|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1928 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 1451.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 848 TRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDL 927
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLCEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 928 EARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDR 1007
Cdd:pfam01576 81 EARLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKMEEDILLLEDQNNKLQKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1008 IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLAR 1087
Cdd:pfam01576 161 ISEFTSNLAEEEEKSKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLEGESSDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1088 KEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 1167
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNAALKKLRELEAQLSELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1168 LRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAK 1247
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1248 QDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEE 1327
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQSRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1328 TRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQR 1407
Cdd:pfam01576 481 TRQKLNLSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALTQR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1408 FDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALS 1487
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETKALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1488 LSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEV 1567
Cdd:pfam01576 641 LARALEEALDAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1568 NMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQL 1647
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIEAANKGRDEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1648 KKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSAL 1727
Cdd:pfam01576 801 KKLQAQMKDLQRELDEARASRDEIFAQSKESEKKLKSLEAELLQLQEDLAAAERARRQAQQERDELAEEIASGNSGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1728 LDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDST 1807
Cdd:pfam01576 881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1808 MRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLE 1887
Cdd:pfam01576 961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKGNSRLKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1785379715 1888 EAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAEAMNREVTTLRSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1442.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1785379715 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-771 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1313.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRK-EHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKeSGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGF-NQYRFLSNGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDpSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 337 GFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 417 ADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPK-FQKPRQLRDKADL 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmgEMSFGSSYKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1785379715 736 IPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1237.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAP----GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 415 EQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKAD 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 575 LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGsSYKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379715 735 AIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1196.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHtapGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1785379715 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1187.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1785379715 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1173.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHT----APGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 415 EQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKAD 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 575 LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSfgSSYKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP--GAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379715 735 AIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1166.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQdREIFQETMESMKIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADLCII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSsyKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1785379715 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1155.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASShKGRKEHTAP----------GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPhpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 249 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQE 328
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 329 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 408
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 409 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 489 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKpRQ 568
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 569 LRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrIVGLDQvSGMGEMSFGSsyKTKKG 648
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGA--RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 649 MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379715 729 EILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-771 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 Cd Length: 674 Bit Score: 1108.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEhtapGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV----GRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 247 RINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREI 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 326 FQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 486 LFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 566 PRQlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMsfgsSYKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST----PKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 646 KKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379715 726 QRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-783 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1014.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 80 NPPKFTKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 160 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkehtapGELEHQLLQANPILEAFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 240 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IP 318
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLtVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 319 GQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNT-AAQKLCHLLGLNVTEFSRAIL 397
Cdd:smart00242 235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 398 MPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 478 YTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQEL 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 558 GNHPKFQKPRQlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgem 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 638 sfGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 534 --GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 718 RIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
35-1245 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 929.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 35 QVWVPSEKHGFEAASIKEERGEEVIVELA---ENGKRVPVAKDDIQ--KMNPPKFTKVEDMAELTCLNEASVLHNLKDRY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 110 YSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGESGAGKTENTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 190 KVIQYLAHVASSHkgrkeHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKS 269
Cdd:COG5022 171 RIMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 270 RAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IPGQQDREIFQETMESMKIMGFNHEEIMSMLK 348
Cdd:COG5022 246 RVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 349 MVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKAL 428
Cdd:COG5022 326 ILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKAL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 429 YERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNF 508
Cdd:COG5022 405 YSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 509 IDFgLDLQPCIDLIERpANPPGVLSLLDEECWFPKATDKSFVEKVIQEL--GNHPKFQKPRQLRDKadLCIIHYAGKVDY 586
Cdd:COG5022 484 IDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQRLnkNSNPKFKKSRFRDNK--FVVKHYAGDVEY 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 587 KADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVgldqvsgmgemsfgssyktKKGMFRTVGQLYKESLSKLMS 666
Cdd:COG5022 560 DVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMS 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 667 TLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMD 742
Cdd:COG5022 621 TLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKED 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 743 GKQACAIMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIVFFQAAARGYLARRAFYKKQQQMSALKVVQRN 822
Cdd:COG5022 701 TKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHG 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 823 CAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKvvelqkvkdtqvkteselKEMANKYQQLFEEKSILAEQLQAETEL 902
Cdd:COG5022 781 FRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSY------------------LACIIKLQKTIKREKKLRETEEVEFSL 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 903 FAEAEEMRARLASKKQELEEILHDLEARVEEeeertlqLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKK 982
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKKETIYLQS-------AQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSL 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 983 MEEDILLLEDQNAKLAKERKLLDDR-IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLD 1061
Cdd:COG5022 916 SSDLIENLEFKTELIARLKKLLNNIdLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1062 GETTDLQDQLLELQQQIEELKQ--QLARKEEELQAALARV---DDEVGQKNNLLKQLRDLQSQLAELhedlesekAARAK 1136
Cdd:COG5022 996 NFKKELAELSKQYGALQESTKQlkELPVEVAELQSASKIIsseSTELSILKPLQKLKGLLLLENNQL--------QARYK 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1137 AEKQRRDLGEELEALKTELEDT--LDSTAAQQELRAKReqevTDLKKTIEEDVKVRDAQVTemrqrhNQVVEEISEQLEQ 1214
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTN----RNLVKPANVLQFIVAQMIK------LNLLQEISKFLSQ 1137
|
1210 1220 1230
....*....|....*....|....*....|...
gi 1785379715 1215 ArrfKGNLEKVKQTLESENTDL--IKEVKNLQA 1245
Cdd:COG5022 1138 L---VNTLEPVFQKLSVLQLELdgLFWEANLEA 1167
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-771 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 Cd Length: 633 Bit Score: 859.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL-----SNGNLPIPGQQDREIFQETMES 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFeeDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 490 TMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQL 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 570 RDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkdvdrivgldqvsgmgemsfgssyktkkgm 649
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 650 frtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1785379715 730 ILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 773.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAP------GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFlatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 253 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKtDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETM 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 331 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 491 MFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPR-- 567
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYdNHLGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 568 -QLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQVsgmGEMSFGSSYKTK 646
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---EDPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 647 KGM-FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379715 726 QRYEILTPNAIPK-GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 768.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSH--KGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYR--FLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 415 EQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDKA 573
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 574 D--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvSGMGEMSFGSSYKTKKGMFR 651
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA--------TADADSGKKKVAKKKGSSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14913 548 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1785379715 732 TPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 628 NASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 760.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLL-EGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 418 DFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLR---DKA 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTnTHLGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivGLDQVSGMGEMSFGSsyKTKKGMFRTV 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAKGGR--GKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 654 GQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 1785379715 734 NAIpKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 729.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASShkGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAG-EHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 418 DFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK---A 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYdNHLGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgEMSFGSSYKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379715 733 PNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-771 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 725.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGrkEHtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ET----QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IPGQQDREIFQETMESMKIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 418 DFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 497 EEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPK--FQKPRqLRDKAD 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR-FSNTAF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 575 LcIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKytaelwkdvdrivgldqvsgmgemsfgssyktKKgmfrTVG 654
Cdd:cd01380 471 I-VKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KK----TVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379715 735 AIPKGfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 594 KEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 707.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHtapGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14929 238 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 419 FAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd14929 318 YAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 499 YQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK--ADL 575
Cdd:cd14929 397 YRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKfeAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKdvdrivglDQVSGMGEMSFGSSYKTKKGMFRTVGQ 655
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------NYISTDSAIQFGEKKRKKGASFQTVAS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14929 546 LHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRT 625
|
650 660 670
....*....|....*....|....*....|....*..
gi 1785379715 736 IPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 626 FPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 706.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE--LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 415 EQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK- 572
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 573 -ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQV--SGMGEMSFGSSyktkkgm 649
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPieKGKGKAKKGSS------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 650 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14917 546 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 625
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379715 730 ILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 626 ILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-771 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 181 GAGKTENTKKVIQYLAHVASSHKGRKEHTAP--GELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDL-IEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 337 GFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 416 QADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDKAD 574
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 575 --LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqVSGMGEMSFGSSYKTKKGMFRT 652
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14918 549 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379715 733 PNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 629 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 687.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE----LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESM 333
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPEL-IEMLLITTNpyDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 334 KIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 493 VLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRD 571
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 572 KAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGldQVSGMGEMSFGssyKTKKGM 649
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--ASAGGGAKKGG---KKKGSS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 650 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14912 551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379715 730 ILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 631 VLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 687.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKE--HTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNTA-AQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQT 413
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 414 KEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK 572
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 573 --ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSyktkkgmF 650
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-------F 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 651 RTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1785379715 731 LTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 682.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE----LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETMESM 333
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDL-IEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 334 KIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 493 VLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRD 571
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 572 K--ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqVSGMGEMSFGSSYKTKKG- 648
Cdd:cd14910 476 KveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGKKKGs 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 649 MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14910 548 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1785379715 729 EILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 628 KVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 681.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTA---PGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYR--FLSNGNLPIPGQQDREIFQETMESMK 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQT 413
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 414 KEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRDK 572
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 573 AD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQVSGMGEMSFGssyKTKKGMF 650
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 651 RTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1785379715 731 LTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 674.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE----LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYRF--LSNGNLPIPGQQDREIFQETMESM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 334 KIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 493 VLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLRD 571
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 572 KAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIvgldQVSGMGEMSFGssyKTKKGM 649
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTA----EAEGGGGKKGG---KKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 650 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379715 730 ILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-771 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 655.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKgrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 337 GFNHEEIMSMLKMVSAVLQFGNIVFRK-ERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 496 QEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKADL 575
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrIVGLDQVSGMGEMSfGSSYKTKKGMfRTVGQ 655
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGTSKGK-PTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 1785379715 736 IPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 626 RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-771 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 648.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRgkKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGrkehtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 NHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 419 FAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 499 YQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPrqlRDKAdLCII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSsyktkkgMFRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS-------QKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 659 ESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 1785379715 739 GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-771 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 644.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTapgelEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERV-----KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 NHEEIMSMLKMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVG---RDYVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFnhTMFVL- 494
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IELTLk 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 495 -EQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLSLLDEECWFP-KATDKSFVEKVIQELGNHPKFQKPRQLRDK 572
Cdd:cd01378 394 aEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 573 ADLC--IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmgemsfgssyKTKKGMF 650
Cdd:cd01378 471 RRGEfrIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRP 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 651 RTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd01378 532 PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKL 611
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1785379715 731 LTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 612 LSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-771 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 614.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKgrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRK--ERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDK 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 573 AdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgEMSFGSSYKTKKgmfRT 652
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE--------------DISMGSETRKKS---PT 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379715 733 PNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-771 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 613.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVAsshkGRKE-HTAPgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 256
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVtEGRS--VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETMESMKI 335
Cdd:cd01384 155 SGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKL---CHLLGLNVTEFSRAiLMPRIKVGRD-YVQKA 411
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIVTPDgIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 412 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 492 FVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRqlRD 571
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 572 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmGEMSfgSSYKtkkgmFR 651
Cdd:cd01384 468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR----------EGTS--SSSK-----FS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd01384 531 SIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379715 732 TPNAiPKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 611 APEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-771 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 574.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASSHKGrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLegfnqyrflsngnlpIPGQQDREIFQETMESMKIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNT-------DQASMPDNTAAQKlchLLGLNVTEF-----SRAILMPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 486 LFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 566 PRQ--------LRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGldqvsgmgem 637
Cdd:cd01382 450 PRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 638 sfGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 520 --DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 718 RIVFQEFRQRYEILTPNAIPKgfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-771 |
1.01e-179 |
|
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: 559.78 E-value: 1.01e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGrkehtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGfnQYRFLSNGN-LPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCH---LLGLNVTEFSRAILMPRIKV-GRDYVQKAQT 413
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 414 KEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKA 573
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdvdrivgldqvsgmgEMSFGSSyKTKKGmfrTV 653
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF----------------PPSEGDQ-KTSKV---TL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 654 GQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtP 733
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-V 605
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379715 734 NAIPKGFM-DGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 606 KTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
1.14e-176 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 552.46 E-value: 1.14e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEH----------TAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 244 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDR 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 324 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmpDNTAAQKLCH---LLGLNVTEFSRAILMPR 400
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 401 IKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 480
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 481 EKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLSLLDeECWFPKAT--DKSFVEKVIQEL 557
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 558 G-------------NHPKFQKPRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkytaelwkdvdr 624
Cdd:cd14890 476 GrksgsggtrrgssQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 625 ivgldqvSGMGEMSFGSSYKTkkgmfrtvgqlykeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGV 704
Cdd:cd14890 542 -------RSIREVSVGAQFRT--------------QLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379715 705 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
8.05e-174 |
|
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: 544.35 E-value: 8.05e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASShkgrkehtAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR--------RNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNG-NLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQ---ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 415 EQADFAVEALAKALYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVL 494
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQlrDKAD 574
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 575 LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgLDQVSGMGEMSFGSSYKTKKGMFRTVG 654
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFVTMKPRTPTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 655 QLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*...
gi 1785379715 735 AIPKGfMDGKQACAIMIRALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 621 KLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
2.95e-168 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 529.35 E-value: 2.95e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVAsshkgrkehtapGELEH----QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 254 GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgeHMKTDLLLEGFNQYRFL-SNGNLPIPGQQDREIFQETMES 332
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASM--PDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 491 MFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKVIqelGNHPKFQK----P 566
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 567 RQlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrIVGLDQVSGMGEMSFGSSYKTK 646
Cdd:cd14903 459 RT--SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 647 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14903 534 ALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379715 727 RYEILTPNAiPKGFMDGKQACAIMIRALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 614 KFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
1.42e-167 |
|
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: 528.87 E-value: 1.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLahVASSHKGrkehTAPGeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG----YGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKER-NTDQASMPDNTAAQKL-CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 416 QADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 492 FVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPrQLRD 571
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 572 KAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdriVGLDQV-------------------- 631
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 632 SGM----------------GEMSFGSSYKTKKGMfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLV 695
Cdd:cd01385 541 AGRrraqrtaghsltlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 696 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
1.94e-165 |
|
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: 521.66 E-value: 1.94e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMY------RGKKRHEIPPHIYAISETAYRSMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 249 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPI--PGQQDREIF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrrDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 327 QETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-RKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 485 QLFNHTMFVLEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 561 PKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfg 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 641 ssyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1785379715 721 FQEFRQRYEILTPNAIPKGFMDGKQACAIMIRA------LELDPNLYrIGQSKIF 769
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
1.32e-163 |
|
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: 515.78 E-value: 1.32e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKK-RHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASShkgrkehtAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQD-------REIFQETM 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 331 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 487 FNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 567 rqLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdvdrivgldqvsgmgemsfgSSYktk 646
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------------------TSY--- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 647 kgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14897 524 ----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379715 727 RYEILTPNAiPKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-733 |
4.39e-163 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 515.78 E-value: 4.39e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRgKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEhtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD------ 251
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 252 ---VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP------------ 316
Cdd:cd14888 155 msgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 317 ------------IPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKL--- 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 382 CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 542 PKATDKSFVEKVIQELGNHPKFQKPRQlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 622 -VDRIVGLdqvsgmgemsfgssyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLR 700
Cdd:cd14888 550 yLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|...
gi 1785379715 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-771 |
4.56e-163 |
|
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: 514.13 E-value: 4.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASShkgrkehtAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA--------NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTD---LLLEGFNQYRFLSNGNLPIPGQQD--REIFQETMESMK 334
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSgnREKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFR---KERNTDQASM-PDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 488
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 489 HTMFVLEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPkFQKPR 567
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 568 qlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfgssyktkk 647
Cdd:cd01379 469 --SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 648 gmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 727
Cdd:cd01379 517 ----TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKR 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1785379715 728 YEILTPNAIPKGFMDgKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 593 YYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
1.18e-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: 511.26 E-value: 1.18e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 337 GFNHEEIMSMLKMVSAVLQFGNIVFrkeRNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQ 416
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 417 ADFAVEALAKALYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 496 QEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDkaDL 575
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvSGMGEMSFGSSYKTKKgmfRTVGQ 655
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR---PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 1785379715 736 IPKGFMDGKqaCAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
2.85e-160 |
|
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: 507.76 E-value: 2.85e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEI---PPHIYAISETAYRSMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 172 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 248 INFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 327 QETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFrkERNTDQ----ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 403 VGRDYV-QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFELNSFE 472
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 473 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFP-KATDKSFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 552 KVIQE-LGNHPKFQKPrqlRDKADLCII-HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkdvdrivgld 629
Cdd:cd14892 476 IYHQThLDKHPHYAKP---RFECDEFVLrHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 630 qvsgmgemsfgssyktkkgmFRTvgqlykeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 709
Cdd:cd14892 536 --------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVR 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379715 710 ICRQGFPNRIVFQEFRQRYEIL---------TPNAIPkGFMDGKQACAIMIRALEldPNLYRIGQSKIFFR 771
Cdd:cd14892 589 IRREGFPIRRQFEEFYEKFWPLarnkagvaaSPDACD-ATTARKKCEEIVARALE--RENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-731 |
1.16e-147 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 471.71 E-value: 1.16e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY-----------RGKKRHEIPPHIYAISETAYRSM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHvASSHKGRKEHTAPGELE---HQLLQANPILEAFGNAKTVKNDNSS 240
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ-AGDNNLAASVSMGKSTSgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 241 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhmktdlllegfnqyrflsngnlpipGQ 320
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------------AA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 321 QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD-QASMPDNTAAQKL------CHLLGLNVTEFS 393
Cdd:cd14900 216 RKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 394 RAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEIFELN 469
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 470 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSF 549
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 550 VEKVIQELGNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSTdkytaelwkdVDrivgld 629
Cdd:cd14900 453 ASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD------ 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 630 qvsgmgemsfgssyktkkgMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 709
Cdd:cd14900 509 -------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVR 568
|
650 660
....*....|....*....|..
gi 1785379715 710 ICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14900 569 VARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
1.68e-142 |
|
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: 458.60 E-value: 1.68e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 257 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHMKTDLLLEGFnqYRFLSN--GNLPIPgQQDREIFQETMES 332
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNgaGCKREV-QYWKKKYDEVCNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVFrkERNTDQASMPDNTAAQKL---CHLLGLNVTEFSRAILMPRIKVGRDYVQ 409
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKTLTCTVTFTRGEQIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 410 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14889 308 RHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 488 NHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPR 567
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 568 qlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWK-DVDRIVGLDQVSGM---GEMSFGSSY 643
Cdd:cd14889 465 --SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLpqaGSDNFNSTR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 644 KtkkgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14889 543 K------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1785379715 724 FRQRYEIL--TPNaIPKgfmdGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 617 FAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
4.74e-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: 454.87 E-value: 4.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH--------EIPPHIYAISETAYRSMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE-----------LEHQLLQANPILEAFGNAKTVKNDN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 239 SSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEG---FNQYRFLS-NG 313
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 314 NLPIPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGLNVTE 391
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 392 FSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 464
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 465 IFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLSLLDEECWFP 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 543 KATDKSFVEKVIQELGNHPKFQKPRQLRdKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdv 622
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 623 driVGLDQVSGMGEMSFGSSYKTKKgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCN 702
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 1785379715 703 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
7.64e-138 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 445.54 E-value: 7.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASshkGRKEHTAPgelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL--SNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 336 MGFNHEEIMSMLKMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKE 415
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 416 QADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLE 495
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 496 QEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKV---IQELGNHPKFQKPRQLRDK 572
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 573 adLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvsGMGEMSFGSSYKTKKGMfRT 652
Cdd:cd14904 468 --FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 653 VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14904 536 LGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379715 733 PNAIPKGfmDGKQACAIMIRAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 616 PPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
1.28e-137 |
|
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: 444.49 E-value: 1.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiytEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 172 QSILCTGESGAGKTENTKKVIQYLAH------------VASSHKGRKEHTApgELEHQLLQANPILEAFGNAKTVKNDNS 239
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTravggkkasgqdIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 240 SRFGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPI- 317
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 318 PGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRK----ERNTDQASMPDNTAAQKLCHLLGLNVTEFS 393
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 394 RAILMPRIkVGRDYVQKAQ-TKEQADFAVEALAKALYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSF 471
Cdd:cd14891 314 KVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 472 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVE 551
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 552 KVIQELGNHPKFQKPRQlRDKADLCII-HYAGKVDYKADEWLMKNMDPLNDNVATLLHQStdkytaelwkdvdrivgldq 630
Cdd:cd14891 469 TLHKTHKRHPCFPRPHP-KDMREMFIVkHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 631 vsgmgemsfgssyktkkgmfrtvgQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRI 710
Cdd:cd14891 528 ------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 711 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 584 LKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-771 |
4.65e-135 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 438.57 E-value: 4.65e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR--GKKRHE-------IPPHIYAISETAYRSMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE---LEHQLLQANPILEAFGNAKTVKNDNSSRFGKF 245
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 246 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HMKTDLLLEGFNQYRFLSNGNLPI 317
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 318 PGQ-QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNtDQASMPDNTAAQK----LCHLLGLNVTEF 392
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 393 SRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIFELNS 470
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 471 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFP-KATDKSF 549
Cdd:cd14908 399 FEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 550 VEKVI--------QELGNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqstdkytaelwk 620
Cdd:cd14908 476 ASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 621 dvdrivgldqvsgmgemsfgssyKTKKGMFRTvGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLR 700
Cdd:cd14908 536 -----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLR 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPKGFM-------DGKQACA--------------IMIRALELDPN 759
Cdd:cd14908 592 YGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVkkmckdlvkgvlspAMVSMKNIPED 670
|
730
....*....|..
gi 1785379715 760 LYRIGQSKIFFR 771
Cdd:cd14908 671 TMQLGKSKVFMR 682
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
2.68e-134 |
|
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: 434.98 E-value: 2.68e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHV---ASSHKGRkehtapgelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGY 255
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLyqdQTEDRLR-----------QPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNL-PIPGQQDREIFQETMESMK 334
Cdd:cd14896 149 IVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 335 IMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQ--ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQ 412
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd14896 309 PVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 492 FVLEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQlrD 571
Cdd:cd14896 389 LAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--P 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 572 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQvsgmgemsfGSSyktkkgmfr 651
Cdd:cd14896 464 LPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQ---------GKP--------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14896 526 TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379715 732 TpNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 606 G-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-824 |
2.79e-134 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 441.39 E-value: 2.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEI-PPHIYAISETAYRSMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTApgelehqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNA-------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 336 MGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASM--PDNTAA-QKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 491 MFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFqKPRQLR 570
Cdd:PTZ00014 500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKY-KPAKVD 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 571 DKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqvsgmgEMSFGssyKTKKGMF 650
Cdd:PTZ00014 576 SNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV-------------EVEKG---KLAKGQL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 651 rtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:PTZ00014 640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 731 LTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIVFFQAAARGYLARRAFy 807
Cdd:PTZ00014 718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKV- 796
|
730
....*....|....*..
gi 1785379715 808 kkqqqMSALKVVQRNCA 824
Cdd:PTZ00014 797 -----RKNIKSLVRIQA 808
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-771 |
1.78e-132 |
|
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: 432.07 E-value: 1.78e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyteqivEMYRGKKRHE-------IPPHIYAISETAYRSMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKEHTAPGElehQLLQANPILEAFGNAKTVKNDNSSR 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 242 FGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFN--QYRFLSNGN 314
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 315 LPI--PGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD---------------QASMPDNTA 377
Cdd:cd14895 232 CYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 378 AQKL---CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTK------ 448
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 449 ----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 524
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 525 pANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRqlRDKADLC--IIHYAGKVDYKADEWLMKNMDPLNDN 602
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADVAfqIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 603 VATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGmfrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPN 682
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 683 HEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELdpnlyr 762
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------ 696
|
....*....
gi 1785379715 763 iGQSKIFFR 771
Cdd:cd14895 697 -GKTRVFLR 704
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-733 |
2.75e-130 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 426.62 E-value: 2.75e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYR--------GKKRHEIPPHIYAISETAYRSMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 169 REDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 248 INFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL-----SNGNLPIPGQQD 322
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygpSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 323 REIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKE-RNTDQASMPDNTAAQ--KLCHLLGLNVTEFSRAILMP 399
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 400 RIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEIFELNSF 471
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 472 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVE 551
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 552 KVIQELGNHPKFqkprqlrdkadlCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkDVDRIVGLDQV 631
Cdd:cd14902 478 KFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 632 SGMGEMSFGSSYKTKKGMFRT--VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIR 709
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660
....*....|....*....|....
