEM--DLNELEG 1652
Cdd:pfam10174 301 KESELLALQTKLETLTNQNSDCKQHIEVLKEsltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLteEKSTLAG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1653 QIEAAN-----KGRDEAV--KQLRKLQAQMKDYQRELEEARASRDEIFTQSKENEKKLKGLEAeilQLQEDHAASERARR 1725
Cdd:pfam10174 381 EIRDLKdmldvKERKINVlqKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE---ALSEKERIIERLKE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1726 HAEQERDELADEISNSASGKSSLLEEKRRLEARIAQLEEELEEEQGNMELLNDRFRKSNIQVDNLNTELAGERSAAQKSE 1805
Cdd:pfam10174 458 QREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLE 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1806 NARQqmerqnkdlKAKLAELEGTVKSKFKAsiaaleaKILQLEDQLEQEAKERAAANKIVRRtekkLKEVMMQVEDERRH 1885
Cdd:pfam10174 538 NQLK---------KAHNAEEAVRTNPEIND-------RIRLLEQEVARYKEESGKAQAEVER----LLGILREVENEKND 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604804596 1886 ADQYKEQMEKANSRmkQLKRQLEEAEEEATRANATRRKLQRELDDATEASEGLTREVSSLK 1946
Cdd:pfam10174 598 KDKKIAELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1648-1752 |
9.83e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.19 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604804596 1648 NELEGQIEAANKGRDEAvkqlrklQAQMKDYQRELEEARASRDEIFTQSKENEKKLKglEAEILQLQEDHAAS-ERARRH 1726
Cdd:cd06503 33 EKIAESLEEAEKAKEEA-------EELLAEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAE 103
|
90 100
....*....|....*....|....*.
gi 1604804596 1727 AEQERDELADEISNSASGKSSLLEEK 1752
Cdd:cd06503 104 IEQEKEKALAELRKEVADLAVEAAEK 129
|
|
| |