gi 1785379715 710 ICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
2.59e-126 |
|
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: 412.84 E-value: 2.59e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApgelehqLLQANPILEAFGNAKTVKNDNSSRFGKFIRInfDVA--GY 255
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQTA-------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQL--DVAseGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 256 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKI 335
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 336 MGFNHEEIMSMLKMVSAVLQFGNIVFRKErntDQASMPDntAA----------QKLCHLLGLNVTEFSRAILMPRIKVGR 405
Cdd:cd14876 232 MGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 406 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 485 QLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFq 564
Cdd:cd14876 385 KNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 565 KPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqvsgmgEMSFGssyK 644
Cdd:cd14876 461 KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV-------------VVEKG---K 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 645 TKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 724
Cdd:cd14876 525 IAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379715 725 RQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIF 769
Cdd:cd14876 603 LYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
3.51e-124 |
|
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: 408.24 E-value: 3.51e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRkehtapgeLEHQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV--------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNqyrflSNGNLPIPGQQDREIFQETM------- 330
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLA-----ESNSFGIVPLQKPEDKQKAAaafsklq 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 331 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMP----------- 399
Cdd:cd01386 228 AAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHhlsggpqqstt 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 400 -RIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN------SFE 472
Cdd:cd01386 308 sSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 473 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLSLLDEECW 540
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 541 FPKATDKSFVEKVIQELG--NHPKFQKPRQLRDKADLCII-HYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQSTDKY 614
Cdd:cd01386 467 YPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPLQFVLgHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 615 TAelwkdvdrivgldqvsgmgemsfgssyKTKKGMFRTVgqlyKESLSKLMSTLRNTNPNFVRCIIPNHE------KKAG 688
Cdd:cd01386 547 AA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 689 KLEPHLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACAIMIRALELD 757
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 1785379715 758 PNLYRIGQSKIFFR 771
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-733 |
4.94e-119 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 392.29 E-value: 4.94e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEIPPHIYAISETAYRSMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSN--GNLpipgqqDREIFQETMES 332
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNpeRNL------EEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 333 MKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTA---AQKLCHLLGLNVTEFSRAILMPRIKVGRDYV- 408
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 409 -QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14880 315 fKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 488 NHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQE-LGNHPKFQKP 566
Cdd:cd14880 395 VAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESaLAGNPCLGHN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 567 RqLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGmgemsfgssykTK 646
Cdd:cd14880 472 K-LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG-----------QS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 647 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14880 540 RAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVE 619
|
....*..
gi 1785379715 727 RYEILTP 733
Cdd:cd14880 620 RYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
1.64e-116 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 387.03 E-value: 1.64e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEIPPHIYAISETAYRSMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 177 TGESGAGKTENTKKVIQYLAHVASSHKGRKEH--TAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 255 YIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEG-FNQYRFL--------------SNGNLPI 317
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 318 PGQQDR-EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQAS--MPDNTAA-QKLCHLLGLNVTEFS 393
Cdd:cd14906 241 NNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 394 RAILMPRIKV-GRDYVQ-KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDR----------TKRQGASFIGILDIA 461
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWF 541
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 542 PKATDKSFVEKVIQELGNHPKFQKpRQLrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkd 621
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL--- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 622 vdrivgldqvSGMGEMSFGSSYKTKKGMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRC 701
Cdd:cd14906 553 ----------FQQQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
|
650 660 670
....*....|....*....|....*....|...
gi 1785379715 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
1.22e-112 |
|
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: 373.84 E-value: 1.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH-----EIPPHIYAISETAYRSMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 173 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkehTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHS--------TSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 253 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETME 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKcYDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 332 SMKIMgFNHEEIMSMLKMVSAVLQFGNIVFRKERN--TDQASMPDNTAA-QKLCHLLGLNVTEFSRAILMPRIKVGRDYV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 409 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINYANERLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 486 LFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHpkfqk 565
Cdd:cd14886 388 YFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCKSKIKNN----- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 566 pRQLRDKADLC---IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLdqvsgmgemsfgss 642
Cdd:cd14886 460 -SFIPGKGSQCnftIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 643 yktKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd14886 525 ---MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1785379715 723 EFRQRYEILT--PNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 600 EFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
1.57e-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: 1.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRG-KKRHEIPPHIYAISETAYRSM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 176 CTGESGAGKTENTKKVIQYLAHVASSHKGR-KEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VA 253
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 254 GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDL-LLEGFNQYRFLSNGNL----PIPGQ--QDREIF 326
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 327 QETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGLNVTEFSRAILmprIKVGRD 406
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 407 YVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 486 LFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNH----- 560
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKspyfv 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 561 -PKFQKPRQLRdkadlcIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdrivgldqvsgmgemsf 639
Cdd:cd14875 474 lPKSTIPNQFG------VNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL--------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 640 gssYKTKKGMFR---TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 716
Cdd:cd14875 527 ---LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYP 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 717 NRIVFQEFRQRYEILTPNAIPKGFMDGK---QACAIMIRALEL----DPNlYRIGQSKIFFR 771
Cdd:cd14875 604 VRRPIEQFCRYFYLIMPRSTASLFKQEKyseAAKDFLAYYQRLygwaKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
1.62e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 355.56 E-value: 1.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY----------RGKKRHEIPPHIYAISETAYRSMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 168 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPGE---------LEHQLLQANPILEAFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 239 SSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG----AGEHMKTDLLLEGFNQYRFLSNG 313
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 314 NLPIP---GQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-----RKERNT--DQASMPDNTAA----- 378
Cdd:cd14899 241 SLCSKrrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 379 QKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRT----------- 447
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 448 ---KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIER 524
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 525 paNPPGVLSLLDEECWFPKATDKSFVEKVIQEL---GNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLND 601
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 602 NVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIP 681
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379715 682 NHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
2.84e-102 |
|
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: 346.25 E-value: 2.84e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 251 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLlegfnqyrflsngnlpiPGQQDREIFQ--- 327
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTDlrr 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 328 --ETMESMKIMGFNHEEImsmLKMVSAVLQFGNIVFRKERNTDQASMPDNTA--------AQKLCHLL-------GLNVT 390
Cdd:cd14887 220 itAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 391 EFSRAIL--------MPRIKVGRDYV------------QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKR- 449
Cdd:cd14887 297 EASRKHLktvarllgLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKp 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 450 ------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFI--DFG 512
Cdd:cd14887 377 sesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 513 LDLQPCIDLIERPAN---------------------PPGVLSLLDE------ECWFPKATDKSFVEKVIQELGNHPKFQK 565
Cdd:cd14887 457 FSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 566 --PRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKYTaelwkdvdRIVGLDQVSGMgemsfgSSY 643
Cdd:cd14887 537 itPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV------RAI 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 644 KTKKgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14887 602 SSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVE 678
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1785379715 724 FRQRYEILTPNAIpKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 679 LWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
8.19e-100 |
|
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: 334.17 E-value: 8.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYTEQIVEMYRGKKRHeIPPHIYAISETAYRSMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAhvasshkgrkEHTAPGE-LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvaGYIVG 258
Cdd:cd14898 78 SGSGKTENAKLVIKYLV----------ERTASTTsIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDlllegFNQYRF-LSNGNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14898 146 AKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMKSLGIAN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FnhEEIMSMLKmvsAVLQFGNIVFRKERNTDQASmpdNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14898 221 F--KSIEDCLL---GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 418 DFAVEALAKALYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14898 293 RTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 498 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKvIQELGNHpkfqkprQLRDKADLCI 577
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVK-IKKYLNG-------FINTKARDKI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 578 I--HYAGKVDYKADEWLMKNMDplndnvatllhqstdkytaelwkdvdrivgldqvsGMGEMSFGSSYKTKKGMFRTVGQ 655
Cdd:cd14898 438 KvsHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDEGSKEDLVK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 656 LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14898 483 YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
8.74e-95 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 321.81 E-value: 8.74e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYTEQIVEMYR-------GKKRHEIPPHIYAISETAYRSM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKehtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGK 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 245 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNL----PIPGQ 320
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGChplpLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 321 QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFR--KERNTDQASMpDNTAA-QKLCHLLGLNVTEFsRAIL 397
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 398 MPRIK-VGRD----YVQKAQTKEQADfaveALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIF---ELN 469
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 470 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLSLLDEEC-WFPKATDKS 548
Cdd:cd14879 386 SLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKTDEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 549 FVEKVIQELGNHPKF---QKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhqstdkytaelwkdvdri 625
Cdd:cd14879 463 MLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 626 vgldqvsgmgemsfgssyktkkgmfRTVGQLyKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVL 705
Cdd:cd14879 525 -------------------------RGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379715 706 EGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACAIMIRALELDPNLYRIGQSKIFF 770
Cdd:cd14879 579 ELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
7.53e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 313.68 E-value: 7.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR---GKKRHEIPPHIYAISETAYRSMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkehtapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 255 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGnlpIPGQ-------QDREIFQ 327
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT---MREDvstaersLNREKLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 328 ETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDY 407
Cdd:cd14878 230 VLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 408 VQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14878 310 IIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 485 QLFNHTMFVLEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLSLLDEECWFPKATDKSFVEKV 553
Cdd:cd14878 390 HYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 554 --IQELGNHPKFQKPRQ-------LRDK-ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvd 623
Cdd:cd14878 457 qsLLESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL----- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 624 rivgldqvsgmgemsFGSSYKTkkgmfrTVGQLYKeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNG 703
Cdd:cd14878 532 ---------------FQSKLVT------IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIG 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379715 704 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14878 590 VLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
1.67e-91 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 311.95 E-value: 1.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQivemYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAhvasshKGRKEHTapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIMGF 338
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 339 nHEEIMSMLKMVSAVLQFGNIVFR---KERNTDQASMPDNT--AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQT 413
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 414 KEQADFAVEALAKALYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFV 493
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 494 LEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRDKa 573
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 574 DLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMgemsfgsSYKtkkgmfrtv 653
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLI-------TFK--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 654 gqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 1785379715 734 NAIPKGFMDGKQACAIMIRAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
5.96e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 273.71 E-value: 5.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHE-------IPPHIYAISETAYRSMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKEHTapgELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT---ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 251 D---------VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHMKTDLLLEGFNQYRFLSN-------- 312
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 313 --GNLPIPG----------QQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKerntdqasmpdntaaqk 380
Cdd:cd14884 234 vkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 381 LCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 453 ---SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERpanpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 530 gVLSLLDE-----ECWFPKATDKSFV-----EKVIQELGNH------PKFQK---PRQLRDKADLCIIHYAGKVDYKADE 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 591 WLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfgSSYKTKKGMFRTVGQLYKESLSKLMSTLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1785379715 671 TNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-758 |
1.21e-76 |
|
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: 268.52 E-value: 1.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyteqiveMYRGKKRHEIPPHIYA-------ISETAYRSMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 173 SILCTGESGAGKTENTKKVIQYLAHVASshkGRKEHTApgeLEHqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdV 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG---GGPETDA---FKH-LAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 253 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETM 330
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 331 ESMKIMGFNHEEIMSMLkmvSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 410
Cdd:cd14881 222 ACLGILGIPFLDVVRVL---AAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 411 AQTKEQADFAVEALAKALYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFELNSFEQLCINYTNEK 482
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 483 LQQLFNHTMFVLEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLSLLDEECwFPKATDKSFVEKVIQELGNHP 561
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 562 KFQKPRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkytaelwkdvdrivgldqvsgmgeMSFGs 641
Cdd:cd14881 450 RLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-------------------------CNFG- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 642 syktkkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14881 503 --------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
650 660 670
....*....|....*....|....*....|....*....
gi 1785379715 722 QEFRQRYEILTPNAIPKGFMDGKQACA--IMIRALELDP 758
Cdd:cd14881 575 KAFNARYRLLAPFRLLRRVEEKALEDCalILQFLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-724 |
4.17e-73 |
|
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: 259.25 E-value: 4.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYrgKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAhvaSSHKGRKEHtapgeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 258
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSKY-----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 259 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSN-GNLPIPGQQDREIFQETMESMKIMG 337
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 338 FNHEEIMSMLKMVSAVLQFGNIVFRKERNtdQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAqtkeqa 417
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 418 dfavEALAKALYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQE 497
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 498 EYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKF-QKPRQLRdkadl 575
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNKFG----- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 576 cIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKY-------------TAELWKDVD----------RIV------ 626
Cdd:cd14905 446 -IEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakksplSIVkvllsc 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 627 ------------------GLDQVSGMGEMSFGSSYKTKKGMFRTVGQlykeslsklmstlRNTNPNFVRCIIPNHEKKAG 688
Cdd:cd14905 525 gsnnpnnvnnpnnnsgggGGGGNSGGGSGSGGSTYTTYSSTNKAINN-------------SNCDFHFIRCIKPNSKKTHL 591
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379715 689 KLEPHLVLDQLRCNGVLEGIRICRQGFP----NRIVFQEF 724
Cdd:cd14905 592 TFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-736 |
4.22e-70 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 249.02 E-value: 4.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYrgkkrheippHIYAISETAYRSMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApgelehqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSA----------IESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 258 GANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETMESMKIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 337 GFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD---QASMPDNTAAQK-LCHLLGLNVTEFSrAILMPRIKVGrdyvqKAQ 412
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDG-----TTI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 413 TKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 493 VLEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQlRD 571
Cdd:cd14874 372 HDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 572 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdrivgldqvsgmgemsFGSSYKTKKGMFR 651
Cdd:cd14874 449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESYSSNTSDMIV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 652 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14874 509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
....*
gi 1785379715 732 TPNAI 736
Cdd:cd14874 589 LPGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-729 |
8.91e-66 |
|
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: 239.10 E-value: 8.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYT----------EQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTpdhmqaynksREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 172 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKGRKEHTAPGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 248 INFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---MKTDLLL-EGFNQYRFLSN-----GNLPIp 318
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFAL- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 319 gqqDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-------------RKERNTDQASMPDNTAAQKL--CH 383
Cdd:cd14893 242 ---DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQSCALKDPAQILlaAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 384 LLGLNVTEFSRaILMPRIKVGRDYVQ-----KAQTKEQADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQG--- 451
Cdd:cd14893 319 LLEVEPVVLDN-YFRTRQFFSKDGNKtvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivi 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 452 -ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IEWNFIDFGLDLQPCIDL 521
Cdd:cd14893 398 nSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 522 IERPanPPGVLSLLDEECWFPKATDKSFVEKVIQ-----------ELGNHPKFQKPRQLRDKADLCII-HYAGKVDYKAD 589
Cdd:cd14893 478 FEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpNMGADTTNEYLAPSKDWRLLFIVqHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 590 EWLMKNMDPLNDNVATLLHQSTDKytaelwkdVDRIVGLDQVSGMGEMSFGSSY---KTKKGMFRTVGQLYKESLS---- 662
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAAASSEKAAKQTeerGSTSSKFRKSASSARESKNitds 627
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379715 663 ----------KLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14893 628 aatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-771 |
3.25e-65 |
|
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: 235.02 E-value: 3.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 180 SGAGKTENTKKVIQYLAHVASSHKGRKEhtapgelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATG---------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 260 NIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHMKTDLLLEGFNqYRFL--SNGNLPIPGQQDR-------EIFQE 328
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKLKYRRddpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 329 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKerNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 408
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 409 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 484 QQLFNHTMFV---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLSLLDEECwfPKATDKSFVEKVIQElgNH 560
Cdd:cd14882 387 QYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYIMDRIKE--KH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 561 PKFQKPRQlrdKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivglDQVSGMgemsfg 640
Cdd:cd14882 457 SQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 641 ssyKTKKGMFRTVgqlykeSLSKLMSTLRNTNP---NFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:cd14882 521 ---RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSY 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 718 RIVFQEFRQRYEILTPNAIPKGFMDgKQACAIMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14882 592 RIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
2.80e-59 |
|
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: 201.80 E-value: 2.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 121 FCVVINPYKNLPIYTEQIV-EMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379715 200 SSHKGRKEHTA-------PGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 255
Cdd:cd01363 81 FNGINKGETEGwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-769 |
2.72e-55 |
|
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: 207.00 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR-GKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAP---------------GELEHQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDqeednihneentdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 244 KFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDR 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 324 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNI----VFRKE----------------------RNTDQASMPDNTA 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 378 AQKL-CHLLGLNVTEFSRAILMPRIkVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 455 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLSL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 535 LDEECWFPKATDKS-FVEKVIQELGNHPKF-QKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTD 612
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 613 KYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQ----LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKA- 687
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 688 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACAIMIRALELDPNLYRIGQSK 767
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1785379715 768 IF 769
Cdd:cd14938 710 IF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1014-1885 |
2.64e-30 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 131.38 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1014 TMAEEEEKVKSLNKLrnkyEAVIADLEDRLKKEEKGRQEMEKMKRKldgETTDLQDQLLELQQQIEELKQQLARKEEELQ 1093
Cdd:COG1196 177 AERKLERTEENLERL----EDLLEELEKQLEKLERQAEKAERYQEL---KAELRELELALLLAKLKELRKELEELEEELS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1094 AALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRE 1173
Cdd:COG1196 250 RLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1174 QEVTDLKKTIEEdvkvRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQR 1253
Cdd:COG1196 330 EKIEALKEELEE----RETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKRE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1254 RKKLEQQVSEFQIRTNEsekvkfeLAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLN 1333
Cdd:COG1196 406 IESLEERLERLSERLED-------LKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQR 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1334 FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSykelefLQQRFDEKHQ 1413
Cdd:COG1196 479 LEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALEAALGNR------LQAVVVENEE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1414 INDK----LEKTR---------NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFD-------------QMLAEEKNISARY 1467
Cdd:COG1196 553 VAKKaiefLKENKagratflplDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEpavrfvlgdtlvvDDLEQARRLARKL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1468 GEERDRAEAEAREKETKALSLSRALEEAIDLKDEldRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQ 1547
Cdd:COG1196 633 RIKYRIVTLDGDLVEPSGSITGGSRNKRSSLAQK--RELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQ 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1548 IEELEDELQAiedgklrlevnmqamkaqferdLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQ 1627
Cdd:COG1196 711 LEELERQLEE----------------------LKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1628 dmesqmdsankgrdEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQ 1707
Cdd:COG1196 769 --------------SLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1708 QERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENAR 1787
Cdd:COG1196 835 EEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERL 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1788 QQMERQNKELKVKLNEMDSTMRSKYKITI-ASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNAD 1866
Cdd:COG1196 915 EELEAKLERLEVELPELEEELEEEYEDTLeTELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKE 994
|
890
....*....|....*....
gi 1785379715 1867 QFKEQLEKanirMKQLKRQ 1885
Cdd:COG1196 995 KLLEVIEE----LDKEKRE 1009
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1127-1943 |
4.16e-27 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 120.97 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1127 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQElRAKREQEVTDLKKTIEEDVKVRDaqvtemRQRHNQVVE 1206
Cdd:COG1196 170 YKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAE-KAERYQELKAELRELELALLLAK------LKELRKELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1207 EISEQLEQARR-------FKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELA 1279
Cdd:COG1196 243 ELEEELSRLEEeleelqeELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1280 EKLQKLQAELDGVSGALGSTEGKSIKLT---KDLSTVQSQLQDTQE-LLQEETRQKLNFSSRVRQLEEEKNNLMENLEEE 1355
Cdd:COG1196 323 ERLEELKEKIEALKEELEERETLLEELEqllAELEEAKEELEEKLSaLLEELEELFEALREELAELEAELAEIRNELEEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1356 ESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVD 1435
Cdd:COG1196 403 KREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1436 LDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRAleeaidlkdeldrqnkqLRAEMDD 1515
Cdd:COG1196 483 LSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALEAA-----------------LGNRLQA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1516 LVSSKDDVGKNVHELERSKRALEQQVQEMKTqIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQ----------NRDD 1585
Cdd:COG1196 546 VVVENEEVAKKAIEFLKENKAGRATFLPLDR-IKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRfvlgdtlvvdDLEQ 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1586 SNDEKKKLLFKQVREMEVELEEE--------RKQKSQILAAKKKLEmdlqDMESQMDSANKGRDEAVKQLKKLQLQFKEV 1657
Cdd:COG1196 625 ARRLARKLRIKYRIVTLDGDLVEpsgsitggSRNKRSSLAQKRELK----ELEEELAELEAQLEKLEEELKSLKNELRSL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1658 WREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMR 1737
Cdd:COG1196 701 EDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1738 ISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDStmrskykiTIA 1817
Cdd:COG1196 781 IEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEE--------ELE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1818 SLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLeeaEEEASRAN 1897
Cdd:COG1196 853 ELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKL---ERLEVELP 929
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1785379715 1898 SNRRRLQRELEDVTEsaesmnrevTTLRSRLSKLERQQRKRAPIQF 1943
Cdd:COG1196 930 ELEEELEEEYEDTLE---------TELEREIERLEEEIEALGPVNL 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1713 |
2.48e-26 |
|
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: 118.24 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 861 LQKVKD------TQVKTESELKEMANKYQQLFEEKSILaeQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE 934
Cdd:TIGR02168 188 LDRLEDilneleRQLKSLERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 935 EERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLddrigeftst 1014
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL---------- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1015 maeeEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQA 1094
Cdd:TIGR02168 336 ----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1095 ALARVDDEVGQKNNLLKQLRDlqSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtldstAAQQELRAKREQ 1174
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1175 evtdlkktiEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESEN--------------TDLIkeV 1240
Cdd:TIGR02168 484 ---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalggrlQAVV--V 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1241 KNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQklqaELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDT 1320
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK----NIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1321 QELLQE-ETRQKLNFSSRVRQLEEEKNNLMENLeeeesakaqlsrqlqalqqqlleSKKRMEDQGGMVEAMEEAKKKSyK 1399
Cdd:TIGR02168 629 DDLDNAlELAKKLRPGYRIVTLDGDLVRPGGVI-----------------------TGGSAKTNSSILERRREIEELE-E 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1400 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR 1479
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1480 EKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIE 1559
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1560 DGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLfkqvremeveleeerKQKSQILAAKKKLEMDLQDMESQMDSANKG 1639
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALL---------------NERASLEEALALLRSELEELSEELRELESK 909
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379715 1640 RDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEK-KLKSLEAELLQLQEDLAAAERAKRQAQQERDDL 1713
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
874-1593 |
3.38e-26 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 117.89 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 874 ELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQ 953
Cdd:COG1196 233 KLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 954 DLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAK----ERKLLDDRIGEFTSTMAEEEEKVKSLNKLR 1029
Cdd:COG1196 313 ELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEakeeLEEKLSALLEELEELFEALREELAELEAEL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1030 NKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDD---EVGQK 1106
Cdd:COG1196 393 AEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKElerELAEL 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1107 N----NLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTEL-----------------------EDTL 1159
Cdd:COG1196 473 QeelqRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIkvkekyetaleaalgnrlqavvvENEE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1160 DSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKE 1239
Cdd:COG1196 553 VAKKAIEFLKENKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDTLVVDDLEQARRLARKL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1240 VKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKF-ELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQ 1318
Cdd:COG1196 633 RIKYRIVTLDGDLVEPSGSITGGSRNKRSSLAQKRELkELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLE 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1319 D-------TQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAME 1391
Cdd:COG1196 713 ElerqleeLKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQ 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1392 EAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEER 1471
Cdd:COG1196 793 EELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEK 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1472 DRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVgknvhELERSKRALEQQVQEMKTQIEEL 1551
Cdd:COG1196 873 EELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERL-----EVELPELEEELEEEYEDTLETEL 947
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1785379715 1552 EDELQAIEDGKLRLE-VNMQAMkAQFERDLQNRDDSNDEKKKL 1593
Cdd:COG1196 948 EREIERLEEEIEALGpVNLRAI-EEYEEVEERYEELKSQREDL 989
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-712 |
7.69e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 116.38 E-value: 7.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 218 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDERTFHVFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 287 LLAGAGEH-----MKTDLLLEGFN--QYRFLSNGNLPIPG--------QQDREIFQETMESMKIMGFNHEEIMSMLKMVS 351
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 352 AVLQFGNIVFRKERNTDQASMPDN---TAAQKLCHLLGLNVTEFSRAILMPR---IKVGRDYVQKAQTKEQADFAVEALA 425
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 426 KALYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQqlfnh 489
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 490 tmfvleQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKAT----------DKSFVEKVIQElgN 559
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR--N 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 560 HPKFQKPRQLRDKAD-----------LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgL 628
Cdd:cd14894 636 SSRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ---L 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 629 DQVSGMGEMSFGSSYKTKKGMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGI 708
Cdd:cd14894 713 GWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQM 791
|
....
gi 1785379715 709 RICR 712
Cdd:cd14894 792 EICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
863-1687 |
1.98e-25 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 115.58 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 863 KVKDTQVKTESELKEMANKYQQLFEEKSILAEQLqaetelfaEAEEMRARLASKKQELEEILHDLEARVEEEEERtlQLQ 942
Cdd:COG1196 169 KYKERKEEAERKLERTEENLERLEDLLEELEKQL--------EKLERQAEKAERYQELKAELRELELALLLAKLK--ELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 943 NEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIgeftstmAEEEEKV 1022
Cdd:COG1196 239 KELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEI-------SLLRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1023 KSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDE 1102
Cdd:COG1196 312 EELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1103 VGQKNNllkQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKT 1182
Cdd:COG1196 392 LAEIRN---ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1183 IEEdVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENT---DLIKE-------------------- 1239
Cdd:COG1196 469 LAE-LQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGpvaELIKVkekyetaleaalgnrlqavv 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1240 VKNLQAAKQDSEQRRKKL----------EQQVSEFQIRTNESEKVKF--ELAEKLQKLQAELDGVSGALG--STEGKSIK 1305
Cdd:COG1196 548 VENEEVAKKAIEFLKENKagratflpldRIKPLRSLKSDAAPGFLGLasDLIDFDPKYEPAVRFVLGDTLvvDDLEQARR 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1306 LTKDLS------TVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAqLSRQLQALQQQLLESKKR 1379
Cdd:COG1196 628 LARKLRikyrivTLDGDLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEE-ELKSLKNELRSLEDLLEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1380 MEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQindKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1459
Cdd:COG1196 707 LRRQLEELERQLEELKRELAALEEELEQLQSRLE---ELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1460 EKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQ 1539
Cdd:COG1196 784 LEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1540 QVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQ-ILAA 1618
Cdd:COG1196 864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEyEDTL 943
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379715 1619 KKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEI--FVQSRDNEKKLKSLEA 1687
Cdd:COG1196 944 ETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLleVIEELDKEKRERFKET 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1082-1934 |
2.31e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1082 KQQLARKEEELQAALARVDDEVgqkNNLLKQLRDLQSQ------LAELHEDLESEKAARAKAEKQrrDLGEELEALKTEL 1155
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDIL---NELERQLKSLERQaekaerYKELKAELRELELALLVLRLE--ELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1156 EDTLDSTAAQQELRAKREQEVTDLKKTIEEDvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTD 1235
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1236 LIKEVKNLQAAKQDSEQRRKKLEQ---QVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLST 1312
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1313 VQSQLQDTQELLQeetrqklNFSSRVRQLEEEKNNLMENLEEEESAkaqlsrqlqalqqqllESKKRMEDQGGMVEAMEE 1392
Cdd:TIGR02168 405 LEARLERLEDRRE-------RLQQEIEELLKKLEEAELKELQAELE----------------ELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1393 AkkksykeLEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEEKNISARYGEERD 1472
Cdd:TIGR02168 462 A-------LEELREELEEAEQALDAAERELAQLQARLDSL-------ERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1473 RAEAEAReketkalsLSRALEEAidlkdeldrqnkqLRAEMDDLV-SSKDDVGKNVHELERS---KRALEQQVQEMKTQI 1548
Cdd:TIGR02168 528 LISVDEG--------YEAAIEAA-------------LGGRLQAVVvENLNAAKKAIAFLKQNelgRVTFLPLDSIKGTEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1549 EELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNR----------DDSNDEKKKLLFKQV---------REMEVELEEER 1609
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRPGYRivtldgdlvRPGGVITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1610 KQKSQILAAK---KKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLE 1686
Cdd:TIGR02168 667 KTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1687 AELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQV 1766
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1767 ETITTELSAERsfsQKAENARQQMERQNKELkvklnemdstmrSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRR 1846
Cdd:TIGR02168 827 ESLERRIAATE---RRLEDLEEQIEELSEDI------------ESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1847 AEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSN-RRRLQRELEDVTESAESMNREVTTLR 1925
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEAR 971
|
....*....
gi 1785379715 1926 SRLSKLERQ 1934
Cdd:TIGR02168 972 RRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
968-1719 |
4.04e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.83 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 968 KLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDdrigeftstmaEEEEKVKSLNKLRNKYEAV-IADLEDRLKKE 1046
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLE-----------RQAEKAERYKELKAELRELeLALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1047 EKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHED 1126
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1127 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQvVE 1206
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1207 EISEQLEQarrfkgnlekvkqtLESENTDLIKEVKNLQAakQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQ 1286
Cdd:TIGR02168 397 SLNNEIER--------------LEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1287 AELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEetrqKLNFSSRVRQLEEEKNNLMENLEEEES--------A 1358
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSElisvdegyE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1359 KAQLSRQLQALQQQLLESKkrmEDQGGMVEAMEEAK---------------KKSYKELEFLQQRFDEKHQINDkLEKTRN 1423
Cdd:TIGR02168 537 AAIEAALGGRLQAVVVENL---NAAKKAIAFLKQNElgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKD-LVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1424 RLQQELDDL-----MVD-----------LDHQRQIVS----------NLEKKQKKFDQMLAEEKNISARYGEERDRAEAE 1477
Cdd:TIGR02168 613 KLRKALSYLlggvlVVDdldnalelakkLRPGYRIVTldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1478 AREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQA 1557
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1558 IEDGKLRLEVNMQAMKAQFERDLQN-----------RDDSNDEKKKLLFKQVREMEVELEEERKQKS--QILAAKKKLEM 1624
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEElkalrealdelRAELTLLNEEAANLRERLESLERRIAATERRleDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1625 DLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKR 1704
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810
....*....|....*
gi 1785379715 1705 QAQQERDDLADELSN 1719
Cdd:TIGR02168 933 GLEVRIDNLQERLSE 947
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
970-1738 |
4.52e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.85 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 970 QLEKVTTEsRLKKMEEDILLLEDQNAK---LAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLkke 1046
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL--- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1047 ekgRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVddevgqkNNLLKQLRDLQSQLAELHED 1126
Cdd:TIGR02169 275 ---EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-------AKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1127 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVvE 1206
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-A 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1207 EISEQLEQARrfkgnlEKVKQtLESENTDLIKEVK----NLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKL 1282
Cdd:TIGR02169 424 DLNAAIAGIE------AKINE-LEEEKEDKALEIKkqewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1283 QKLQAELDGVSGALGSTE--GKSIK----LTKDLSTVQSQLQDTQE-----------------------LLQEETRQKLN 1333
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEvlKASIQgvhgTVAQLGSVGERYATAIEvaagnrlnnvvveddavakeaieLLKRRKAGRAT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1334 FS--SRVRQLEEEKNNLMENLEEEES----------AKAQLSRQLQALQQQLLESKKRMEDQGGMVE----------AME 1391
Cdd:TIGR02169 577 FLplNKMRDERRDLSILSEDGVIGFAvdlvefdpkyEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTlegelfeksgAMT 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1392 EAKKKSYKELEFLQQRFDEKHQINDKLEKtrnrLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEER 1471
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1472 DRAEAEAREKETKALSLSRALEEAIDLKDELD-------RQNKQLRAEMDDLVSSKDDVGknVHELERSKRALEQQVQEM 1544
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEarieeleEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1545 KTQIEELEDELQAIEDGKLRLEVNMQAMKAQfERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEM 1624
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1625 DLQDMESQMDSANKGRDEA---VKQLKKLQLQFKEVWREVEETRAARDEIF---VQSRDNEKKLKSLEAELLQLQEDLAA 1698
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPKgedEEIPEEELSLEDVQAELQRVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1785379715 1699 AERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRI 1738
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
998-1822 |
7.37e-20 |
|
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: 97.06 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 998 AKERKLLDDRI---GEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKM------------------ 1056
Cdd:TIGR02169 152 PVERRKIIDEIagvAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYqallkekreyegyellke 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1057 KRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEV--------GQKNNLLKQLRDLQSQLAELhEDLE 1128
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASL-ERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1129 SEKAARAK-AEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEE---DVKVRDAQVTEMRQRHNQV 1204
Cdd:TIGR02169 311 AEKERELEdAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1205 VEEiseqLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQK 1284
Cdd:TIGR02169 391 REK----LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1285 LQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSR-------VRQLEEEKNNLMENLEEEES 1357
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtVAQLGSVGERYATAIEVAAG 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1358 AKAQLSRqlqalqqqlleskkrMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDdlMVDLD 1437
Cdd:TIGR02169 547 NRLNNVV---------------VEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVD--LVEFD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1438 HQRQ-----------IVSNLEKKQKKFDQ--MLAEEKNISARYG------EERDRAEAEAREKETKALSLSRALEEAIDL 1498
Cdd:TIGR02169 610 PKYEpafkyvfgdtlVVEDIEAARRLMGKyrMVTLEGELFEKSGamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRE 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1499 KDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQ---AMKAQ 1575
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1576 FERDLQN-RDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQF 1654
Cdd:TIGR02169 770 LEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1655 KEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRAL 1734
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1735 EMRISQLEEELDEEQSNTELINDrYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMdSTMRSKYKI 1814
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL-EEERKAILE 1007
|
....*...
gi 1785379715 1815 TIASLEAK 1822
Cdd:TIGR02169 1008 RIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
855-1560 |
2.85e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.12 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 855 QAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE 934
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 935 EERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEedillLEDQNAKLAKERKLLDDRIGEFTST 1014
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1015 MAEEEEKVKSLNKLRNKYEAVIADLEdrlkkEEKGRQEM-EKMKRKLDGETTDLQDQLLELQQQIEELKQ--QLARKEEE 1091
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELA-----QLQARLDSlERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1092 LQAALARV------------DDEVGQKNNLLKQLRDLQSQLAEL----HEDLESEKAARAKAEKQRRDLGEELEALKTEL 1155
Cdd:TIGR02168 535 YEAAIEAAlggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLdsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1156 E-------------DTLDSTAAQQELRAKREQEVTDLKKTIEED------VKVRDAQVTEMRQRHNQVVEEISEQLEQAR 1216
Cdd:TIGR02168 615 RkalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1217 rfkgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGAL 1296
Cdd:TIGR02168 695 ----ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1297 GSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLES 1376
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1377 KKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEkhqindkLEKTRNRLQQELDDLMVDLDhqrqivsNLEKKQKKFDQM 1456
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELR-------ELESKRSELRRE 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1457 LAEEKNISARYGEERDRAEAEAREKETKALSL-SRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGkNVHEL-ERSK 1534
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG-PVNLAaIEEY 995
|
730 740
....*....|....*....|....*.
gi 1785379715 1535 RALEQQVQEMKTQIEELEDELQAIED 1560
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
867-1719 |
4.48e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 867 TQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEA---EEMRARLASKKQE----LEEILHDLEARVEEEEERTL 939
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkktETGKAEEARKAEEakkkAEDARKAEEARKAEDARKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 940 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKllddrigeftstMAEEE 1019
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR------------KAEEE 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1020 EKVKSLNKLRN--KYEAVIADLEDRLKKEEKGRQEMEkmkRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALA 1097
Cdd:PTZ00121 1212 RKAEEARKAEDakKAEAVKKAEEAKKDAEEAKKAEEE---RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1098 RVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVT 1177
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1178 DLKKTIEEDVKVRDA-QVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTdlIKEVKNLQAAKQDSEQRRKK 1256
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAkKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1257 LEQQVSEFQIRTNESEKVKFELAEKLQKL--QAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKlnf 1334
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAkkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--- 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1335 SSRVRQLEE----EKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDE 1410
Cdd:PTZ00121 1524 ADEAKKAEEakkaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1411 KHQINDKLEKTRNRLQQELDDLMVDLDHQR---QIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKET--KA 1485
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKkveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKA 1683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1486 LSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEEL---EDELQAIEDGK 1562
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLK 1763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1563 LRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQ--KSQILAAKKKLEMDLQDMESQMDSANKGR 1640
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379715 1641 DEAvkqlkklqlqfkevwREVEETRAARDEIFVQSRDNEKKLKSleaELLQLQEDLAAAERAKRQAQQERDDLADELSN 1719
Cdd:PTZ00121 1844 EEA---------------DAFEKHKFNKNNENGEDGNKEADFNK---EKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
851-1554 |
7.77e-19 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 94.01 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 851 DEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEAR 930
Cdd:COG1196 280 REELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 931 VEEEEERTLQLQNEKKKMHQHIQDLEEQLEeeeGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGE 1010
Cdd:COG1196 360 KEELEEKLSALLEELEELFEALREELAELE---AELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1011 FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRL----KKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQ--- 1083
Cdd:COG1196 437 LQTELEELNEELEELEEQLEELRDRLKELERELaelqEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGlpg 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1084 ------QLARKEEELQAALAR----------VDDEVGQKN--NLLKQLR---------DLQSQLAELHEDLESEKAARAk 1136
Cdd:COG1196 517 vygpvaELIKVKEKYETALEAalgnrlqavvVENEEVAKKaiEFLKENKagratflplDRIKPLRSLKSDAAPGFLGLA- 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1137 AEKQRRDlGEELEALKTELEDTL---DSTAAQQELRAKR--------EQEVTDLKKTI-------------EEDVKVRDA 1192
Cdd:COG1196 596 SDLIDFD-PKYEPAVRFVLGDTLvvdDLEQARRLARKLRikyrivtlDGDLVEPSGSItggsrnkrsslaqKRELKELEE 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1193 QVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLES---ENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTN 1269
Cdd:COG1196 675 ELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEElerQLEELKRELAALEEELEQLQSRLEELEEELEELEEELE 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1270 ESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLM 1349
Cdd:COG1196 755 ELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1350 ENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQEL 1429
Cdd:COG1196 835 EEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERL 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1430 DDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKnisarygEERDRAEAEAREKETKALSLsRALEEAIDLKDELDRQNKQL 1509
Cdd:COG1196 915 EELEAKLERLEVELPELEEELEEEYEDTLETE-------LEREIERLEEEIEALGPVNL-RAIEEYEEVEERYEELKSQR 986
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1785379715 1510 RaemddlvsskddvgknvhELERSKRALEQQVQEMKTQIEELEDE 1554
Cdd:COG1196 987 E------------------DLEEAKEKLLEVIEELDKEKRERFKE 1013
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1112-1962 |
8.40e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 93.63 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1112 QLRDLQSQLAELHEdlesekaaraKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1191
Cdd:pfam15921 86 QVKDLQRRLNESNE----------LHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1192 AQvtemRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLiKEVKNLQAAKQDS-------------EQRRKKLE 1258
Cdd:pfam15921 156 AA----KCLKEDMLNDSNTQIEQLRKMMLSHEGVLQEIRSILVDF-EEASGKKIYEHDSmstihfrslgsaiSKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1259 QQVSEFQIRT----NESEKVKFELAEKLQKL-QAELDGVSGALGSTEGKSIKLTKDLSTVQSQ---LQDTQELLQEETRQ 1330
Cdd:pfam15921 231 TEISYLKGRIfpveDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1331 KlnFSSRVRQLEEeknnlmenleeeesakaqLSRQLQALQQQLLESKKRMEDQggmVEAMEeakkksyKELEFLQQRFDE 1410
Cdd:pfam15921 311 Q--NSMYMRQLSD------------------LESTVSQLRSELREAKRMYEDK---IEELE-------KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1411 KHQINDKLEKTRNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKNIsarygeERDRAEAEAREKETKALsl 1488
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITI------DHLRRELDDRNMEVQRL-- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1489 sRALEEAidLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVN 1568
Cdd:pfam15921 432 -EALLKA--MKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1569 MQAMKAQFER--DLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANK-GRDEAVK 1645
Cdd:pfam15921 509 ERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhGRTAGAM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1646 QLKKLQLQfKEV---WREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVS 1722
Cdd:pfam15921 589 QVEKAQLE-KEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1723 GKSALLDEKRALEMRISQLeeeldeeqsnTELINDRYRKLTLQVETITTELSAERSFSQKAENArqqmerQNKELKVKLN 1802
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNK----------SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS------DGHAMKVAMG 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1803 eMDSTMRSKyKITIASLEAKISQLEEQMEQESKERII----ANKL--------------------VRRAEKRLKEVLLQV 1858
Cdd:pfam15921 732 -MQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFlkeeKNKLsqelstvateknkmagelevLRSQERRLKEKVANM 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1859 EEERRNAD-QFKE------QLEKANIRMKqLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNreVTTLRSRLSKL 1931
Cdd:pfam15921 810 EVALDKASlQFAEcqdiiqRQEQESVRLK-LQHTLDVKELQGPGYTSNSSVKPRLLQPASFTRPHSN--VPSSQSTASFL 886
|
890 900 910
....*....|....*....|....*....|...
gi 1785379715 1932 ERQQRKRAPI-QFTTRTIRQVYQ-LEAVSDEEP 1962
Cdd:pfam15921 887 SHHSIKCEMLkEDPTRDLKQLLQeLRSVINEEP 919
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1555 |
2.99e-17 |
|
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: 88.59 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 844 LLQVTRQDEVMQAKVVElqkvKDTQVKTESELKEMANKYQQLFEEK-----SILAEQLQAeteLFAEAEEMRARLASKKQ 918
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE----KRQQLERLRREREKAERYQALLKEKreyegYELLKEKEA---LERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 919 ELEEI---LHDLEARVEEEEERTLQLQNEKKKMHQHIQdleeqleeeegARQKLQLEKVTTEsrLKKMEEDILLLEDQNA 995
Cdd:TIGR02169 252 ELEKLteeISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----------LRVKEKIGELEAE--IASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 996 KLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRL-----------KKEEKGRQEMEKMKRKLDgET 1064
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeleevdKEFAETRDELKDYREKLE-KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1065 TDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDevgQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDL 1144
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEA---KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1145 GEELEALKTELE------DTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRH-------------NQVV 1205
Cdd:TIGR02169 475 KEEYDRVEKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnNVVV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1206 EEIS---EQLEQARRFKGN------LEKVKQtlESENTDLIKE------------------------------VKNLQAA 1246
Cdd:TIGR02169 555 EDDAvakEAIELLKRRKAGratflpLNKMRD--ERRDLSILSEdgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1247 K-QDSEQRRKKLEQQVSEFQ-------IRTNESEKVKFELAEKLQKLQAELDGVSGALGStegksikLTKDLSTVQSQLQ 1318
Cdd:TIGR02169 633 RrLMGKYRMVTLEGELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1319 DTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSY 1398
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1399 KELefLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLdhqrqivsnlekKQKKFDQMLAEEKnisaRYGEERDRAEAEA 1478
Cdd:TIGR02169 786 ARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKL------------NRLTLEKEYLEKE----IQELQEQRIDLKE 847
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379715 1479 REKETKalslsRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDEL 1555
Cdd:TIGR02169 848 QIKSIE-----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
915-1296 |
1.22e-16 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 86.69 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 915 SKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQN 994
Cdd:COG1196 667 RELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEEL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 995 AKLAKERKLLDDRIgeftstmAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLEL 1074
Cdd:COG1196 747 EELEEELEELQERL-------EELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1075 QQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTE 1154
Cdd:COG1196 820 EQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESE 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1155 LEDTLDSTAAQQELRAKREQEVTDLKktieedVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENT 1234
Cdd:COG1196 900 LAELKEEIEKLRERLEELEAKLERLE------VELPELEEELEEEYEDTLETELEREIERLEEEIEALGPVNLRAIEEYE 973
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1235 DLIKEVKNLQAAKQDSEQRRKKLEQQVSEF-QIRTNESEKVKFELAEKLQKLQAEL-DGVSGAL 1296
Cdd:COG1196 974 EVEERYEELKSQREDLEEAKEKLLEVIEELdKEKRERFKETFDKINENFSEIFKELfGGGTAEL 1037
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1184-1945 |
1.84e-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: 85.89 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1184 EEDVKVRDA-----QVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTL----ESENTDLIKEVKNLQAAKQDSEQRR 1254
Cdd:TIGR02169 167 EFDRKKEKAleeleEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1255 KKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVsgalgsTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNF 1334
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1335 SSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDE-KHQ 1413
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1414 INDkLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqmlaeeknisarygEERDRAEAEAREKETKalslsraLE 1493
Cdd:TIGR02169 401 INE-LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWK-------LE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1494 EAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAI-----------EDGK 1562
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgERYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1563 LRLEV--------------------------------------NMQAMKA------------------QFERDLQN---- 1582
Cdd:TIGR02169 539 TAIEVaagnrlnnvvveddavakeaiellkrrkagratflplnKMRDERRdlsilsedgvigfavdlvEFDPKYEPafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1583 --RD----DSNDEKKKL------------LFKQVREMEVELEEERKQKSQILAAKKKLEM---DLQDMESQMDSANKGRD 1641
Cdd:TIGR02169 619 vfGDtlvvEDIEAARRLmgkyrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1642 EAVKQLKKLQLQFKEVWREVEETRAARDEIfvqsrdnEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGV 1721
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQL-------EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1722 SGKSALLDEKRALEMRISQLEEELDEEQSNTelINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKL 1801
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1802 N------EMDSTMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKA 1875
Cdd:TIGR02169 850 KsiekeiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1876 NIRMKQLKRQLEEAEEEASRANS------NRRRLQRE---LEDVTESAESMNREVTTLRSRL-SKLERQQRKRAPIQFTT 1945
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELSledvqaELQRVEEEiraLEPVNMLAIQEYEEVLKRLDELkEKRAKLEEERKAILERI 1009
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
999-1871 |
5.17e-16 |
|
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: 84.64 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 999 KERKLLDDRIGEFTSTMAEEE------EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLL 1072
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEalkkliEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1073 ELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALK 1152
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1153 TELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRdaqvtemRQRHNQVVEEISEQLEQARRFKGNLEKvKQTLESE 1232
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK-------REAEEEEEEELEKLQEKLEQLEEELLA-KKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1233 NTDLIKEVKNLQAAKQDSEQRRKKLEQQVSE-----FQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLT 1307
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARqledlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1308 KDLSTVQSQLQDTQELLQEETRQKLNFSS---RVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQG 1384
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQkleERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1385 GMVEAMEEAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS 1464
Cdd:pfam02463 545 ISTAVIVEVSATA-DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1465 ARYGEERDRAEAEAREKETKALSLSRA---LEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQV 1541
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1542 QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQIL-AAKK 1620
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEeREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1621 KLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKL----KSLEAELLQLQEDL 1696
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEqkleKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1697 AAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAE 1776
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1777 RSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLL 1856
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
890
....*....|....*
gi 1785379715 1857 QVEEERRNADQFKEQ 1871
Cdd:pfam02463 1024 ELFVSINKGWNKVFF 1038
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
907-1560 |
6.97e-16 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 84.04 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 907 EEMRARLASKKQELEEILHDLearveeeeertlqLQNEKKKMHqhiqdleeqLEEEEGARQKLQLEKVTTESRLKKMEED 986
Cdd:COG0419 143 GEFDAFLKSKPKERKEILDEL-------------FGLEKYEKL---------SELLKEVIKEAKAKIEELEGQLSELLED 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 987 IL-LLEDQNAKLAKERKLLDdrigeftstmAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKrkldgetT 1065
Cdd:COG0419 201 IEdLLEALEEELKELKKLEE----------IQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIE-------S 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1066 DLQDQLLELQQQIEELKQQLARKEEELQaALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLG 1145
Cdd:COG0419 264 LELEALKIREEELRELERLLEELEEKIE-RLEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1146 EELEALKTELEDTLDstaAQQELRAKREQEVTDLKKTIEEDVKVRDaQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKV 1225
Cdd:COG0419 343 SELEELAEEKNELAK---LLEERLKELEERLEELEKELEKALERLK-QLEEAIQELKEELAELSAALEEIQEELEELEKE 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1226 KQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQaeldgvsgalgstEGKSIK 1305
Cdd:COG0419 419 LEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQELPEEHEKELLELY-------------ELELEE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1306 LTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGG 1385
Cdd:COG0419 486 LEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLE 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1386 MVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFD-QMLAEEKNIS 1464
Cdd:COG0419 566 DRLQELKELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEAEEElESELEKLNLQ 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1465 ARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQN---KQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQV 1541
Cdd:COG0419 646 AELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLeelEQLEEELEQLREELEELLKKLGEIEQLIEELESRK 725
|
650
....*....|....*....
gi 1785379715 1542 QEMKTQIEELEDELQAIED 1560
Cdd:COG0419 726 AELEELKKELEKLEKALEL 744
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
857-1665 |
1.20e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 857 KVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMR-----ARLASKKQELEEILHDLEARV 931
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKkdaeeAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 932 EEEEERTLQLQNEKKKMHQHIQDleeqleeeegARQKLQLEKVTTESRLKKMEEdiLLLEDQNAKLAKERKllddrigef 1011
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKK----------AEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADEAK--------- 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1012 tstmAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGEttdlqdqllelqqqieELKQQLARKEEE 1091
Cdd:PTZ00121 1322 ----KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA----------------EKKKEEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1092 lqaALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAA---RAKAEKQRRdlgeeLEALKTELEDTLDSTAAQQEL 1168
Cdd:PTZ00121 1382 ---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKA 1453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1169 RAKREQEvtDLKKTIEEDVKVRDAQVTEMRQRH----NQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1244
Cdd:PTZ00121 1454 EEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKadeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1245 AAKQDSEQRR----KKLEQQVSEFQIRTNEsEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDT 1320
Cdd:PTZ00121 1532 EAKKADEAKKaeekKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1321 QELLQEETRQKlnfSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQL---LESKKRMEDQGGMVEAMEEAKKKS 1397
Cdd:PTZ00121 1611 EAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1398 YKELEFLQQRFDEKHqindKLEKTRNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEknisARYGEERDRAE 1475
Cdd:PTZ00121 1688 KKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEEEKKKI 1759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1476 AEAREKETKALSLSRALEEAIdLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMktqieELEDEL 1555
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM-----EDSAIK 1833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1556 QAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKkllfkqvreMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDS 1635
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEAD---------FNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
810 820 830
....*....|....*....|....*....|.
gi 1785379715 1636 AN-KGRDEAVKQLKKLQLQFKEvwREVEETR 1665
Cdd:PTZ00121 1905 NNmAGKNNDIIDDKLDKDEYIK--RDAEETR 1933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
870-1674 |
2.64e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 870 KTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE-EERTLQLQNEKKKM 948
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 949 H--------------QHIQDLEEQleeeegaRQKLQLEKVTTESRLKKMEEDIlllEDQNAKLAKerkllddrigeftsT 1014
Cdd:TIGR02169 300 EaeiaslersiaekeRELEDAEER-------LAKLEAEIDKLLAEIEELEREI---EEERKRRDK--------------L 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1015 MAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdQLLELQQQIEELKQQLARKEEELQA 1094
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN--------ELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1095 ALARVDDevgQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtldstaAQQELRAKREQ 1174
Cdd:TIGR02169 428 AIAGIEA---KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK------LQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1175 evtdlKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKV-----------KQTLESENTDLIKEVKN- 1242
Cdd:TIGR02169 499 -----ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAagnrlnnvvveDDAVAKEAIELLKRRKAg 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1243 ------LQAAKQDSEQRRKKLEQQVSEFQIRTNESEKvKFELAeklqklqaeldgVSGALGST-------EGKSIKLTKD 1309
Cdd:TIGR02169 574 ratflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDP-KYEPA------------FKYVFGDTlvvedieAARRLMGKYR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1310 LSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEA 1389
Cdd:TIGR02169 641 MVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1390 MEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKniSARYGE 1469
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1470 ERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIE 1549
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1550 ELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKS------------QILA 1617
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsleDVQA 958
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1618 AKKKLEMDLQDMES-------QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQ 1674
Cdd:TIGR02169 959 ELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1391-1937 |
3.07e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 78.65 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1391 EEAKKKSYKELEFLQQRFDEKHQIND-KLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGE 1469
Cdd:COG0419 195 SELLEDIEDLLEALEEELKELKKLEEiQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1470 ERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLrAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIE 1549
Cdd:COG0419 275 ELRELERLLEELEEKIERLEELEREIEELEEELEGLRALL-EELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1550 ELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKL---LFKQVREMEVELEEERKQKSQILAAKKKLEMDL 1626
Cdd:COG0419 354 ELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEElaeLSAALEEIQEELEELEKELEELERELEELEEEI 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1627 QDMESQMDSANKGRdEAVKQLKKLQLQ--------FKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAA 1698
Cdd:COG0419 434 KKLEEQINQLESKE-LMIAELAGAGEKcpvcgqelPEEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELRE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1699 AERAKRQAQQERDDLADELSngvsgksalLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERS 1778
Cdd:COG0419 513 LEEELIELLELEEALKEELE---------EKLEKLENLLEELEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRT 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1779 FSQKAENARQ---QMERQNKELKVKLNEMDSTMRSKYKITIAS-LEAKISQLEEQMEQeSKERIIANKLVRRAEKRLKEV 1854
Cdd:COG0419 584 RKEELEELRErlkELKKKLKELEERLSQLEELLQSLELSEAENeLEEAEEELESELEK-LNLQAELEELLQAALEELEEK 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1855 LLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEaeeeasransnRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQ 1934
Cdd:COG0419 663 VEELEAEIRRELQRIENEEQLEEKLEELEQLEEE-----------LEQLREELEELLKKLGEIEQLIEELESRKAELEEL 731
|
...
gi 1785379715 1935 QRK 1937
Cdd:COG0419 732 KKE 734
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
860-1345 |
3.28e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 78.65 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 860 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTL 939
Cdd:COG0419 257 RLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 940 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEE 1019
Cdd:COG0419 337 KLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGE-TTDLQDQLLELQQQIEELKQQLARKEEELQAA--L 1096
Cdd:COG0419 417 KELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKCpVCGQELPEEHEKELLELYELELEELEEELSREkeE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1097 ARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRdlgEELEALKTELEdtLDSTAAQQELRAKREQEV 1176
Cdd:COG0419 497 AELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLL---EELEELKEKLQ--LQQLKEELRQLEDRLQEL 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1177 TDLKKTIEEDVKVRDAQvtemrQRHNQVVEEISEQLEQARRFKGNLEKVKQTLEsentdLIKEVKNLQAAKQDSEQRRKK 1256
Cdd:COG0419 572 KELLEELRLLRTRKEEL-----EELRERLKELKKKLKELEERLSQLEELLQSLE-----LSEAENELEEAEEELESELEK 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1257 LEQQVSEFQIRTNESEKVKFELAEKLQKLQAELdgvsgALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSS 1336
Cdd:COG0419 642 LNLQAELEELLQAALEELEEKVEELEAEIRREL-----QRIENEEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQ 716
|
....*....
gi 1785379715 1337 RVRQLEEEK 1345
Cdd:COG0419 717 LIEELESRK 725
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
851-1212 |
6.86e-14 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 77.45 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 851 DEVMQAKVvELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEAR 930
Cdd:COG1196 688 EELKSLKN-ELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 931 VEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGE 1010
Cdd:COG1196 767 LESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDE 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1011 FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGEttdlqdqllelqqqIEELKQQLARKEE 1090
Cdd:COG1196 847 LEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESE--------------LAELKEEIEKLRE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1091 ELQAALARVDDEVGQKNNLLKQLRDLQSQlaELHEDLESEKaarAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRA 1170
Cdd:COG1196 913 RLEELEAKLERLEVELPELEEELEEEYED--TLETELEREI---ERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQRE 987
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1785379715 1171 KREQEVTDLKKTIEEDVKvrdaqvtEMRQRHNQVVEEISEQL 1212
Cdd:COG1196 988 DLEEAKEKLLEVIEELDK-------EKRERFKETFDKINENF 1022
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1125-1876 |
1.69e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1125 EDLESEKAARAKAEKQRRdlGEELEALKtELEDTLDSTAAQQELRAKREQEVTDLKKtIEEDVKVRDAQVTEMRQRHNQV 1204
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARK--AEEARKAE-DARKAEEARKAEDAKRVEIARKAEDARK-AEEARKAEDAKKAEAARKAEEV 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1205 VE-------EISEQLEQARRFKgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFE 1277
Cdd:PTZ00121 1188 RKaeelrkaEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1278 LAEKLQKLQA--ELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKlnfssrvrQLEEEKNNLMENLEEE 1355
Cdd:PTZ00121 1267 RRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK--------KAEEAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1356 ESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSykelEFLQQRFDEKHQInDKLEKTRNRLQQELDDLMVD 1435
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKA 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1436 LDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR---------EKETKALSLSRALEEAIDlKDELDRQN 1506
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeeakkkaEEAKKADEAKKKAEEAKK-ADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1507 KQLRAEMDDLvSSKDDVGKNVHEL---ERSKRALEQQVQEMKTQIEELE--------DELQAIEDGKLRLEVNMQAMKAQ 1575
Cdd:PTZ00121 1493 EEAKKKADEA-KKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKK 1571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1576 FERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQilAAKKKLEMDLQDMESqmdsanKGRDEAVKQLKKLQLQFK 1655
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEEL------KKAEEEKKKVEQLKKKEA 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1656 EVWREVEETRAARDEIFVQSRDNEKKlkslEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKR-AL 1734
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkAE 1719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1735 EMRISQLEEELDEEQSNTELINDRYRKLTLQVEtitTELSAERSFSQKAENARQQMERQNKELKVK--LNEMDSTMRSKY 1812
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEV 1796
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1813 KITIASLEakiSQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKAN 1876
Cdd:PTZ00121 1797 DKKIKDIF---DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
847-1716 |
1.86e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.16 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 847 VTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRArlASKKQELEEILHD 926
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 927 LEARveeeeertLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVttesrlKKMEEDILLLEDQNAKLAKERKLLDD 1006
Cdd:pfam02463 242 LQEL--------LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK------KLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1007 RIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKrkldgettdlqdqllelqqqieelKQQLA 1086
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE------------------------EELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1087 RKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQ 1166
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1167 ELRAKREQEVTDLKKTIEEDvKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAA 1246
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKD-ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1247 KQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLstVQSQLQDTQELLQE 1326
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK--LKLPLKSIAVLEID 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1327 ETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQ 1406
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1407 RFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEA----REKE 1482
Cdd:pfam02463 681 LQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEeksrLKKE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1483 TKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGK 1562
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1563 LRLEVNMQAMKAQFErdlQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDE 1642
Cdd:pfam02463 841 ELKEEQKLEKLAEEE---LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1643 AVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADE 1716
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
875-1497 |
3.08e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 75.18 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 875 LKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQN----EKKKMHQ 950
Cdd:COG0419 149 LKSKPKERKEILDELFGLEKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKleeiQEEQEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 951 HIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRN 1030
Cdd:COG0419 229 ELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1031 KYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLL 1110
Cdd:COG0419 309 GLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1111 KQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVR 1190
Cdd:COG0419 389 EAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQELP 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1191 DAQVTEMRQRHNQVVEEISEQL---EQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIR 1267
Cdd:COG0419 469 EEHEKELLELYELELEELEEELsreKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1268 TNESekvkfelaeKLQKLQAELDGVSgalgstegKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNN 1347
Cdd:COG0419 549 KEKL---------QLQQLKEELRQLE--------DRLQELKELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQ 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1348 LMENLEEEESAKAqlSRQLQALQQQLLESKKRMEDQggmvEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQ 1427
Cdd:COG0419 612 LEELLQSLELSEA--ENELEEAEEELESELEKLNLQ----AELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEE 685
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1428 ELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYgEERDRAEAEArEKETKALSLSRALEEAID 1497
Cdd:COG0419 686 KLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRK-AELEELKKEL-EKLEKALELLEELREKLG 753
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
968-1568 |
3.24e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 75.18 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 968 KLQLEKVTTESRLKKMEEDIL-LLEDQNAKLAKERKLLDdrigeftstmAEEEEKVKSLNKLRNKYEAVIADLEDRLKKE 1046
Cdd:COG0419 182 EAKAKIEELEGQLSELLEDIEdLLEALEEELKELKKLEE----------IQEEQEEEELEQEIEALEERLAELEEEKERL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1047 EKGRQEMEKMKRKLDgettdlqDQLLELQQQIEELKQQLARKEEELQAaLARVDDEVGQKNNLLKQLRDLQSQLAELHED 1126
Cdd:COG0419 252 EELKARLLEIESLEL-------EALKIREEELRELERLLEELEEKIER-LEELEREIEELEEELEGLRALLEELEELLEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1127 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDstaAQQELRAKREQEVTDLKKTIEEDVKVRDaQVTEMRQRHNQVVE 1206
Cdd:COG0419 324 LKSLEERLEKLEEKLEKLESELEELAEEKNELAK---LLEERLKELEERLEELEKELEKALERLK-QLEEAIQELKEELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1207 EISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEF--------QIRTNESEKVKFEL 1278
Cdd:COG0419 400 ELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGekcpvcgqELPEEHEKELLELY 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1279 AEKLQKLQAELDGVSGA--LGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLnfSSRVRQLEEEKNNLMENLEEEE 1356
Cdd:COG0419 480 ELELEELEEELSREKEEaeLREEIEELEKELRELEEELIELLELEEALKEELEEKL--EKLENLLEELEELKEKLQLQQL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1357 SAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEK---------HQINDKLEKTRNRLQQ 1427
Cdd:COG0419 558 KEELRQLEDRLQELKELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLeellqslelSEAENELEEAEEELES 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1428 ELDDLMVDLDHQRQI---VSNLEKKQKKFDQMLAEEKNISAR---YGEERDRAE-------------AEAREKETKALSL 1488
Cdd:COG0419 638 ELEKLNLQAELEELLqaaLEELEEKVEELEAEIRRELQRIENeeqLEEKLEELEqleeeleqlreelEELLKKLGEIEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1489 SRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVN 1568
Cdd:COG0419 718 IEELESRKAELEELKKELEKLEKALELLEELREKLGKAGLRADILRNLLAQIEAEANEILSKLSLNRYDLRRLTIRKDGN 797
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
905-1550 |
3.72e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.06 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 905 EAEEMRARLASKKQEL---EEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLK 981
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 982 KMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLD 1061
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1062 GETTDLQDQLLELQQQIEELKqQLARKEEELQAALARVDDEVGQKNnllKQLRDLQSQLAELHEDLESEKAARAKAEKQR 1141
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQ---QEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1142 RDLGEELEALKTELEDTLDS-TAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQR---HNQVVEEISEQLEQARR 1217
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQlNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1218 FKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSgalg 1297
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1298 stegKSIKLTKdlSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKaqlsrqlqalqQQLLESK 1377
Cdd:TIGR04523 426 ----KEIERLK--ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK-----------QNLEQKQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1378 KRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDL--DHQRQIVSNLEKKQKKFDQ 1455
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNK 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1456 MLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDvgknvheLERSKR 1535
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN-------IKSKKN 641
|
650
....*....|....*
gi 1785379715 1536 ALEQQVQEMKTQIEE 1550
Cdd:TIGR04523 642 KLKQEVKQIKETIKE 656
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1526 |
5.68e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 828 KLRHWQWWRLFTKVKPLLQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAEtELFAEAE 907
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 908 EMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQlEKVTTESRLKKMEEDI 987
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 988 LLLEDQNAKLAKERKllddriGEFTSTMAEEEEKVKSLNKlrnkyEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdl 1067
Cdd:PTZ00121 1405 KKADELKKAAAAKKK------ADEAKKKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAE------ 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1068 qdqlLELQQQIEELKQQLARKEEELQaalaRVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRdlgEE 1147
Cdd:PTZ00121 1468 ----EAKKADEAKKKAEEAKKADEAK----KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK---KA 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1148 LEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEI-----------SEQLEQAR 1216
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeekkmkAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1217 RFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKfeLAEKLQKLQAELDGVSGAL 1296
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEAL 1694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1297 GSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMEnleeeesAKAQLSRQLQALQQQLLES 1376
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE-------AKKDEEEKKKIAHLKKEEE 1767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1377 KKRMEDQGGMVEAMEEAKKKsykelEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLeKKQKKFDQM 1456
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDE-----EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI-KEVADSKNM 1841
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1457 LAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKN 1526
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKN 1911
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1136-1717 |
8.01e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1136 KAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRdaqvtemrqrhnqvvEEISEQLEQA 1215
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL---------------PELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1216 RRFKGNLEKVKQTLES---ENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKfELAEKLQKLQAELDgv 1292
Cdd:PRK03918 227 EKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYE-- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1293 sgalgSTEGKSIKLTKDLSTVQSQLQDTQELLQ--EETRQKLN-FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQAL 1369
Cdd:PRK03918 304 -----EYLDELREIEKRLSRLEEEINGIEERIKelEEKEERLEeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1370 QQQLLESKKRMEDqggMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQ---------------------- 1427
Cdd:PRK03918 379 KRLTGLTPEKLEK---ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelle 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1428 ----ELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELD 1503
Cdd:PRK03918 456 eytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1504 RQNKQLRAEMDDLvSSKDDVGKNVHELERSKRALEQQVQEMKTQI--------EELEDELQAIE----------DGKLRL 1565
Cdd:PRK03918 536 KLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEpfyneylelkDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1566 EVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVK 1645
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379715 1646 QLKKLQlqfkevwREVEETRAARDEIfvqsrdneKKLKSLEAELLQLQEDLAAAE-RAKRQAQQERDDLADEL 1717
Cdd:PRK03918 695 TLEKLK-------EELEEREKAKKEL--------EKLEKALERVEELREKVKKYKaLLKERALSKVGEIASEI 752
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1267-1872 |
1.09e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 73.64 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1267 RTNESEKVKFELAEKLQKLQAELDGVSGALgstegkSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKN 1346
Cdd:COG0419 165 GLEKYEKLSELLKEVIKEAKAKIEELEGQL------SELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1347 NLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQggmveamEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQ 1426
Cdd:COG0419 239 ERLAELEEEKERLEELKARLLEIESLELEALKIREEE-------LRELERLLEELEEKIERLEELEREIEELEEELEGLR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1427 QELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQN 1506
Cdd:COG0419 312 ALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAI 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1507 KQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvnmQAMKAQFERDLQNRDDS 1586
Cdd:COG0419 392 QELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIA---ELAGAGEKCPVCGQELP 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1587 NDEKKKLLFKQVREMEVELE--EERKQKSQILAAKKKLEMDLQDMESQMDSANKgrdEAVKQLKKLQLQFKEVWREVEET 1664
Cdd:COG0419 469 EEHEKELLELYELELEELEEelSREKEEAELREEIEELEKELRELEEELIELLE---LEEALKEELEEKLEKLENLLEEL 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1665 RAARDEIFVQS--------RDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLA---------DELSNGVSGKSAL 1727
Cdd:COG0419 546 EELKEKLQLQQlkeelrqlEDRLQELKELLEELRLLRTRKEELEELRERLKELKKKLKeleerlsqlEELLQSLELSEAE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1728 LDEKRALEmRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQnKELKVKLNEMDST 1807
Cdd:COG0419 626 NELEEAEE-ELESELEKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEEL-EQLEEELEQLREE 703
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1808 MRSKYKI--TIASLEAKISQLEEQME---QESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQL 1872
Cdd:COG0419 704 LEELLKKlgEIEQLIEELESRKAELEelkKELEKLEKALELLEELREKLGKAGLRADILRNLLAQIEAEA 773
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
849-1555 |
1.10e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 849 RQDEVmqAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHdle 928
Cdd:PRK03918 133 RQGEI--DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 929 aRVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEgarqKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLddri 1008
Cdd:PRK03918 208 -EINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1009 geftstmaeeEEKVKSLNKLRNK---YEAVIADLEDRLKKEEKGRQEMEKMKRKLDGettdlQDQLLELQQQIEELKQQL 1085
Cdd:PRK03918 279 ----------EEKVKELKELKEKaeeYIKLSEFYEEYLDELREIEKRLSRLEEEING-----IEERIKELEEKEERLEEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1086 ARKEEELQAALARVDDEVgqknNLLKQLRDLQSQLAELHEDLESEKAARAKAEKqrrdlgEELEALKTELEDTLDSTAAQ 1165
Cdd:PRK03918 344 KKKLKELEKRLEELEERH----ELYEEAKAKKEELERLKKRLTGLTPEKLEKEL------EELEKAKEEIEEEISKITAR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1166 qelRAKREQEVTDLKKTIEEDVKVRD------AQVTEmrqrhnqvvEEISEQLEQARRFKGNLEKVKQTLESENTDLIKE 1239
Cdd:PRK03918 414 ---IGELKKEIKELKKAIEELKKAKGkcpvcgRELTE---------EHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1240 VKNLQaaKQDSEQRRKKLEQQVSEfQIRTNESEKVKFELaEKLQKLQAELDGVsgalgstEGKSIKLTKDLSTVQSQLQD 1319
Cdd:PRK03918 482 LRELE--KVLKKESELIKLKELAE-QLKELEEKLKKYNL-EELEKKAEEYEKL-------KEKLIKLKGEIKSLKKELEK 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1320 TQELLQEetrqKLNFSSRVRQLEEEKnnlmenleeeesakaqlsrqlqalqqqlLESKKRMEDQGgmVEAMEEAKKKsYK 1399
Cdd:PRK03918 551 LEELKKK----LAELEKKLDELEEEL----------------------------AELLKELEELG--FESVEELEER-LK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1400 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEEKNISARYGEErdraeaEAR 1479
Cdd:PRK03918 596 ELEPFYNEYLELKDAEKELEREEKELKKLEEEL-------DKAFEELAETEKRLEELRKELEELEKKYSEE------EYE 662
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 1480 EKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEqQVQEMKTQIEELEDEL 1555
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1172-1885 |
1.74e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1172 REQEVTDLKKTIEEDVKV-RDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDL--IKEVKNLQAAKQ 1248
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAeAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1249 DSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQ--SQLQDTQELLQE 1326
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDARKA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1327 ETRQKlnfSSRVRQLEEEKNNlmenleeeesakaqlsrqlqalqqqllESKKRMEDqggmVEAMEEAKKKSYKEleflqq 1406
Cdd:PTZ00121 1203 EAARK---AEEERKAEEARKA---------------------------EDAKKAEA----VKKAEEAKKDAEEA------ 1242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1407 rfdekhqinDKLEKTRNRLQ-QELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS--ARYGEERDRAEAEAR--EK 1481
Cdd:PTZ00121 1243 ---------KKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKkaEE 1313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1482 ETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELE---DELQAI 1558
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKA 1393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1559 EDGKLRLEVNMQamKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQilAAKKKLEMDLQDMESQMDSANK 1638
Cdd:PTZ00121 1394 DEAKKKAEEDKK--KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEA 1469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1639 GRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAK-----RQAQQERDdl 1713
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkadeaKKAEEKKK-- 1547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1714 ADELSNGVSGKSA-----LLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQ 1788
Cdd:PTZ00121 1548 ADELKKAEELKKAeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1789 QMERQNKELKVKLNEMDSTMRSK--------YKITIASLEAKISQ----LEEQMEQESKERIIANKLVRRAE--KRLKEV 1854
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEelkkaeeeNKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAAEALKKEAEeaKKAEEL 1707
|
730 740 750
....*....|....*....|....*....|.
gi 1785379715 1855 LLQVEEERRNADQFKEQLEKANIRMKQLKRQ 1885
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1375-1938 |
3.56e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1375 ESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEkhqINDKLEKTRNRLQqELDDLMVDLDHQRQIVSNLEKKQKKFD 1454
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINE---ISSELPELREELE-KLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1455 QmlaEEKNISARYGEERDRAEaEAREKETKALSLSRALEEAIDLKDELDRqnkqLRAEMDDLVSSKDDVGKNVHELERSK 1534
Cdd:PRK03918 252 G---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1535 RALEQQVQE---MKTQIEELEDELQAIEDGKLRLEVNMQAmkaqFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQ 1611
Cdd:PRK03918 324 NGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1612 KSQILAAKKKLEmdlqDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEEtraardeifvqsRDNEKKLKSLEAELLQ 1691
Cdd:PRK03918 400 KEEIEEEISKIT----ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE------------EHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1692 LQEDLAAAERAKRQAQQERDDLADELSNG--VSGKSALLDEKRALEMRISQ-LEEELDEEQSNTELINDRYRKLTLQVET 1768
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1769 ITTELSAERSFsqkaENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKeriianklVRRAE 1848
Cdd:PRK03918 544 LKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE--------LKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1849 KRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEAS-----RANSNRRRLQRELEDVTESAESMNREVTT 1923
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELAGLRAELEELEKRREE 691
|
570
....*....|....*
gi 1785379715 1924 LRSRLSKLERQQRKR 1938
Cdd:PRK03918 692 IKKTLEKLKEELEER 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
892-1229 |
4.65e-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: 71.63 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 892 LAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQL 971
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 972 EKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQ 1051
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1052 EMEKMKRK-------LDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH 1124
Cdd:TIGR02168 842 DLEEQIEElsediesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1125 EDLESEKAARAKAEKQRRDLGEEL-EALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIE-------------EDVKVR 1190
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyEELKER 1001
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1785379715 1191 -------DAQVTEMRQRHNQVVEEISEQLEQarRFKGNLEKVKQTL 1229
Cdd:TIGR02168 1002 ydfltaqKEDLTEAKETLEEAIEEIDREARE--RFKDTFDQVNENF 1045
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
860-1534 |
5.57e-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: 71.29 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 860 ELQKVKDTQVKTESELKEMANKYQqlfEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHD----------LEA 929
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 930 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEkvTTESRLK---KMEEDILLLEDQNAKLAKERKLLDD 1006
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQ--AENARLEmhfKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1007 RIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELkqqla 1086
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL----- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1087 rkEEELQAALARVDDEVGQKNNLLKQLR-----------DLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTEL 1155
Cdd:pfam05483 316 --EEDLQIATKTICQLTEEKEAQMEELNkakaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1156 EDtldstaaQQELRAKREQEVTDLKKTIEEDVKVRD--AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESEN 1233
Cdd:pfam05483 394 EE-------MTKFKNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1234 TDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSgalgSTEGKSIKLTKDLSTV 1313
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK----KQEERMLKQIENLEEK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1314 QSQLQDTQELLQEETRQKLN-FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEE 1392
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1393 AKKKSYKELEFLQQRFD----EKHQINDKLEKTRNRLQQELDD-------LMVDLDHQRQIVSNLEKKQKKFDQ------ 1455
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNklelELASAKQKFEEIIDNYQKEIEDkkiseekLLEEVEKAKAIADEAVKLQKEIDKrcqhki 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1456 -----MLAEEKNISARYGEERDRAEAEAREKETKALSLSRALE-EAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHE 1529
Cdd:pfam05483 703 aemvaLMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEiELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAI 782
|
....*
gi 1785379715 1530 LERSK 1534
Cdd:pfam05483 783 LKDKK 787
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
855-1420 |
6.04e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 70.94 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 855 QAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE 934
Cdd:COG0419 193 QLSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIR 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 935 EERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESR------LKKMEEDILLLEDQNAKLAKERKLLDDRi 1008
Cdd:COG0419 273 EEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELeellekLKSLEERLEKLEEKLEKLESELEELAEE- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1009 geFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARK 1088
Cdd:COG0419 352 --KNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEEL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1089 EEELqaalarvddevgqknNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLG-EELEALKTELEDTLDSTAAQQE 1167
Cdd:COG0419 430 EEEI---------------KKLEEQINQLESKELMIAELAGAGEKCPVCGQELPEEHeKELLELYELELEELEEELSREK 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1168 LRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQV---VEEISEQLEQARRFKGNLEkvKQTLESENTDLIKEVKNLQ 1244
Cdd:COG0419 495 EEAELREEIEELEKELRELEEELIELLELEEALKEELeekLEKLENLLEELEELKEKLQ--LQQLKEELRQLEDRLQELK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1245 AAKQDSEQRRKKLEQQvSEFQIRTNESEKVKFELAEKLQKLQAELDGVSgaLGSTEGKSIKLTKDLSTVQSQLQDTQELL 1324
Cdd:COG0419 573 ELLEELRLLRTRKEEL-EELRERLKELKKKLKELEERLSQLEELLQSLE--LSEAENELEEAEEELESELEKLNLQAELE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1325 QEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQ---------QQLLESKKRMEDQGGMVEAMEEAKK 1395
Cdd:COG0419 650 ELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEeleqlreelEELLKKLGEIEQLIEELESRKAELE 729
|
570 580
....*....|....*....|....*
gi 1785379715 1396 KSYKELEFLQQRFDEKHQINDKLEK 1420
Cdd:COG0419 730 ELKKELEKLEKALELLEELREKLGK 754
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
998-1532 |
6.39e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 998 AKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMK---RKLDGETTDLQDQLLEL 1074
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1075 QQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLE----SEKAARAKAEKQRRD------- 1143
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddleer 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1144 ---LGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIE------EDVKVRDAQVTEMRQRHNQVVEEISEQLEQ 1214
Cdd:PRK02224 358 aeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREERDELREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1215 ARrfkGNLEKVKQTLES----ENTDLIKEVKNLQAAkQDSEQRRKKLEQQVSEFQIRTNESEKvKFELAEKLQKLQAELD 1290
Cdd:PRK02224 438 AR---ERVEEAEALLEAgkcpECGQPVEGSPHVETI-EEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1291 gvsgalgstegksiKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQ 1370
Cdd:PRK02224 513 --------------RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1371 QQLLESKKRMEDQGGMVEAMEEAKKKSyKELEFLQQRFDEKHQIND----KLEKTRNR---LQQELDDLMVDLDHQR--Q 1441
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIADAE-DEIERLREKREALAELNDerreRLAEKRERkreLEAEFDEARIEEAREDkeR 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1442 IVSNLEKKQKKFDQMLAEEKNISARYGE-ERDRAEAEAREKETKALSLSR-ALEEAIDLKDELDRQNKQLRAEMDDlvss 1519
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAvENELEELEELRERREALENRVeALEALYDEAEELESMYGDLRAELRQ---- 733
|
570
....*....|...
gi 1785379715 1520 kddvgKNVHELER 1532
Cdd:PRK02224 734 -----RNVETLER 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1151 |
6.46e-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: 71.24 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 850 QDEVMQAKVVELQKVKDTQvktESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA 929
Cdd:TIGR02168 706 ELEELEEELEQLRKELEEL---SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 930 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIG 1009
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1010 EFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKE 1089
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379715 1090 E--------ELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH-------EDLESEKAARAKAEKQRRDLGEELEAL 1151
Cdd:TIGR02168 943 ErlseeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1416-1932 |
6.67e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.82 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1416 DKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEA 1495
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1496 IDLKDELDRQNKQLRAEMDDLVSSK---DDVGKNVHELERSKRALEQQVQ-----EMKTQIEELEDELQAIEDGKLRLEV 1567
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNkkiKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1568 NMQAMK---AQFERDLQNRDDSNDEKKKllfkQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAV 1644
Cdd:TIGR04523 336 IISQLNeqiSQLKKELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1645 KQLKKLQLQFKEVWREVEETRAAR-------DEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADEL 1717
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIiknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1718 SNGVSGKSALLDEKRALEMrisqleeeldeeqsntelindryrkltlQVETITTELSAERSFSQKAENARQQMERQNKEL 1797
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEE----------------------------KVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1798 KVKLNEMDSTM-RSKYKITIASLEAKISQLEEqmeqeskeriiANKLVRRAEKRLKEVLLQVEEERRNadqFKEQLEKAN 1876
Cdd:TIGR04523 544 EDELNKDDFELkKENLEKEIDEKNKEIEELKQ-----------TQKSLKKKQEEKQELIDQKEKEKKD---LIKEIEEKE 609
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 1877 IRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLE 1932
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1279-1937 |
7.02e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 70.96 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1279 AEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEeknnlmenleeeesa 1358
Cdd:pfam01576 11 EEELQKVKEKQQKAESELKELEKKHQQLCEEKNILAEQLQAETELFAEAEEMRARLAARKQELEE--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1359 kaqlsrqlqalqqQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLE----KTRNRLQQELDDLMV 1434
Cdd:pfam01576 76 -------------ILHELEARLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQlekvTTEAKIKKMEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1435 DLDHQrqivSNLEKKQKKFDQMLAEeknISARYGEErdraeaearEKETKALSLSRALEEAI--DLKDELDRQNKQlRAE 1512
Cdd:pfam01576 143 LEDQN----NKLQKERKLLEERISE---FTSNLAEE---------EEKSKSLNKLKNKHEAMisDLEDRLKKEEKG-RQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1513 MDDLvssKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDgklRLEvNMQAMKAQFERDLQNRDDSNDEKKK 1592
Cdd:pfam01576 206 LEKA---KRKLEGESSDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLE-EETAQKNAALKKLRELEAQLSELQE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1593 LLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKgRDEAVKQLKKLQlqfkevwreVEETRAARDEIF 1672
Cdd:pfam01576 279 DLESERAARAKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK-REQEVTELKKAL---------EEETRSHEAQLQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1673 VQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNT 1752
Cdd:pfam01576 349 EMRQKHTQALEELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAKQDSEHKRKKLEGQLQELQSRLSESERQR 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1753 ELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEmDSTMRSKYKITIASLEAKISQLEEQMEQ 1832
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSSRLRQLEDEKNSLQEQLEE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1833 ESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTe 1912
Cdd:pfam01576 508 EEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAAYDKLEKTKNRLQQELDDLL- 586
|
650 660
....*....|....*....|....*
gi 1785379715 1913 saesmnREVTTLRSRLSKLERQQRK 1937
Cdd:pfam01576 587 ------VDLDHQRQLVSNLEKKQKK 605
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1246-1953 |
8.83e-12 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 70.51 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1246 AKQDSEQRRKKLEQQ--VSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALgstegksikltKDLSTVQSQLQDTQEL 1323
Cdd:COG1196 150 INAKPEERRKLIEEAagVSKYKERKEEAERKLERTEENLERLEDLLEELEKQL-----------EKLERQAEKAERYQEL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1324 LQEetRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSrqlqalqqqllESKKRMEDQGGMVEAMEEAKKKSYKELEF 1403
Cdd:COG1196 219 KAE--LRELELALLLAKLKELRKELEELEEELSRLEEELE-----------ELQEELEEAEKEIEELKSELEELREELEE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1404 LQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKEt 1483
Cdd:COG1196 286 LQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELE- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1484 kalslsralEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKL 1563
Cdd:COG1196 365 ---------EKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1564 RLEVNMQAMKAQFERDLQNRDDSNDEKKKLlfkqvremeveleeeRKQKSQILAAKKKLEMDLQDMESQMDSankgrdea 1643
Cdd:COG1196 436 ELQTELEELNEELEELEEQLEELRDRLKEL---------------ERELAELQEELQRLEKELSSLEARLDR-------- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1644 vkqLKKLQLQFKEVWREVEETRAARDEIFVQSRD----NEKKLKSLEAEL---LQ--LQEDLAAAERAKRQAQQERDDLA 1714
Cdd:COG1196 493 ---LEAEQRASQGVRAVLEALESGLPGVYGPVAElikvKEKYETALEAALgnrLQavVVENEEVAKKAIEFLKENKAGRA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1715 DELsngvsgksaLLDEKRALEMRISQLEEELDEEQSNTELINDRYRKL-------TLQVETITTELSAERSFSQKAENAR 1787
Cdd:COG1196 570 TFL---------PLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAvrfvlgdTLVVDDLEQARRLARKLRIKYRIVT 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1788 QQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQ 1867
Cdd:COG1196 641 LDGDLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEE 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1868 FKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELedvtESAESMNREVTTLRSRL-SKLERQQRKRAPIQFTTR 1946
Cdd:COG1196 721 LKRELAALEEELEQLQSRLEELEEELEELEEELEELQERL----EELEEELESLEEALAKLkEEIEELEEKRQALQEELE 796
|
....*..
gi 1785379715 1947 TIRQVYQ 1953
Cdd:COG1196 797 ELEEELE 803
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1036-1594 |
1.41e-11 |
|
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: 69.87 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1036 IADLEDRLKKEEKGRQEMEKMKR-KLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV----DDEVGQKNNLL 1110
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1111 KQLRDLQSQLAELHEDLE--SEKAARAKAEKQRRDLGEELEaLKTELEDTLDSTAAQQELRakreqevtDLKKTIEEDVk 1188
Cdd:pfam12128 347 EQLPSWQSELENLEERLKalTGKHQDVTAKYNRRRSKIKEQ-NNRDIAGIKDKLAKIREAR--------DRQLAVAEDD- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1189 vRDAQVTEMRQRHNQVVEEISEQleqARRFKGNLEKVK------QTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVS 1262
Cdd:pfam12128 417 -LQALESELREQLEAGKLEFNEE---EYRLKSRLGELKlrlnqaTATPELLLQLENFDERIERAREEQEAANAEVERLQS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1263 EFQI----RTNESEKVKF------ELAEKLQKLQAELDGVSGAL-----GSTEGKSIKLTKDLSTVQSQLQDTQ-ELLQE 1326
Cdd:pfam12128 493 ELRQarkrRDQASEALRQasrrleERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKVISPELLHRTDLDpEVWDG 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1327 ETRQKLNFSS---RVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESK-KRMEDQGGMVEAMEEAKKKSYKELE 1402
Cdd:pfam12128 573 SVGGELNLYGvklDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQlVQANGELEKASREETFARTALKNAR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1403 FLQQR-FDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIvsnLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREK 1481
Cdd:pfam12128 653 LDLRRlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1482 ETKALSLSRALEEAidlkdELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQV-------------------- 1541
Cdd:pfam12128 730 QLALLKAAIAARRS-----GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriavrrqevlryfdwyqet 804
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379715 1542 -----QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLL 1594
Cdd:pfam12128 805 wlqrrPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENL 862
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
1.45e-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: 426949 Cd Length: 45 Bit Score: 60.91 E-value: 1.45e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1785379715 31 TAKRQVWVPSEKHGFEAASIKEERGEEVIVELaENGKRVPVAKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1622-1936 |
2.67e-11 |
|
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: 69.32 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1622 LEMDLQDMESQMDSANKGRdEAVKQLKKLQLqfkEVW-REVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAE 1700
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYK-ELKAELRELEL---ALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1701 RAKRQAQQERDDLADELSNgvsgksaLLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFS 1780
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYA-------LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1781 QKAENARQQMERQNKELKVKLNEMDSTMRSKYKiTIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEE 1860
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEE-QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 1861 ERRNADqfKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQR 1936
Cdd:TIGR02168 426 LLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
938-1883 |
2.96e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 68.92 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 938 TLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKvttESRLKKMEEDILLLEDQNAKLAKerklLDDRIGEFTSTMAE 1017
Cdd:TIGR00606 208 ELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY---ENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSRKKQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1018 EEEKVKSLNKLRnkyEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALA 1097
Cdd:TIGR00606 281 MEKDNSELELKM---EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQAD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1098 RVDDEVgQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVT 1177
Cdd:TIGR00606 358 RHQEHI-RARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1178 DLKKTIEEDVKVRDAQVTEMRQRHNQV------VEEISEQLEQARRFKGNLEKVKQTLESENtdLIKEVKNLQAAKQDSE 1251
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELqqlegsSDRILELDQELRKAERELSKAEKNSLTET--LKKEVKSLQNEKADLD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1252 QRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQA-------ELDGVSGALGSTEGKSI------KLTKDLSTVQSQLQ 1318
Cdd:TIGR00606 515 RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1319 DTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRmedqggmveAMEEAKKKSY 1398
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQR---------AMLAGATAVY 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1399 KelEFLQQRFDEKHQ---INDKLEKTRNRLQQELDDLMVDL----DHQRQIVSNLEKKQKKFDQMLAeeknISARYGEER 1471
Cdd:TIGR00606 666 S--QFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMLG----LAPGRQSII 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1472 DRAEAEAREKETKALSLSRALEEaidLKDELDRQNKQLRAEMDDLVSSKdDVGKNVHELERskraLEQQVQEMKTQIEEL 1551
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQR---LKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMER----FQMELKDVERKIAQQ 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1552 EDELQAIEDGKLRLEVNmqamkaQFERDLQNRDDSNDEKKKLLFKqvremeveleEERKQKSQILAAKKKLEmDLQDMES 1631
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVN------QEKQEKQHELDTVVSKIELNRK----------LIQDQQEQIQHLKSKTN-ELKSEKL 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1632 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEEtraARDEIFVQSrdnekklKSLEAELLQLQEDLAAAERAKRQAQQERD 1711
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKD---AKEQDSPLE-------TFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1712 DLADELSNGVSGKSALL--------DEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVET--ITTELSAERSFSQ 1781
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIEnkiqdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkIQERWLQDNLTLR 1024
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1782 KAENARQQMERQNKELKVKLNEMDST-MRSKYKI------TIASLEAKISQLEEQMEQESK--ERIIANKLVRRAEKRLK 1852
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLqMKQEHQKleenidLIKRNHVLALGRQKGYEKEIKhfKKELREPQFRDAEEKYR 1104
|
970 980 990
....*....|....*....|....*....|....
gi 1785379715 1853 EVLLQV---EEERRNADQFKEQLEKANIRMKQLK 1883
Cdd:TIGR00606 1105 EMMIVMrttELVNKDLDIYYKTLDQAIMKFHSMK 1138
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
1199-1938 |
8.27e-11 |
|
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: 67.69 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1199 QRHNQVVEEISEQLEQARRFKgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEqqvsEFQIRTNESEKVKFEL 1278
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKE-ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE----YYQLKEKLELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1279 AEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFssrvrqLEEEKNNLMENLEEEESA 1358
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL------QEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1359 KAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDH 1438
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1439 QRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDEldrqNKQLRAEMDDLVS 1518
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG----KLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1519 SKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMK-AQFERDLQNRDDSNDEKKKLLFKQ 1597
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLlALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1598 VREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSaNKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRD 1677
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPL-GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1678 NEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDD--LADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELI 1755
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1756 NDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLE-EQMEQES 1834
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1835 KERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMkqlKRQLEEAEEEASRANSNRRRLQRELEDVTESA 1914
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740
....*....|....*....|....
gi 1785379715 1915 ESMNREVTTLRSRLSKLERQQRKR 1938
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEE 877
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1438-1942 |
9.25e-11 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 67.09 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1438 HQRQIVSNLEKKQKKFDQMLAEEKNIsarygEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLV 1517
Cdd:COG0419 141 PQGEFDAFLKSKPKERKEILDELFGL-----EKYEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1518 SSKDDVgknvhELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvNMQAMKAQFERDLQNRDDSNDEKKKLLFKQ 1597
Cdd:COG0419 216 KKLEEI-----QEEQEEEELEQEIEALEERLAELEEEKERLEELKARLL-EIESLELEALKIREEELRELERLLEELEEK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1598 VREMEVELEEERKQKSQILAAKKKLEmDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFvqsRD 1677
Cdd:COG0419 290 IERLEELEREIEELEEELEGLRALLE-ELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERL---KE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1678 NEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEmrisQLEEELDEEQSNTELIND 1757
Cdd:COG0419 366 LEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELE----RELEELEEEIKKLEEQIN 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1758 RYRKLTLQVETITTELSAERSFSQKAENARQQ--MERQNKELKVKLNEMDSTMRskykitIASLEAKISQLEEQMEQESK 1835
Cdd:COG0419 442 QLESKELMIAELAGAGEKCPVCGQELPEEHEKelLELYELELEELEEELSREKE------EAELREEIEELEKELRELEE 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1836 ERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIR--MKQLKRQLEEAEEEASRANSNRRRLQrELEDVTES 1913
Cdd:COG0419 516 ELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKeeLRQLEDRLQELKELLEELRLLRTRKE-ELEELRER 594
|
490 500
....*....|....*....|....*....
gi 1785379715 1914 AESMNREVTTLRSRLSKLERQQRKRAPIQ 1942
Cdd:COG0419 595 LKELKKKLKELEERLSQLEELLQSLELSE 623
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
838-1719 |
1.05e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 67.38 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 838 FTKVKPLLQVTRQD--EVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSIlAEQLQAETELFAEAEEMRARLAS 915
Cdd:TIGR00606 184 YIKALETLRQVRQTqgQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 916 KKQELEEILHDLEArveeeeeRTLQLQNEKKKMHQhiqdleEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNA 995
Cdd:TIGR00606 263 KIMKLDNEIKALKS-------RKKQMEKDNSELEL------KMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 996 KLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLK------------------KEEKGRQEME-KM 1056
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpfserqiknfhTLVIERQEDEaKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1057 KRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAK 1136
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1137 AEKQR--RDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKT--IEEDVKVRDAQVTEMRQRHNQVVEEISEQL 1212
Cdd:TIGR00606 490 AEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMemLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1213 EQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRR---KKLEQQVSEFQIRTNESEKVKfELAEKLQKLQAEL 1289
Cdd:TIGR00606 570 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINnelESKEEQLSSYEDKLFDVCGSQ-DEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1290 DGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESakaqlsrqlqal 1369
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES------------ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1370 qqQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRF--------DEKHQI--NDKLEKTRNRLQQELDDLMVDLDHQ 1439
Cdd:TIGR00606 717 --ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqkvnrdiqRLKNDIeeQETLLGTIMPEEESAKVCLTDVTIM 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1440 RQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEarEKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSS 1519
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1520 KDDVGKNVHElersKRALEQQVQEMKTQIEELedeLQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVR 1599
Cdd:TIGR00606 873 KLQIGTNLQR----RQQFEEQLVELSTEVQSL---IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1600 EMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVE----ETRAARDEIFVQS 1675
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkiQERWLQDNLTLRK 1025
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1785379715 1676 RDNEkkLKSLEAELLQLQEDLaaAERAKRQAQQERDDLADELSN 1719
Cdd:TIGR00606 1026 RENE--LKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDL 1065
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
854-1567 |
2.23e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 65.89 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 854 MQAKVVELQKVKDTQV---KTESELKE-----MANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILH 925
Cdd:pfam15921 115 LQTKLQEMQMERDAMAdirRRESQSQEdlrnqLQNTVHELEAAKCLKEDMLNDSNTQIEQLRKMMLSHEGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 926 DLEarveeeeertlqlQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMeedILLLEDQNAKLAKERK--- 1002
Cdd:pfam15921 195 DFE-------------EASGKKIYEHDSMSTIHFRSLGSAISKILRELDTEISYLKGR---IFPVEDQLEALKSESQnki 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1003 --LLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLK--KEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQI 1078
Cdd:pfam15921 259 elLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1079 ------EELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAekQRRDLGEE--LEA 1150
Cdd:pfam15921 339 myedkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL--WDRDTGNSitIDH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1151 LKTELED------TLDS--TAAQQELRAKREQEVTDLKKTIE--EDVKVRDAQVTEMRQRHNQVVEEISEQleqarrfKG 1220
Cdd:pfam15921 417 LRRELDDrnmevqRLEAllKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAK-------KM 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1221 NLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES----------EKVKFELAEK---LQKLQA 1287
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKdkvIEILRQ 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1288 ELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQ 1367
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1368 ALQQQLLESKKRMEDQGGMVEAMEEakkksykELEFLQQRFDEKhqiNDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLE 1447
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSE-------DYEVLKRNFRNK---SEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1448 KKQ-KKFDQMLAEEKNISARYGeerdraeaEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKN 1526
Cdd:pfam15921 720 GSDgHAMKVAMGMQKQITAKRG--------QIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1785379715 1527 VHELERSKRALEQQVQEMKT-------QIEELEDELQAIEDGKLRLEV 1567
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
872-1339 |
4.43e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 872 ESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA----------RVEEEEERTLQL 941
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereelaeEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 942 QNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRL--------------KKMEEDILLLEDQNAKLAKERKLLDDR 1007
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeecrvaaqahneeaESLREDADDLEERAEELREEAAELESE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1008 IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIeelkqqlaR 1087
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV--------E 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1088 KEEELQAA---------------LARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAArAKAEKQRRDLGEELEALK 1152
Cdd:PRK02224 444 EAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1153 TELEDTLDSTAAQQELRAKREQEVTDLkktieedvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESE 1232
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAEL-----------EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1233 NT---------DLIKEVKNLQAAKQD----SEQRRKKL---------------EQQVSEFQIRTNESEKVKFELAEKLQK 1284
Cdd:PRK02224 592 ERirtllaaiaDAEDEIERLREKREAlaelNDERRERLaekrerkreleaefdEARIEEAREDKERAEEYLEQVEEKLDE 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379715 1285 LQAELDGVSGALGSTEGkSIKLTKDLSTVQSQLQDTQELLQ---EETRQKLNFSSRVR 1339
Cdd:PRK02224 672 LREERDDLQAEIGAVEN-ELEELEELRERREALENRVEALEalyDEAEELESMYGDLR 728
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1402-1938 |
9.34e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1402 EFLQQRFDEKHQINDKLEKTRnrlqQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEArek 1481
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERR----EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1482 etkalSLSRALEEAI-DLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQ---- 1556
Cdd:PRK02224 303 -----GLDDADAEAVeARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEeare 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1557 AIEDGKLRLEvnmqamkaqferDLQNRDDSNDEkkkllfkqvremeveleeerkqksqilaAKKKLEMDLQDMESQMDSA 1636
Cdd:PRK02224 378 AVEDRREEIE------------ELEEEIEELRE----------------------------RFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1637 NKGRDEAVKQLKKLQLQFKEVWREVEETRAARDE--------------IFVQSRDNEKKLKSLEAELLQLQEDLAAAEra 1702
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVE-- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1703 krqaqqERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRyrkltlqVETITTELSAERSFSQK 1782
Cdd:PRK02224 496 ------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1783 AENARQQMERQNKELKVKLNEMDSTMRSKYKI-----TIASLEAKISQLEEQ------MEQESKERiIANKLVRRAEKRL 1851
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLERIrtllaAIADAEDEIERLREKrealaeLNDERRER-LAEKRERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1852 KEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQR------ELEDVTESAESMNREVTTLR 1925
Cdd:PRK02224 642 EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEElrerreALENRVEALEALYDEAEELE 721
|
570
....*....|...
gi 1785379715 1926 SRLSKLERQQRKR 1938
Cdd:PRK02224 722 SMYGDLRAELRQR 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
852-1432 |
1.26e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 852 EVMQAKVVELQKV-------KDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEIL 924
Cdd:TIGR02169 364 EELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 925 HDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQnaklakeRKLL 1004
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV-------EEVL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1005 DDRIGEFTSTMAE----EEEKVKSL-----NKLRN---KYEAVIADLEDRLKKEEKGR---------------------- 1050
Cdd:TIGR02169 517 KASIQGVHGTVAQlgsvGERYATAIevaagNRLNNvvvEDDAVAKEAIELLKRRKAGRatflplnkmrderrdlsilsed 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1051 ------------------------------QEMEKMKR--------KLDGETTDLQDQLLELQQQIEELKQQLARKEEEL 1092
Cdd:TIGR02169 597 gvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1093 QAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKR 1172
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1173 EQEVTDLKKTI---EEDVKVRDAQVTEMRQRHN-QVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQ 1248
Cdd:TIGR02169 757 KSELKELEARIeelEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1249 DSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDtqellQEET 1328
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-----LEAQ 911
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1329 RQKLNfsSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMvEAMEEAKKKSYKELEFLQQRF 1408
Cdd:TIGR02169 912 IEKKR--KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRL 988
|
650 660
....*....|....*....|....
gi 1785379715 1409 DEKHQINDKLEKTRNRLQQELDDL 1432
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEY 1012
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1119-1735 |
1.54e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1119 QLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtldstaaqqelraKREQEVTDLKKTIEEDVKVRDAQvtemr 1198
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEE-------------KEEKDLHERLNGLESELAELDEE----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1199 qrhnqvVEEISEQLEQARRFKGNLEKV----KQTLEsENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNesekv 1274
Cdd:PRK02224 222 ------IERYEEQREQARETRDEADEVleehEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE----- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1275 kfELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEE 1354
Cdd:PRK02224 290 --ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1355 EESAkaqlsrqlqalqqqLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMV 1434
Cdd:PRK02224 368 LESE--------------LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1435 DLdhqrqivSNLEKKQKKFDQMLAEEK-----------NISARYGEERDRAEAEAREKETKALSLSrALEEAIDLKDELd 1503
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVE-EVEERLERAEDL- 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1504 rqnKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMK---AQFERDL 1580
Cdd:PRK02224 505 ---VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKL 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1581 QNRDDSNDEKKKLlfkqvremeveleeerkqkSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWRE 1660
Cdd:PRK02224 582 AELKERIESLERI-------------------RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1661 VEETRA----ARDEIFVQSRDN-EKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLaDELSNGVSGKSALLDEKRALE 1735
Cdd:PRK02224 643 FDEARIeearEDKERAEEYLEQvEEKLDELREERDDLQAEIGAVENELEELEELRERR-EALENRVEALEALYDEAEELE 721
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1082-1874 |
2.55e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1082 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKaarakaeKQRRDLGEELEALKTELEDtlds 1161
Cdd:TIGR04523 46 KNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-------DKINKLNSDLSKINSEIKN---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1162 taaQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVvEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVK 1241
Cdd:TIGR04523 115 ---DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL-EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1242 NLQAAKQDSE----------QRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLS 1311
Cdd:TIGR04523 191 KIKNKLLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1312 TVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKnnlmenleeeesakaqlsrqlqalqqqlleskkrmeDQGGMVEAME 1391
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK------------------------------------EQDWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1392 EAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELddlmvdldhqrqivSNLEKKQKKFDQMLAEEKNisarygeer 1471
Cdd:TIGR04523 315 ELKNQE-KKLEEIQNQISQNNKIISQLNEQISQLKKEL--------------TNSESENSEKQRELEEKQN--------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1472 dRAEAEAREKETKALSLSRALEEAIDLKDELDRQnKQLRAEMDdlvsskddvgKNVHELERSKRALEQQVQEMKTQIEEL 1551
Cdd:TIGR04523 371 -EIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-EKLNQQKD----------EQIKKLQQEKELLEKEIERLKETIIKN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1552 EDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEErKQKSQILAAKKKLEMDLQDMES 1631
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE-KELKKLNEEKKELEEKVKDLTK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1632 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEEtraarDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERD 1711
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNK-----DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1712 DLADElsngvsgKSALLDEKRALEMRISQleeeldeEQSNTELINDRYRKLTLQVETIttelsaeRSFSQKAENARQQME 1791
Cdd:TIGR04523 593 QKEKE-------KKDLIKEIEEKEKKISS-------LEKELEKAKKENEKLSSIIKNI-------KSKKNKLKQEVKQIK 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1792 RQNKELKVKLNEMDSTMR-SKYKITiasleaKISQLEEQMEQESKERI---IANKLVRRAEKRLKEVLLQVEEERRNADQ 1867
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKeSKTKID------DIIELMKDWLKELSLHYkkyITRMIRIKDLPKLEEKYKEIEKELKKLDE 725
|
....*..
gi 1785379715 1868 FKEQLEK 1874
Cdd:TIGR04523 726 FSKELEN 732
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
874-1313 |
2.95e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 62.47 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 874 ELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHD----LEARVEEEEERTLQLQNEKKKMH 949
Cdd:COG0419 302 ELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNElaklLEERLKELEERLEELEKELEKAL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 950 QHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIG--EFTSTMAEEEEKVKSL-- 1025
Cdd:COG0419 382 ERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINqlESKELMIAELAGAGEKcp 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1026 -----------NKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKrKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQA 1094
Cdd:COG0419 462 vcgqelpeeheKELLELYELELEELEEELSREKEEAELREEIE-ELEKELRELEEELIELLELEEALKEELEEKLEKLEN 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1095 ALA--RVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARA---------KAEKQRRDLGEELEALKTELEDTLDSTA 1163
Cdd:COG0419 541 LLEelEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTrkeeleelrERLKELKKKLKELEERLSQLEELLQSLE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1164 AQQELRA--KREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQvVEEISEQLEQARRFKGNLEKVKQTLESENtDLIKEVK 1241
Cdd:COG0419 621 LSEAENEleEAEEELESELEKLNLQAELEELLQAALEELEEK-VEELEAEIRRELQRIENEEQLEEKLEELE-QLEEELE 698
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 1242 NLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELaEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTV 1313
Cdd:COG0419 699 QLREELEELLKKLGEIEQLIEELESRKAELEELKKEL-EKLEKALELLEELREKLGKAGLRADILRNLLAQI 769
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1405-1938 |
3.11e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 62.09 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1405 QQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQmlaEEKNISARYGEERDRAEAEAREKETK 1484
Cdd:COG0419 174 ELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQEE---QEEEELEQEIEALEERLAELEEEKER 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1485 ALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEdgklr 1564
Cdd:COG0419 251 LEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLK----- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1565 levNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAV 1644
Cdd:COG0419 326 ---SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELS 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1645 KQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGK 1724
Cdd:COG0419 403 AALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQELPEEHEKELLELYELE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1725 SALLDEKRALEMRISQLEEELDeeqsntELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMER-QNKELKVKLNE 1803
Cdd:COG0419 483 LEELEEELSREKEEAELREEIE------ELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEElEELKEKLQLQQ 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1804 MDStMRSKYKITIASLEAKISQLEEQMEQESKERII--ANKLVRRAEKRLKEVLLQVEE--ERRNADQFKEQLEKANIRM 1879
Cdd:COG0419 557 LKE-ELRQLEDRLQELKELLEELRLLRTRKEELEELreRLKELKKKLKELEERLSQLEEllQSLELSEAENELEEAEEEL 635
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379715 1880 KQLKRQLEEaeeeasrANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKR 1938
Cdd:COG0419 636 ESELEKLNL-------QAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKL 687
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1325 |
3.20e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 861 LQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQ 940
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 941 LQNEKKKMHQHIQDLEEQLEEEEGARQKLQLE-----KVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTM 1015
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1016 AEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdqllelqqqieelkQQLARKEEELQAA 1095
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD---------------------EQIKKLQQEKELL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1096 LARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTldstaaQQELRAKREQ- 1174
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK------QKELKSKEKEl 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1175 -EVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENtdLIKEVKNLQAAKQDSEQR 1253
Cdd:TIGR04523 499 kKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQT 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 1254 RKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQ 1325
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1245 |
3.50e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 850 QDEVMQAKVVELQKVKDTQVKTEsELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA 929
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 930 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQ--------------LEKVTTESRLKKMEEDILLLEDQNA 995
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 996 KLAKERKLLDDRIgEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQ 1075
Cdd:PRK02224 486 DLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1076 QQIEELKQQLARKEEELQAALARVDDevgqknnlLKQLRDLQSQLAELHEDLES---EKAARAKAEKQRRDLGEELEALK 1152
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIES--------LERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1153 TELEDTLDStAAQQELRAKREQEVTDLKKtIEEDVKVRDAQVTEMRQRHNQVVEEIsEQLEQARRFKGNLEKVKQTLESe 1232
Cdd:PRK02224 637 RELEAEFDE-ARIEEAREDKERAEEYLEQ-VEEKLDELREERDDLQAEIGAVENEL-EELEELRERREALENRVEALEA- 712
|
410
....*....|...
gi 1785379715 1233 ntdLIKEVKNLQA 1245
Cdd:PRK02224 713 ---LYDEAEELES 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1196-1933 |
4.12e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1196 EMRQRHNQVVEEISeQLEQARRFKGNLEKVKQTLESEntdlIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVK 1275
Cdd:PRK03918 142 ESDESREKVVRQIL-GLDDYENAYKNLGEVIKEIKRR----IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1276 FELAEKLQKLQAELDgvsgalgstegksikltkdlstvqsQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEee 1355
Cdd:PRK03918 217 PELREELEKLEKEVK-------------------------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1356 esakaqlsrqlqalqqqllESKKRMEDQGGMVEAMEEAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvd 1435
Cdd:PRK03918 270 -------------------ELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI--- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1436 ldhQRQIvSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAeareketkalslsraLEEAIDLKDELDRQNKQLRAEmdd 1515
Cdd:PRK03918 327 ---EERI-KELEEKEERLEELKKKLKELEKRLEELEERHEL---------------YEEAKAKKEELERLKKRLTGL--- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1516 lvsSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvnmqamKAQFERDLQNRDDSNDEKKKLLF 1595
Cdd:PRK03918 385 ---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELLE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1596 K---QVREMEVELEEERKQKSQILAAKKKLEMDLQDME--SQMDSANKGRDEAVKQLKKLQLQ-FKEVWREVEETRAARD 1669
Cdd:PRK03918 456 EytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLI 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1670 EIFVQSRDNEKKLKSLEAellqLQEDLAAAERAKRQAQQERDDLADELSNgVSGKSALLDEKRALEMrisqleeeldeeq 1749
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERLKEL------------- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1750 sntELINDRYRKLtlqvetittelsaersfsqkaENARQQMERQNKELKVKLNEMDST--MRSKYKITIASLEAKISQLE 1827
Cdd:PRK03918 598 ---EPFYNEYLEL---------------------KDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1828 EQMEQESKERIiaNKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKanirmkqLKRQLEEAeeeaSRANSNRRRLQREL 1907
Cdd:PRK03918 654 KKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEK-------LKEELEER----EKAKKELEKLEKAL 720
|
730 740
....*....|....*....|....*..
gi 1785379715 1908 EDVTESAESMNREVTTLRSR-LSKLER 1933
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERaLSKVGE 747
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1000-1879 |
5.99e-09 |
|
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: 61.61 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1000 ERKLLDDR--IGEFTSTMAEEEEKVKSLNKLrNKYEAVIADLEDRLkkeEKGRQEMEKMKRKLDGETTDLQDQLLELQQQ 1077
Cdd:TIGR01612 889 EKKFNDSKslINEINKSIEEEYQNINTLKKV-DEYIKICENTKESI---EKFHNKQNILKEILNKNIDTIKESNLIEKSY 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1078 IEELKQQLARKEEELQAAL--ARVDDEVGQKNNLLKQLRDLQSQLAELHEDL------ESEKAAR---AKAEKQRRDLGE 1146
Cdd:TIGR01612 965 KDKFDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfdEKEKATNdieQKIEDANKNIPN 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1147 ELEALKTELEDTLDstaaqqELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQR--HNQVVEEISEQleqARRFKGNLEK 1224
Cdd:TIGR01612 1045 IEIAIHTSIYNIID------EIEKEIGKNIELLNKEILEEAEINITNFNEIKEKlkHYNFDDFGKEE---NIKYADEINK 1115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1225 VKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES---EKVKfELAEKLQKLQAELDgvsgalgstEG 1301
Cdd:TIGR01612 1116 IKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKID---------KK 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1302 KSI--KLTKDLSTVqSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNlmenleeeesakaqlsrqlqalqqqllESKKR 1379
Cdd:TIGR01612 1186 KNIydEIKKLLNEI-AEIEKDKTSLEEVKGINLSYGKNLGKLFLEKID---------------------------EEKKK 1237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1380 MEDqggMVEAME-------EAKKKSYKELEFLQQRFDEKHQINdklekTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1452
Cdd:TIGR01612 1238 SEH---MIKAMEayiedldEIKEKSPEIENEMGIEMDIKAEME-----TFNISHDDDKDHHIISKKHDENISDIREKSLK 1309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1453 FDQMLAEEKNISarygEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQN-KQLRAEMDDLVSSKDDVGKNVH-EL 1530
Cdd:TIGR01612 1310 IIEDFSEESDIN----DIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKiKKIIDEVKEYTKEIEENNKNIKdEL 1385
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1531 ERSKRaLEQQVQEmKTQIEELEDELQAIEDGKLRLEV--NMQAMKAQFERDLQNRD------DSNDEKKKLLFKQVREME 1602
Cdd:TIGR01612 1386 DKSEK-LIKKIKD-DINLEECKSKIESTLDDKDIDECikKIKELKNHILSEESNIDtyfknaDENNENVLLLFKNIEMAD 1463
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1603 VELEEERKQKSQilAAKKKLEMDLQDMESQMDSANKGRDEA---VKQLKKLQLQFKEVWREVEE------TRAARDEIFV 1673
Cdd:TIGR01612 1464 NKSQHILKIKKD--NATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEllnkysALAIKNKFAK 1541
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1674 QSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALE------MRISQLEEELDE 1747
Cdd:TIGR01612 1542 TKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEnfenkfLKISDIKKKIND 1621
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1748 EQSNTELINDRYRklTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDStMRSKykitIASLEAKISQLE 1827
Cdd:TIGR01612 1622 CLKETESIEKKIS--SFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE-LDSE----IEKIEIDVDQHK 1694
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379715 1828 EQME----QESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFK-----EQLEKANIRM 1879
Cdd:TIGR01612 1695 KNYEigiiEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEgidpnEKLEEYNTEI 1755
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1082-1486 |
7.39e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 60.99 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1082 KQQLARKEEELQAALARVDDEVGQkNNLLKQLRD---------------LQSQLAELHEDLESEKAARAKAEKQRRDLGE 1146
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQ-NSDCKQHIEvlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1147 ELEALKTELEDTLDSTAAqqelrakREQEVTDLKKTIE---EDVKVRDAQVTEMRQRHNQVVEEISEQ------LEQARR 1217
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGLKERVKSLQTDSSNTdtalttLEEALS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1218 FKGN-LEKVKQTLESENTDLIKEVknlqaakQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGAL 1296
Cdd:pfam10174 447 EKERiIERLKEQREREDRERLEEL-------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1297 GSTEGKSIKLTKDLSTVQSQLQDTQELlQEETRQKLNFSSRVRQLEEEknnlmENLEEEESAKAQLSRQLQALQQQLLES 1376
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQE-----VARYKEESGKAQAEVERLLGILREVEN 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1377 KKRMEDQggMVEAMEEAKKKSYKELEFLQQRFDEKHQI-------------NDKLEKTRNRLQQELDDLMVDLDHQRQIV 1443
Cdd:pfam10174 594 EKNDKDK--KIAELESLTLRQMKEQNKKVANIKHGQQEmkkkgaqlleearRREDNLADNSQQLQLEELMGALEKTRQEL 671
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379715 1444 SNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKAL 1486
Cdd:pfam10174 672 DATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1316 |
7.88e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 860 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEemrarlaskkqELEEILHDLEARVEEEEERTL 939
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS-----------ELKKQNNQLKDNIEKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 940 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKllDDRIGEFTSTMAEEE 1019
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV 1099
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1100 DDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1179
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1180 KKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQtLESENTDLIKEVKNLQAA--KQDSEQRRKKL 1257
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK-LESEKKEKESKISDLEDElnKDDFELKKENL 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 1258 EQQVSEFQIR-------TNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQ 1316
Cdd:TIGR04523 560 EKEIDEKNKEieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
845-1143 |
1.20e-08 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 60.50 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 845 LQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEIL 924
Cdd:COG1196 716 RQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEEL 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 925 HDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLL 1004
Cdd:COG1196 796 EELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEEL 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1005 DDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEkgrqemEKMKRKLDGETTDLQDQLLELQQQIEELKQQ 1084
Cdd:COG1196 876 EDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELE------AKLERLEVELPELEEELEEEYEDTLETELER 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1085 LARKEEELQAALARVDDEV-GQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRD 1143
Cdd:COG1196 950 EIERLEEEIEALGPVNLRAiEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRE 1009
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
827-1469 |
1.05e-07 |
|
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: 57.29 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 827 LKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKVVELQkvkdTQVKTESELKEMANKYQQlfeeKSILAEQLQAETELFAEA 906
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELR----AQEAVLEETQERINRARK----AAPLAAHIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 907 EEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQleKVTTESRLKKMEED 986
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 987 ILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEE------KVKSLNKLRNKYEAVIADLEDRLKKEEKGRQ-EMEKMKRK 1059
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDlqgqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQS 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1060 LDGETTDLQDQLLELQQQIEELKQQLARKEE-----------ELQAALARVD-DEVGQKNNLLKQLRDLQSQLAELHEDL 1127
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVLARLLElqeepcplcgsCIHPNPARQDiDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1128 ESEKAARakaEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEE 1207
Cdd:TIGR00618 548 YHQLTSE---RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1208 ISEQLEQA--RRFKGNLEKVKQTLESENTDLIKE--VKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQ 1283
Cdd:TIGR00618 625 QDLQDVRLhlQQCSQELALKLTALHALQLTLTQErvREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1284 KLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQklnfssRVRQLEEEKNNLMENLEEEESAKAQLS 1363
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVTAALQTGA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1364 RQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYkelEFLQQRFDEKHQINDKLEKTRNRLqQELDDLMVDLDHQRQiv 1443
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP---SDEDILNLQCETLVQEEEQFLSRL-EEKSATLGEITHQLL-- 852
|
650 660
....*....|....*....|....*.
gi 1785379715 1444 sNLEKKQKKFDQMLAEEKNISARYGE 1469
Cdd:TIGR00618 853 -KYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1112-1342 |
1.18e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 56.57 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1112 QLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtldstAAQQELRAKREQEVTDLKKTieedvkvrd 1191
Cdd:COG4372 75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQERE------AVRQELAAARQNLAKAQQEL--------- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1192 AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTnes 1271
Cdd:COG4372 140 ARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQART--- 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379715 1272 ekvkfelaEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLE 1342
Cdd:COG4372 217 --------EELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLE 279
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1244 |
2.04e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 860 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLqaeTELFAEAEEMRARLASKKQELEEILHDLEARVEEEEertl 939
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL---TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 940 QLQNEKKKMHQHIQDLEEQLEEEegarqklqlekvttESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEE 1019
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQK--------------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEEkgrQEMEKMKRKLDGETTDLQDQLLELQQQIEELKqQLARKEEELQAALARV 1099
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKELEEKVK-DLTKKISSLKEKIEKL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1100 DDEVGQKNNllkQLRDLQSQLAELHEDLESEkaaraKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1179
Cdd:TIGR04523 530 ESEKKEKES---KISDLEDELNKDDFELKKE-----NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379715 1180 KKTIEEdvkvrdaqvtemrqrHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1244
Cdd:TIGR04523 602 IKEIEE---------------KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1636-1953 |
2.75e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 55.42 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1636 ANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLAD 1715
Cdd:COG4372 65 LNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1716 ELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTElsaersfSQKAENARQQMERQNK 1795
Cdd:COG4372 145 QAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQE-------AQNLATRANAAQARTE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1796 ELkvklnemdstmrSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEvllqVEEERRNADQFKEQLEKA 1875
Cdd:COG4372 218 EL------------ARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQR----LETAQARLEQEVAQLEAY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1876 NIRMKQLKRQLEEAEEEASRANSNRRRLQRE--LEDVTESAESMNRevtTLRSRLSKLERQQRKRAPI-QFTTRTIRQVY 1952
Cdd:COG4372 282 YQAYVRLRQQAAATQRGQVLAGAAQRVAQAQaqAQAQAQLLSSANR---PAALRLRRSPRRGRRQRPVtRHTTRRRRPAT 358
|
.
gi 1785379715 1953 Q 1953
Cdd:COG4372 359 R 359
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1177-1883 |
2.89e-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: 55.88 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1177 TDLKKTIEEDVKVRDAQVTEMRQRHNQVVEE---ISEQLEQARRFKGNLEKVKQTLE---SENTDLIKEVKNLQAAKQDS 1250
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQENrkiIEAQRKAIQELQFENEKVSLKLEeeiQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1251 EQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVS-GALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETR 1329
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1330 QklnFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEfLQQRFD 1409
Cdd:pfam05483 241 Q---VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS-TQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1410 EKHQIndkLEKTRNRLQQELDDLMVDLDHQRQ----IVSNLEKKQKKFDQMLAEEKNisaRYGEERDRAEAEAREKETKa 1485
Cdd:pfam05483 317 EDLQI---ATKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQ---RLEKNEDQLKIITMELQKK- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1486 lslSRALEEAIDLKDELDRQNKQLR---AEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGK 1562
Cdd:pfam05483 390 ---SSELEEMTKFKNNKEVELEELKkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1563 LRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELE---EERKQKSQILAAKKKLEMDLQDMESQMDSANKG 1639
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMNL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1640 RDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADElsn 1719
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK--- 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1720 gvsgKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKlTLQVETITTELSAERSFSQK--AENARQQMERQNKEL 1797
Cdd:pfam05483 624 ----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKLLEEVEKAKaiADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1798 KVKLNEMDSTM---RSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEK 1874
Cdd:pfam05483 699 QHKIAEMVALMekhKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
....*....
gi 1785379715 1875 ANIRMKQLK 1883
Cdd:pfam05483 779 NTAILKDKK 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
873-1463 |
5.84e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 873 SELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHI 952
Cdd:TIGR04523 89 DKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 953 QDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEdqnaKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKY 1032
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1033 EAVIADLEDRLKKEekgRQEMEKMKRKLDGETtdlqdqllelqQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLkq 1112
Cdd:TIGR04523 245 TTEISNTQTQLNQL---KDEQNKIKKQLSEKQ-----------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1113 LRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELED-TLDSTAAQQELRAKrEQEVTDLKKTIEEDVKvrd 1191
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsESENSEKQRELEEK-QNEIEKLKKENQSYKQ--- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1192 aQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKvkqtLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES 1271
Cdd:TIGR04523 385 -EIKNLESQINDLESKIQNQEKLNQQKDEQIKK----LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1272 EKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKnnlmen 1351
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK------ 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1352 leeeesakaqlsrQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDD 1431
Cdd:TIGR04523 534 -------------KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
570 580 590
....*....|....*....|....*....|....*.
gi 1785379715 1432 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNI 1463
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNI 636
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1645-1977 |
6.99e-07 |
|
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: 54.68 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1645 KQLKKLQLQfkevwreveeTRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGK 1724
Cdd:TIGR02168 200 RQLKSLERQ----------AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1725 SALLDEKRALEMRIsqleeeldeeqsntELINDRYRKLTLQVETITTELsaersfsQKAENARQQMERQNKELKVKLNEM 1804
Cdd:TIGR02168 270 EELRLEVSELEEEI--------------EELQKELYALANEISRLEQQK-------QILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1805 DStMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVllqveeerrnadqfKEQLEKANIRMKQLKR 1884
Cdd:TIGR02168 329 ES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--------------EEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1885 QLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKRAPIQFTTRTIRQVYQLEAVSDEEPES 1964
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330
....*....|...
gi 1785379715 1965 HSGEPSANHQQQQ 1977
Cdd:TIGR02168 474 EQALDAAERELAQ 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1526-1941 |
3.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1526 NVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvnmqAMKAQFERDLQNRDDSNDEKKKL---------LFK 1596
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK----EKEKELEEVLREINEISSELPELreeleklekEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1597 QVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQlQFKEVWREVEETRAARDEIFVQSR 1676
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1677 DNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLadelsngvsgkSALLDEKRALEMRISQLEEELDEEqsnTELIN 1756
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----------KELEKRLEELEERHELYEEAKAKK---EELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1757 DRYRKLTLQVETITTELsaersfsQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKIS------QLEEQM 1830
Cdd:PRK03918 377 LKKRLTGLTPEKLEKEL-------EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1831 EQESKERIIANklVRRAEKRLKEVLLQVEEERRNADQFKEQLEKAN--IRMKQLKRQLEEAEEEASRANSNR-RRLQREL 1907
Cdd:PRK03918 450 RKELLEEYTAE--LKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEElEKKAEEY 527
|
410 420 430
....*....|....*....|....*....|....
gi 1785379715 1908 EDVTESAESMNREVTTLRSRLSKLERQQRKRAPI 1941
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
947-1708 |
3.98e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 947 KMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLN 1026
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1027 KlRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgeTTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQK 1106
Cdd:TIGR00618 254 E-QLKKQQLLKQLRARIEELRAQEAVLEETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1107 NNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEAlkTELEDTLDSTAAQQELRAKREQEVTDLKKTIEED 1186
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1187 VKVRDAQVTEMR-QRHNQVVEEISEQLEQARrfkgnLEKVKQTLESENTDLIKEVKNLQAAKQdSEQRRKKLEQQVSEFQ 1265
Cdd:TIGR00618 409 QATIDTRTSAFRdLQGQLAHAKKQQELQQRY-----AELCAAAITCTAQCEKLEKIHLQESAQ-SLKEREQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1266 IRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEK 1345
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1346 NNLMENLEEEEsakaqlsrqlqalqqqlleskkrmedqggmveAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRL 1425
Cdd:TIGR00618 563 EQMQEIQQSFS--------------------------------ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1426 QQELDDLMVDLDHQrQIVSNLEKKQKKFDQMLAEEKNISARYGEERdraeaeAREKETKALSLSRALEEaidlkdeldRQ 1505
Cdd:TIGR00618 611 ACEQHALLRKLQPE-QDLQDVRLHLQQCSQELALKLTALHALQLTL------TQERVREHALSIRVLPK---------EL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1506 NKQLRAEMDDLVSSKDDVGKNVHELERSKRALeqqvQEMKTQIEELEDELQAIEdgklrlevnmQAMKAQfERDLQNRDD 1585
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIE----------NASSSL-GSDLAARED 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1586 SNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETR 1665
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1785379715 1666 AARDEIFVQSRDNEK-KLKSLEAELLQLQEDLAAAERAKRQAQQ 1708
Cdd:TIGR00618 820 NLQCETLVQEEEQFLsRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1390-1933 |
1.13e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1390 MEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNL---EKKQKKFDQMLAE-EKNISA 1465
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELsslEDMKNRYESEIKTaESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1466 RYGEERDRAEAEAREKETKALSLSRALEEAID-LKDELDRQN-KQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQE 1543
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDyFKYKNDIENkKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1544 MKtQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVRemeveleeerkQKSQILAAKKKLE 1623
Cdd:PRK01156 348 YD-DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEI-----------DPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1624 MDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWRE----VEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAA 1699
Cdd:PRK01156 416 VKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1700 ERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTL----QVETITTELSA 1775
Cdd:PRK01156 496 DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLedldSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1776 ERSfSQKAENARQQMERQNKELK---VKLNEMDSTM---RSKYKITIASLEAKISQLEEQMeQESKERIIANKLVRRAEK 1849
Cdd:PRK01156 576 VIS-LIDIETNRSRSNEIKKQLNdleSRLQEIEIGFpddKSYIDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKID 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1850 RLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLeeaeeeaSRANSNRRRLQRELEDVTESAESMNREVTTLRSRLS 1929
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKAL-------DDAKANRARLESTIEILRTRINELSDRINDINETLE 726
|
....
gi 1785379715 1930 KLER 1933
Cdd:PRK01156 727 SMKK 730
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1427-1949 |
1.44e-05 |
|
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: 50.22 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1427 QELDDLMVDLDHQRQIVSN---LEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELd 1503
Cdd:pfam12128 221 QQVEHWIRDIQAIAGIMKIrpeFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1504 rqnKQLRAEMD-DLVSSKDDVGKNVHELER-------------SKRALEQ-QVQEMKTQIEELEDELQAIEDGKLRLEVN 1568
Cdd:pfam12128 300 ---KEKRDELNgELSAADAAVAKDRSELEAledqhgafldadiETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1569 MQAMKAQfeRDLQNRDDSNDEKKKLlfkqvremEVELEEERKQKSQILAAKKKLEMDLQD-MESQMDSANKGRDEAVKQL 1647
Cdd:pfam12128 377 YNRRRSK--IKEQNNRDIAGIKDKL--------AKIREARDRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1648 KKLQLQ-------------------------------FKEVWR---EVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQ 1693
Cdd:pfam12128 447 GELKLRlnqatatpelllqlenfderierareeqeaaNAEVERlqsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1694 EDLAAA-----ERAKRQAQQERDDLADELS-------------NGVSGKSAL------LDEKR-----------ALEMRI 1738
Cdd:pfam12128 527 LQLFPQagtllHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpewaaseeELRERL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1739 SQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIAS 1818
Cdd:pfam12128 607 DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1819 LEAKISQLEEQMeQESKERIIANKLVRRAEKrlKEVLLQVEEERRNA-DQFKEQLEKANI----RMKQLKRQLEEAEEEA 1893
Cdd:pfam12128 687 LEAQLKQLDKKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALDAQlALLKAAIAARRSgakaELKALETWYKRDLASL 763
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 1894 SRANSNRRRLQRELEDVTESAESMNREvttlRSRLSKLERQQRKRAPIQFTTRTIR 1949
Cdd:pfam12128 764 GVDPDVIAKLKREIRTLERKIERIAVR----RQEVLRYFDWYQETWLQRRPRLATQ 815
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1100-1960 |
1.46e-05 |
|
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: 50.22 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1100 DDEVGQKNNLLKqlRDLQSQLAELHEDLESEKAARAKAEKQRRDLgEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1179
Cdd:pfam12128 208 DDGVVPPKSRLN--RQQVEHWIRDIQAIAGIMKIRPEFTKLQQEF-NTLESAELRLSHLHFGYKSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1180 KKTIEEDVKVRDAQVTEMRQRHNQvveEISEQLEQARRFKGNLEKVkqtlesentdlikEVKNLQAAKQDSEQRRKKLEQ 1259
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDELNG---ELSAADAAVAKDRSELEAL-------------EDQHGAFLDADIETAAADQEQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1260 QVSeFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRvR 1339
Cdd:pfam12128 349 LPS-WQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR-E 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1340 QLEEEKNNLMENLEEEESAkAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQ-------RFDEKH 1412
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSR-LGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSelrqarkRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1413 QINDKLEKTRNRLQQELDDLMVDLDHQR-QIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRA 1491
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1492 LEEAIDLKDELDrQNKQLRAEMDDLVSSKDDvgknvhELERSKRALEQQVQ---EMKTQIEELEDELQAIEDGKL---RL 1565
Cdd:pfam12128 586 DLKRIDVPEWAA-SEEELRERLDKAEEALQS------AREKQAAAEEQLVQangELEKASREETFARTALKNARLdlrRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1566 EVNMQAMKAQFERDLQNRDDS--------NDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSAN 1637
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDSanerlnslEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1638 KGRDEAVK-QLKKLqlqfkEVWREVEETRAARDEIFVQSRdnEKKLKSLEAELLQLQEDLAAAERAKRQAQ----QERDD 1712
Cdd:pfam12128 739 AARRSGAKaELKAL-----ETWYKRDLASLGVDPDVIAKL--KREIRTLERKIERIAVRRQEVLRYFDWYQetwlQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1713 LADELSNgvsgksallDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVEtITTELSAERSFSQKAenARQQMER 1792
Cdd:pfam12128 812 LATQLSN---------IERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVR-LSENLRGLRCEMSKL--ATLKEDA 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1793 QNKELKVKLNEMD---STMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFK 1869
Cdd:pfam12128 880 NSEQAQGSIGERLaqlEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1870 EQLekANIRMKQLKRQLEEAEEEASRANSNrrrLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKRAPIQFTTRTIR 1949
Cdd:pfam12128 960 EQW--FDVRVPQSIMVLREQVSILGVDLTE---FYDVLADFDRRIASFSRELQREVGEEAFFEGVSESAVRIRSKVSELE 1034
|
890
....*....|.
gi 1785379715 1950 QVYQLEAVSDE 1960
Cdd:pfam12128 1035 YWPELRVFVKA 1045
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
1.76e-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: 46.95 E-value: 1.76e-05
10 20
....*....|....*....|....*
gi 1785379715 657 YKESLSKLMSTLRNTNPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1083-1546 |
2.33e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 49.64 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1083 QQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQ-SQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDS 1161
Cdd:COG5281 233 EQLGDVAQAAARFASASGESIDKTIKAFSKLTDDPvNGAKALNRQFHYLTAAQLEQIAALQRAGDTAAAAAAAAEAAAAM 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1162 TAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVk 1241
Cdd:COG5281 313 DDRTARVKENMGTLETAWDALADAAKKMWDAVLGIGREDKQAALLAAKLAAEKLARVTAQGALNARLKLAQDDLTQAEL- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1242 NLQAAKQDSEQRRKKLEQQVSEFQIRTNEsekvKFELAEKLQKLQAEldgVSGALGSTEGKSIKLTKDLSTVQSQLQDTQ 1321
Cdd:COG5281 392 NYAAADQAANQEGALNAREDEAEVLSTQE----ERRDILKNLLADAE---KRTARQEELNKALAKAKILQADKAAKAYQE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1322 ELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEeesakaqlsrqlqalqqqllesKKRMEDQGGMVEAMEEAKKKSYKEL 1401
Cdd:COG5281 465 DILQREAQSRGKTAAAERSQEQMTAALKALLAF----------------------QQQIADLSGAKEKASDQKSLLWKAE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1402 EFLQQRFDEKHQINDKLEKTRNRLQQELddlmvdLDHQRQIVSNLEKKQKKFDQMLAEeknisarYGEERDRAEAEAREK 1481
Cdd:COG5281 523 EQYALLKEEAKQRQLQEQKALLEHKKET------LEYTSQLAELLDQQADRFELSAQA-------AGSQKERGSDLYREA 589
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379715 1482 ET-KALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKR-----ALEQQVQEMKT 1546
Cdd:COG5281 590 LAqNAAALNKALNELAAYWSALDLLQGDWKAGALSALANYRDSATDVASQAAQLFtnafdGMANNAAKFAT 660
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1416-1596 |
2.98e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1416 DKLEKTRNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR 1479
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1480 EKETKALSLSRALEEAIDLKDELDRQNK---------------QLRAEMDDLVSSKDDVGKNV-HELERSKRALEQ---- 1539
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctQQISEGPDRITKIKDKLKELqHSLEKLDTAIDEleei 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379715 1540 ---------QVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFK 1596
Cdd:PHA02562 329 mdefneqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| NtpI |
COG1269 |
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]; |
997-1286 |
3.23e-05 |
|
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
Pssm-ID: 224188 [Multi-domain] Cd Length: 660 Bit Score: 48.90 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 997 LAKERKLLDDRIGEFTSTMAEE-EEKVKSLNKL-----RNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGEttdlqdq 1070
Cdd:COG1269 14 LKSELDPVLAELHDFGLVHLEDlEEGEKGLKELeklkvAEVAQISLSSLLSEVLDYLRSVKGLEGRLFILPEE------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1071 llelqqqieelKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEkqrrDLGEELEA 1150
Cdd:COG1269 87 -----------VEKLEAELKSLEEVIKPAEKFSSEVEELTRKLEERLSELDEELEDLEDLLEELEPLA----YLDFDLSL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1151 LKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEqARR-----FKGNLEKV 1225
Cdd:COG1269 152 LRGLKFLLVRLGLVRREKLEALVGVIEDEVALYGENVEASVVIVVAHGAEDLDKVSKILNELG-FELyevpeFDGGPSEL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 1226 KQTLESENTDLIKEVKNLQAAKQD-SEQRRKKLeqqvsEFQIRTNESEKVKFELAEKLQKLQ 1286
Cdd:COG1269 231 ISELEEVIAEIQDELESLRSELEAlAEKIAEEL-----LAVREILEIEKALGDVLSKLARTE 287
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
764-1125 |
4.79e-05 |
|
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: 48.51 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 764 GQSKIFFRAGVLAHLEEERDLKITDIIVFFQAAARgylARRAFYKKQQQMSALKVVQRNCAAYLKLRHWQWWRLFTKVKP 843
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 844 LLQ-VTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEE 922
Cdd:TIGR02168 745 LEErIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 923 ILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERK 1002
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1003 LLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKkeEKGRQEMEKMKRKldgettdlqdqLLELQQQIEELK 1082
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-----------ENKIEDDEEEAR 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1083 QQLARKEEELQ-------AALARVDDEVGQKNNLLKQLRDLQSQLAELHE 1125
Cdd:TIGR02168 972 RRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
896-1188 |
5.78e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 896 LQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVT 975
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 976 TESRLKKMEE---DILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLN-KLRNKYEAV------IADLEDRLKK 1045
Cdd:PLN02939 182 TDARIKLAAQekiHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENmLLKDDIQFLkaelieVAETEERVFK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1046 EEKGRQEMEKMKRKLDgetTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHE 1125
Cdd:PLN02939 262 LEKERSLLDASLRELE---SKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEA 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1126 DLESEKAARAKAEKQRRdLGEELEALKTELEDTLDSTAAQQELRAKREQEVTD-LKKTIEEDVK 1188
Cdd:PLN02939 339 SLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDtLSKLKEESKK 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1022-1289 |
6.30e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 47.79 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1022 VKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARvdd 1101
Cdd:COG4942 33 AAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQ--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1102 EVGQKNNLLKQLRDLQSQ-----LAELHEDLESEKAARAKAEKQR--RDLGEELEALKTELEDTLDSTAAQQELRAKREQ 1174
Cdd:COG4942 110 EREQRRRLAEQLAALQRSgrnppPALLVSPEDAQRSVRLAIYYGAlnPARAERIDALKATLKQLAAVRAEIAAEQAELTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1175 EVTDLKKTIEEDVKVRDAQvTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTdlikEVKNLQAAKQDSEQRR 1254
Cdd:COG4942 190 LLSEQRAQQAKLAQLLEER-KKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAA----KAREAAAAAEAAAARA 264
|
250 260 270
....*....|....*....|....*....|....*
gi 1785379715 1255 KKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAEL 1289
Cdd:COG4942 265 RAAEAKRTGETYKPTAPEKMLISSTGGFGALRGQL 299
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
1107-1333 |
8.66e-05 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225803 [Multi-domain] Cd Length: 835 Bit Score: 47.76 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1107 NNLLKQLRDLQSQLAELhedlesEKAARAKAEKQRRDLGEEL---EALKTELEDTLDSTAAQQELraKREQEVTDLKKTI 1183
Cdd:COG3264 6 NNVLQELLQSRRELLTA------ESAQLEAALQLLQEAVNSKrqeEAEPAAEEAELQAELIQQEL--AINDQLSQALNQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1184 EEDVKV---RDAQVTEMRQRhnqvVEEISEQL-EQARRFKGNLEKVKQtlesentdLIKEVKNLQAAKQDSEQrrkkleq 1259
Cdd:COG3264 78 TERLNAlasDDRQLANLLLQ----LLQSSRTIrEQIAVLRGSLLLSRI--------LLQQLGPLPEAGQPQEQ------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1260 qvsefqirtnesekvkFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTV-----------------------QSQ 1316
Cdd:COG3264 139 ----------------FEVTQERDALQAEKAYINALEGQAEQLTAEVRDILDQIldtrrellnsllsqreaislqlnQQQ 202
|
250
....*....|....*..
gi 1785379715 1317 LQDTQELLQEETRQKLN 1333
Cdd:COG3264 203 LSAASDELRSLLHQQSF 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1578 |
9.29e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 47.02 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1387 VEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvdlDHQ-RQIVSNLEKKQKKFDQMLAEEKNISA 1465
Cdd:COG4942 33 AAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASL----EAQlIETADDLKKLRKQIADLNARLNALEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1466 RYGEERDRAEA---------------------EAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVG 1524
Cdd:COG4942 109 QEREQRRRLAEqlaalqrsgrnpppallvspeDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQAELT 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1525 KNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFER 1578
Cdd:COG4942 189 TLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIAS 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1387-1960 |
9.76e-05 |
|
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: 47.73 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1387 VEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNlEKKQKKFDQMLAEEKNISAR 1466
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR-EKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1467 YGEERDRAEAEAREKEtkaLSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVG--KNVHELERskralEQQVQEM 1544
Cdd:TIGR00606 336 RLLNQEKTELLVEQGR---LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVI-----ERQEDEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1545 KTqIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNrddsndEKKKLLFKQVREMEVELEEERKQKSqilaAKKKLEM 1624
Cdd:TIGR00606 408 KT-AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL------KKEILEKKQEELKFVIKELQQLEGS----SDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1625 DLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEaelLQLQEDLAAAERAKR 1704
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME---MLTKDKMDKDEQIRK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1705 QAQQERDDLADELSNGVSGK------SALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITT---ELSA 1775
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfDVCG 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1776 ERSFSQKAENARQQMERQNKELKVklnemdstmrskykitIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVL 1855
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAM----------------LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFI 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1856 LQVEEERRNADQFKEQLEKaniRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQ- 1934
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTES---ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLl 774
|
570 580 590
....*....|....*....|....*....|.
gi 1785379715 1935 -----QRKRAPIQFTTRTIRQVYQLEAVSDE 1960
Cdd:TIGR00606 775 gtimpEEESAKVCLTDVTIMERFQMELKDVE 805
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
967-1309 |
1.15e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.16 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 967 QKLQLEKVTTESRLKKMEEDILLledqnaklaKERKLLDDRIGEFTSTMAEEEEKVKSLnKLRNKYEAVIADLEDRLKK- 1045
Cdd:PLN03229 372 QQIKIAINENMDELGKMDTEELL---------KHRMLKFRKIGGFQEGVPVDPERKVNM-KKREAVKTPVRELEGEVEKl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1046 ---------------EEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEEL-----------------KQQLARKEEELQ 1093
Cdd:PLN03229 442 keqilkakessskpsELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLReefskansqdqlmhpvlMEKIEKLKDEFN 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1094 AALARVDDEVGQKNNLlKQLRDLQ-----SQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAqqEL 1168
Cdd:PLN03229 522 KRLSRAPNYLSLKYKL-DMLNEFSrakalSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEALKAEVASSGASSGD--EL 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1169 RAKREQEVTDLKKTIEEDV----KVRDAQVTEMRQRHNQVVEEISEQleqarRFKGNLEKVKQTLESENTDLIK--EVKN 1242
Cdd:PLN03229 599 DDDLKEKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPP-----NLQEKIESLNEEINKKIERVIRssDLKS 673
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379715 1243 ------LQAAK------QDSEQRRKKLEQQVSEfQIRTNESEKvkfELAEKLQKLQAELdgvSGALGSTEGKSIKLTKD 1309
Cdd:PLN03229 674 kiellkLEVAKasktpdVTEKEKIEALEQQIKQ-KIAEALNSS---ELKEKFEELEAEL---AAARETAAESNGSLKND 745
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1542-1935 |
1.17e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1542 QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDD--SNDEKKKLLFKQVREMEVELEEERKQKSQILAAK 1619
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1620 KKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEvwreveetraardeifvqsrdNEKKLKSLEAELLQLQEDLaaa 1699
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ---------------------NNKKIKELEKQLNQLKSEI--- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1700 ERAKRQAQQERD-DLADELSNgvsgksaLLDEKRALEMRISQleeeldeeqsNTELINdryrKLTLQVETITTELSAERS 1778
Cdd:TIGR04523 298 SDLNNQKEQDWNkELKSELKN-------QEKKLEEIQNQISQ----------NNKIIS----QLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1779 FSQKAENarqQMERQNKELKVKLNEMDSTMRSKYKIT--IASLEAKIS---QLEEQMEQESKERIIANKLVRRAEKRLKE 1853
Cdd:TIGR04523 357 ENSEKQR---ELEEKQNEIEKLKKENQSYKQEIKNLEsqINDLESKIQnqeKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1854 VLLQVEEERRNAD----QFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLS 1929
Cdd:TIGR04523 434 TIIKNNSEIKDLTnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
....*.
gi 1785379715 1930 KLERQQ 1935
Cdd:TIGR04523 514 DLTKKI 519
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
846-1305 |
1.24e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 47.40 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 846 QVTRQDEVMQAKVVELQKVKDTQVKTESElKEMANKYQQLFEEKSI---------------LAEQLQAETELFAEAEEMR 910
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLEST-KEMLRKVVEELTAKKMtlessertvsdltasLQEKERAIEATNAEITKLR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 911 ARLASKKQELEEILHDLE-ARVEEEEERTLQLQNEKKK-----MHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKME 984
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDhLRNVQTECEALKLQMAEKDkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 985 edillLEDQNAKLAKERKllDDRIGEFTSTMAE-EEEKVKSLNKLRNKYEAViadledrlkkeekgrQEMEKMKRKLDGE 1063
Cdd:pfam15921 604 -----LELQEFKILKDKK--DAKIRELEARVSDlELEKVKLVNAGSERLRAV---------------KDIKQERDQLLNE 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1064 TTDLQDQLLELQQQIEELKQQLARKEEELQAAlarvddevgqKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQrrd 1143
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETT----------TNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV--- 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1144 lgeelealkteledtldSTAAQQELRAKREQeVTDLKKTI---EEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKG 1220
Cdd:pfam15921 729 -----------------AMGMQKQITAKRGQ-IDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1221 NLEkvkqTLESENTDLIKEVKNLQAAKQdseqrrkKLEQQVSEFQ--IRTNESEKVKFELAEKLQklQAELDGVsgalGS 1298
Cdd:pfam15921 791 ELE----VLRSQERRLKEKVANMEVALD-------KASLQFAECQdiIQRQEQESVRLKLQHTLD--VKELQGP----GY 853
|
....*..
gi 1785379715 1299 TEGKSIK 1305
Cdd:pfam15921 854 TSNSSVK 860
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1626-1862 |
1.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1626 LQDMESQMdsANKGRDEAVKQLKKLQLQFKEVWREVE----------ETRAARDEIFVQSRDNEKKLKSLEAELLQLQED 1695
Cdd:PRK02224 189 LDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIEryeeqreqarETRDEADEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1696 LAAAERakrqaqqERDDLADElsngVSGKSALLDEkraLEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSA 1775
Cdd:PRK02224 267 IAETER-------EREELAEE----VRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1776 ER----SFSQKAENARQ---QMERQNKELKVKLNEMDSTMRSKyKITIASLEAKISQLEEQMEQESKERIIANKLVRRAE 1848
Cdd:PRK02224 333 CRvaaqAHNEEAESLREdadDLEERAEELREEAAELESELEEA-REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250
....*....|....
gi 1785379715 1849 KRLKEVLLQVEEER 1862
Cdd:PRK02224 412 DFLEELREERDELR 425
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown]; |
1107-1289 |
1.64e-04 |
|
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 226400 [Multi-domain] Cd Length: 265 Bit Score: 45.48 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1107 NNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEV-TDLKKTIEE 1185
Cdd:COG3883 41 SELQKEKKNIQNEIESLDNQIEEIQSKIDELQKEIDQSKAEIKKLQKEIAELKENIVERQELLKKRARAMqVNGTATSYI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1186 DVKVRDAQVTEMRQRhnqvVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVsefq 1265
Cdd:COG3883 121 DVILNSKSFSDLISR----VTAISVIVDADKKILEQQKEDKKSLEEKQAALEDKLETLVALQNELETQLNSLNSQK---- 192
|
170 180
....*....|....*....|....
gi 1785379715 1266 irtNESEKVKFELAEKLQKLQAEL 1289
Cdd:COG3883 193 ---AEKNALIAALAAKEASALGEK 213
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1632-1965 |
2.20e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1632 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARD-EIFVQSR---DNEKKLKSLEAELLQLQEDlaaaERAKRQAQ 1707
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1708 QERDDLADELSNGVSGKSALLDEKRALEmRISQLEEELDEEQSNTElinDRYRKLTLQVETITtELSAERSFSQKAENAR 1787
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1788 QQMERQNKELKVKLNEMDstmRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRA-EKRLKEVLLQ-VEEERRNA 1865
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1866 DQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESA---ESMNREVTTLRSRLSKLERQQRKRAPIQ 1942
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMMRQIVESEKARAEYEATTP 596
|
330 340
....*....|....*....|....*
gi 1785379715 1943 FTtrTIRQVYQLEAVSDEEP--ESH 1965
Cdd:pfam17380 597 IT--TIKPIYRPRISEYQPPdvESH 619
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
840-1278 |
2.32e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 840 KVKPLLQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRarlasKKQE 919
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 920 leeilhdlearveeeeertlqlqnEKKKMHQhiqdleeqleeeegaRQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAK 999
Cdd:PTZ00121 1631 ------------------------EKKKVEQ---------------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1000 ERKLLDDRIGEftstmAEEEEKVKslnklrnkyeaviadlEDRLKKEEKGRQEMEKMKRKlDGETTDLQDQLLELQQQIE 1079
Cdd:PTZ00121 1672 EDKKKAEEAKK-----AEEDEKKA----------------AEALKKEAEEAKKAEELKKK-EAEEKKKAEELKKAEEENK 1729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1080 ELKQQLARKEEELQAALARVDDEVGQKNnllkQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTeLEDTL 1159
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIF 1804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1160 DSTAAQQELRAKREQEVTDLKKTieedvkvRDAQVTEMRQRHNQVVEEiSEQLEQARRFKGNLEKVKQTLES----ENTD 1235
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEM-------EDSAIKEVADSKNMQLEE-ADAFEKHKFNKNNENGEDGNKEAdfnkEKDL 1876
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379715 1236 LIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFEL 1278
Cdd:PTZ00121 1877 KEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKL 1919
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1460-1675 |
2.76e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 45.85 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1460 EKNISaRYGEERDRAEAEAREkeTKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKD--DVGKNVHELERSKRAL 1537
Cdd:COG2433 365 ERKLP-ELGIWKDVERIKALV--IRGYPLAEALSKVKEEERPREKEGTEEEERREITVYEKRikKLEETVERLEEENSEL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1538 EQQVQEMKTQIEELEDELQAIEDgklRLEVnmqamKAQFERDLQNRDDSNDEKKKLLfkqvremeveleeeRKQKSQILA 1617
Cdd:COG2433 442 KRELEELKREIEKLESELERFRR---EVRD-----KVRKDREIRARDRRIERLEKEL--------------EEKKKRVEE 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1618 AKKKLE--MDLQDMESQmdsankGRDEAVKQLKKLQLQFKEVwREVEETRAARDEIFVQS 1675
Cdd:COG2433 500 LERKLAelRKMRKLELS------GKGTPVKVVEKLTLEAIEE-AEEEYGIKEGDVILVED 552
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1115-1919 |
4.30e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1115 DLQSQLAELHEDLESEKAARAKAEKQRRDLGE---ELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1191
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1192 AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEV--KNLQAAKQDSEQRRKKLEQQVSEFQIRTN 1269
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1270 ESEKVKFELAEKLQKLQAELDGVsgalgstEGKSIKLTKDLSTVQSQLQDTQELLqEETRQKLNFSSRVRQLEEEKNnlm 1349
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQ-------EDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEIL--- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1350 enleeeeSAKAQLSRQLQALQQQLLESKKRMEDqggmveaMEEAKKKSYKELEFLqqrfdEKHQINDKLEKTRNRLQQEL 1429
Cdd:TIGR00606 450 -------EKKQEELKFVIKELQQLEGSSDRILE-------LDQELRKAERELSKA-----EKNSLTETLKKEVKSLQNEK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1430 DDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREketkALSLSRALEEAIDLKDELDRQNKQL 1509
Cdd:TIGR00606 511 ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE----LTSLLGYFPNKKQLEDWLHSKSKEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1510 RAEMDDLVsskdDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIeDGKLRLEVNMQAMKAQFERdlQNRDDSNDE 1589
Cdd:TIGR00606 587 NQTRDRLA----KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEK--SSKQRAMLA 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1590 KKKLLFKQVREMEVELEEERKQKSQ-ILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAAR 1668
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1669 DEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQErDDLADELSNGVSGKSALLDEKRALEMRISQleeeldee 1748
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQ-------- 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1749 qsntelindryrkltlqvetittelsaersfsQKAENARQQMERQNKELKVKLNEMDSTMRskykitiasleaKISQLEE 1828
Cdd:TIGR00606 811 --------------------------------QAAKLQGSDLDRTVQQVNQEKQEKQHELD------------TVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1829 QMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELE 1908
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810
....*....|.
gi 1785379715 1909 DVTESAESMNR 1919
Cdd:TIGR00606 927 ELISSKETSNK 937
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1485-1719 |
4.58e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 44.71 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1485 ALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKnvhelerSKRALEQQVQEMKTQIEELEDELQAIEDGKLR 1564
Cdd:COG4942 19 ASLLSAAVLAAAFSAAADDKQLKQIQKEIAALEKKIREQQD-------QRAKLEKQLKSLETEIASLEAQLIETADDLKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1565 LEVNMQAMKAQFERdLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMesqmdsaNKGRDEAV 1644
Cdd:COG4942 92 LRKQIADLNARLNA-LEVQEREQRRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGAL-------NPARAERI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379715 1645 KQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSN 1719
Cdd:COG4942 164 DALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKN 238
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
884-1260 |
4.88e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 44.88 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 884 QLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEE 963
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEELA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 964 GARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNklrnkyeaviADLEDRL 1043
Cdd:pfam07888 115 EEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQ----------AKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1044 KKEEKGRQEMEKMKRKLDGETTDLqdqllelqqqieelkQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAEL 1123
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQV---------------LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1124 HEDLESEKAARAKAEKQRRDLGEELEALKTELEDT----LDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQ 1199
Cdd:pfam07888 250 ERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLtlqlADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379715 1200 RHNQVVEEISE----QLEQARRFKGNLEKVKQT------LESENTDLIKEVKNLQAAKQDSEQRRKKLEQQ 1260
Cdd:pfam07888 330 LEERLQEERMEreklEVELGREKDCNRVQLSESrrelqeLKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1104-1886 |
5.91e-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: 44.96 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1104 GQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTI 1183
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1184 EEDVKvrdaqvtEMRQRHNQVVEEISEQLEQARRFKgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSE 1263
Cdd:TIGR00618 232 REALQ-------QTQQSHAYLTQKREAQEEQLKKQQ--LLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1264 FQIRtNESEKVKFELAEKLQKLQAELDGVSGALgSTEGKSIKLTKDLSTVQSQ------LQDTQELLQEETRQKLNFSSR 1337
Cdd:TIGR00618 303 TQIE-QQAQRIHTELQSKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQeihirdAHEVATSIREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1338 VRQLEEEKNNLMENLEeeeSAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAmEEAKKKSYKELEFLQQRFDEKHQIndk 1417
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQ---SLCKELDILQREQATIDTRTSAFRDLQGQLAHA-KKQQELQQRYAELCAAAITCTAQC--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1418 lEKTRNRLQQELddlmvdldhqrqivsnlEKKQKKFDQMLAEEKNISARygeerdraeaearEKETKALSLSRALEEAiD 1497
Cdd:TIGR00618 454 -EKLEKIHLQES-----------------AQSLKEREQQLQTKEQIHLQ-------------ETRKKAVVLARLLELQ-E 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1498 LKDELDRQNKQLRAEMDDLvsskDDVGKNVHELERskraLEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFE 1577
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDI----DNPGPLTRRMQR----GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1578 RDLQNRDDSNDEKKKLLfKQVREMEVELEEERKQKSQILAAKKKLEMDLQDmesqmdSANKGRDEAVKQLKKLQLQFKEV 1657
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQP------EQDLQDVRLHLQQCSQELALKLT 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1658 WREVEETRAARDEIfvqsRDNEKKLKSLEAELLQL-QEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEM 1736
Cdd:TIGR00618 647 ALHALQLTLTQERV----REHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1737 RISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMrskykiti 1816
Cdd:TIGR00618 723 IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-------- 794
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1817 ASLEAKISQLEEQMEQESKERiianklvrraekrLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQL 1886
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSD-------------EDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1773-1884 |
6.10e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1773 LSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQesKERIIANKL--VRRAEKR 1850
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQ--KEENLDRKLelLEKREEE 111
|
90 100 110
....*....|....*....|....*....|....
gi 1785379715 1851 LKEVLLQVEEERRNADQFKEQLEKanIRMKQLKR 1884
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEE--LIEEQLQE 143
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1820-1938 |
6.58e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1820 EAKISQLEEQMEQESKEriiANKlvrRAEKRLKEVLLQVEEERRNA-DQFKEQLEKANIRMKQLKRQLEEAEEEASRANS 1898
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE---AKK---EAEAIKKEALLEAKEEIHKLrNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1785379715 1899 NRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKR 1938
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1475-1837 |
6.94e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 44.49 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1475 EAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDE 1554
Cdd:pfam07888 58 EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEELAEEKDALLAQRAESEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1555 LQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVremeveleeerkqksQILAAKKKLEMDLQDMESQMD 1634
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQAKLQ---------------QTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1635 SankgRDEAVKQLK----KLQLQFKEVWREVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLA--AAERAKRQAQQ 1708
Cdd:pfam07888 203 Q----RDTQVLQLQdtitTLTQKLTTAHRKEAENEALLEEL----RSLQERLNASERKVEGLGEELSsmAAQRDRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1709 ERDDL-ADELSNGVSGKSALLDEKRAlemrisQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAE--- 1784
Cdd:pfam07888 275 HQARLqAAQLTLQLADASLALREGRA------RWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEvel 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1785 -NARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAK------ISQLEEQMEQESKER 1837
Cdd:pfam07888 349 gREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKqelleyIRQLEQRLETVADAK 408
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
860-1561 |
8.07e-04 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 44.45 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 860 ELQKVKDTQVKTESELKEMAnKYQQLFEEKsilaeqlqaetelfaeaEEMRARLASKKQELEEILHDLEArvEEEEERTL 939
Cdd:COG4717 186 LLEKLKQERNEIDEAEKEYA-TYHKLLESR-----------------RAEHARLAELRSELRADRDHIRA--LRDAVELW 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 940 QLQNEKKKMHQHIqDLEEQLEEEEGARQKLQLEKVttESRLKKMEEDILLLEDQNAKLAKERKLLddrigeftstmAEEE 1019
Cdd:COG4717 246 PRLQEWKQLEQEL-TRRREELATFPRDGVLRLEKR--EAHLQKTEAEIDALLVRLAELKDLASQL-----------IPAK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1020 EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV 1099
Cdd:COG4717 312 EAVLQALVRLHQQLSEIKASAFELTETLAGIEADLRDKEEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEAAYCKR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1100 DDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1179
Cdd:COG4717 392 LDEKRLFEDEAEEEARQRLADDEEEVRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTAWQKQRFLREKQTAFERQKTEH 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1180 KKTIeedvKVRDAQVTemrqrhnQVVEEISEQLEQARRFKGnlEKVKQTLESENTDLIKEVKNLQAAKQDSEQrrKKLEQ 1259
Cdd:COG4717 472 TKII----ALRLAGML-------LVALSRLLTSLIFQIIFA--VAQIVFLSAEIKSSSRAVREEKAAVTDIPE--ELARL 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1260 QVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKsikltkdlstvQSQLQDTQELLQEETRQKLNFSSRVR 1339
Cdd:COG4717 537 LITDELPELAVDLLVQSRIRQHWQQLRKALDQLEAAYEALEGR-----------FAAAEAAMAEWQSEWEEALDELGLSR 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1340 QLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKkksYKELEFLQQRFDEKHQINDKLE 1419
Cdd:COG4717 606 ELSPEQQLDILSTMKDLKKLMQKKAELTHQVARLREEQAAFEERVEGLLAVLEAQ---FIDLSTLFCVQRLRVAAELQKE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1420 KTRNRLQQELDDLMVDLDHQRQivsNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLK 1499
Cdd:COG4717 683 EARLALEGNIERTKELNDELRA---ELELHRKEILDLFDCGTADTEDAFREAAREEQQLTQRESRLESLEAQLEGVAAEA 759
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 1500 DELDRQNKQlraemddlvssKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDG 1561
Cdd:COG4717 760 YELSASLDQ-----------RELKEEELALLEEAIDALDEEVEELHAQVAALSRQIAQLEGG 810
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1487-1584 |
8.37e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 431934 [Multi-domain] Cd Length: 151 Bit Score: 41.92 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1487 SLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLE 1566
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90
....*....|....*...
gi 1785379715 1567 VNMQAMKAQFERDLQNRD 1584
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRD 139
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
981-1284 |
8.90e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 44.25 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 981 KKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKL 1060
Cdd:COG4372 67 RNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1061 DgETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVgqknnllkqlRDLqsqlaelhedleseKAARAKAEKQ 1140
Cdd:COG4372 147 Q-DLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQV----------LDL--------------KLRSAQIEQE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1141 RRDLGEELEALKTELEDTLDSTAAQQELRAKREQevtdlkktieedvkvRDAQVTEMRQRHNQVVEEISEQLEQARRfkg 1220
Cdd:COG4372 202 AQNLATRANAAQARTEELARRAAAAQQTAQAIQQ---------------RDAQISQKAQQIAARAEQIRERERQLQR--- 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379715 1221 nlekvkqtLESENTDLIKEVKNLQAAKQDS-EQRRKKLEQQVSEFQ----IRTNESEKVKFELAEKLQK 1284
Cdd:COG4372 264 --------LETAQARLEQEVAQLEAYYQAYvRLRQQAAATQRGQVLagaaQRVAQAQAQAQAQAQLLSS 324
|
|
| MscK |
COG3264 |
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis]; |
1092-1297 |
1.11e-03 |
|
Small-conductance mechanosensitive channel [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225803 [Multi-domain] Cd Length: 835 Bit Score: 43.91 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1092 LQAALA-RVDDEVGQKNNLLKQLRDLQSQLAELHEdLESEKAArAKAEKQRRDLGEELEALKtELEDTLD------STAA 1164
Cdd:COG3264 9 LQELLQsRRELLTAESAQLEAALQLLQEAVNSKRQ-EEAEPAA-EEAELQAELIQQELAIND-QLSQALNqqterlNALA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1165 QQELRAK--REQeVTDLKKTIEEDVKVRDAQVTEMRQRhNQVVEEISEQLEQARRFKGNLEKVK-QTLESENTDLIKEVK 1241
Cdd:COG3264 86 SDDRQLAnlLLQ-LLQSSRTIREQIAVLRGSLLLSRIL-LQQLGPLPEAGQPQEQFEVTQERDAlQAEKAYINALEGQAE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 1242 NL-QAAKQDSEQ----RRKKLEQQVSEfqiRTNESEKVKFELAEK-LQKLQAELDGVSGALG 1297
Cdd:COG3264 164 QLtAEVRDILDQildtRRELLNSLLSQ---REAISLQLNQQQLSAaSDELRSLLHQQSFWVS 222
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1124-1482 |
1.21e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1124 HEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEvtdLKKTIEEDVKVRDAQVTEmrqrhnq 1203
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKRELERIRQ------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1204 vvEEISEQLEQARRfkgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFqirtnesEKVKFElaeklq 1283
Cdd:pfam17380 368 --EEIAMEISRMRE----LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM-------EQIRAE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1284 klqaeldgvsgalgstegksikltkdlstvqsqlqdtqellQEETRQKlnfssRVRQLEEEKNNLMENLEEEESAKAQLS 1363
Cdd:pfam17380 429 -----------------------------------------QEEARQR-----EVRRLEEERAREMERVRLEEQERQQQV 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1364 RQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKsykeleFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDL--DHQRQ 1441
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK------ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRR 536
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1785379715 1442 IVSNLEKKQKKFDQMLAEEKNISaRYGEERDRAEAEAREKE 1482
Cdd:pfam17380 537 EAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMERERE 576
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1530-1939 |
1.44e-03 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 43.61 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1530 LERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKqVREMEVELEEER 1609
Cdd:pfam01576 66 LAARKQELEEILHELEARLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAK-IKKMEEDILLLE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1610 KQKSQILAAKKKLEMDLQDMESQMDSankgRDEAVKQLKKLQLQFKEVWREVEEtRAARDEIFVQsrDNEKKLKSLEAEL 1689
Cdd:pfam01576 145 DQNNKLQKERKLLEERISEFTSNLAE----EEEKSKSLNKLKNKHEAMISDLED-RLKKEEKGRQ--ELEKAKRKLEGES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1690 LQLQEDLAaaeraKRQAQqerddlADELSNGVSGKSallDEKRALEMRISQLEEELDEEQSNTelindryRKLTLQVETI 1769
Cdd:pfam01576 218 SDLQEQIA-----ELQAQ------IAELRAQLAKKE---EELQAALARLEEETAQKNAALKKL-------RELEAQLSEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1770 TTELSAERSFSQKAENARQQMERQNKELKVKLNE-MDST-----MRSKYkitiaslEAKISQLEEQMEQESKERiiaNKL 1843
Cdd:pfam01576 277 QEDLESERAARAKAEKQRRDLGEELEALKTELEDtLDTTaaqqeLRSKR-------EQEVTELKKALEEETRSH---EAQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1844 VRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEdvtesaesmnREVTT 1923
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAKQDSEHKRKKLE----------GQLQE 416
|
410
....*....|....*.
gi 1785379715 1924 LRSRLSKLERQQRKRA 1939
Cdd:pfam01576 417 LQSRLSESERQRAELA 432
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1082-1257 |
1.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1082 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDS 1161
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1162 TAAQQELRAKREQEVTDLKKTIEedvkvrdaqvtEMRQRHNQVVEEISE-QLEQARRFKgnLEKVKQTLESENTDLIKEV 1240
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELE-----------ELIEEQLQELERISGlTAEEAKEIL--LEKVEEEARHEAAVLIKEI 178
|
170
....*....|....*..
gi 1785379715 1241 KNLqaAKQDSEQRRKKL 1257
Cdd:PRK12704 179 EEE--AKEEADKKAKEI 193
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
971-1265 |
1.73e-03 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 43.20 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 971 LEKVTTESRLKKM-EEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKE--- 1046
Cdd:COG3206 95 LEKVIDKLKLDDDpEFVGKPLIASFLRLLKDLIGPDPTIFEISYRLDDLLESLKVLRAGRSRVIELSYTSNDPKLAAkla 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1047 EKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAelhed 1126
Cdd:COG3206 175 NALAQAYLADQLEAQLEAFRRASDSLDERLEELRARLQEAEAQVEDFRAQHGLTDAARGQLLSEQQLSALNTQLQ----- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1127 leSEKAARAKAEKQRRDLGEELEAlkTELEDTLDSTAAQQELRAKREQEVTdlKKTIEEDVKvrdaqvTEMRQRHNQVVe 1206
Cdd:COG3206 250 --SARARLAQAEARLASLLQLLPL--GREAAALREVLESPTIQDLRQQYAQ--VRQQIADLS------TELGAKHPQLV- 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379715 1207 EISEQLEQARRF-KGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKL---EQQVSEFQ 1265
Cdd:COG3206 317 ALEAQLAELRQQiAAELRQILASLPNELALLEQQEAALEKELAQLKGRLSKLpklQVQLRELE 379
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1104-1341 |
1.76e-03 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1104 GQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQqelrakreqevtdLKKTI 1183
Cdd:pfam07902 71 GESTGLFKSLEEMLSQLKELNLELTDTKNSNLWSKIKLNNNGMLREYHNDTIKTEIVESAEG-------------IATRI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1184 EEDVKVRDAQVTEMRQRHNQVVEEISEQLeqARRFKGNLEKVKQTLESENTDLIKEVKNLQ---AAKQDSEQRR------ 1254
Cdd:pfam07902 138 SEDTDKKLALINETISGIRREYQDADRQL--SSSYQAGIEGLKATMASDKIGLQAEIQASAqglSQRYDNEIRKlsakit 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1255 -----------KKLEQQVSEFqirTNESEKVKFELAEKLQKL----QAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQD 1319
Cdd:pfam07902 216 ttssgtteayeSKLDDLRAEF---TRSNQGMRTELESKISGLqstqQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQD 292
|
250 260 270
....*....|....*....|....*....|...
gi 1785379715 1320 TQEL----------LQEETR-QKLNFSSRVRQL 1341
Cdd:pfam07902 293 AEKNyssltqtvkgLQSTVSdPNSKLESRITQL 325
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1490-1560 |
2.05e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.75 E-value: 2.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1490 RALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSK---RALEQQVQEMKTQIEELEDELQAIED 1560
Cdd:PRK05431 21 RGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEA 94
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1112-1321 |
2.08e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 429718 [Multi-domain] Cd Length: 488 Bit Score: 42.95 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1112 QLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELedtlDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1191
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEELAEEK----DALLAQRAESEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1192 AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLikevknlQAAKQDSEQRRKKLEQQVSEFQIRTNES 1271
Cdd:pfam07888 150 TELERMKERVKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF-------QELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1272 EKVKFELAEkLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQ 1321
Cdd:pfam07888 223 TTAHRKEAE-NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQ 271
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1388-1937 |
2.10e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1388 EAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARY 1467
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1468 GEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDdlVSSKDDVGKNVHELERSKRAL---EQQVQEM 1544
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKIQHLEEEYKKEIndkEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1545 KTQIEELEDELQaieDGKLRLEVNMQAMKaqferDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEM 1624
Cdd:pfam05483 246 LIQITEKENKMK---DLTFLLEESRDKAN-----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1625 DLQ-----------DMESQMDSANKGRDE---------------------AVKQLKKLQLQFKEVWREVEETRAARDEIF 1672
Cdd:pfam05483 318 DLQiatkticqlteEKEAQMEELNKAKAAhsfvvtefeattcsleellrtEQQRLEKNEDQLKIITMELQKKSSELEEMT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1673 VQSRDNEKKLKSLEAELLQLQ---------EDLAAAERAKRQA--------QQERDDLADELSNGVSGKSALLDEKRALE 1735
Cdd:pfam05483 398 KFKNNKEVELEELKKILAEDEklldekkqfEKIAEELKGKEQElifllqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1736 MRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERsfsQKAENARQQMERQNK------ELKVKLNEMDSTMR 1809
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ---EDIINCKKQEERMLKqienleEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1810 SKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKE--------------QLEKA 1875
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkalkkkgsaenkQLNAY 634
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 1876 NIRMKQLKRQLEEAEEEASRANSNrrrLQRELEDVTESAESMNREVTTLRSRLSKLERQQRK 1937
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDN---YQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1131-1344 |
2.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1131 KAARAKAEKQRRDLGEELEALKTEledtldstaaqQELRAKreQEVTDLKKTIEEDVKVRDaqvtemrqrhnqvvEEISE 1210
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKE-----------ALLEAK--EEIHKLRNEFEKELRERR--------------NELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1211 QLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEqqvsefqirtnesekvkfelaEKLQKLQAELD 1290
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELE---------------------ELIEEQLQELE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1291 GVSGaLGSTEGKSIKLTKdlstvqsqlqdtqelLQEETRQKLnfSSRVRQLEEE 1344
Cdd:PRK12704 146 RISG-LTAEEAKEILLEK---------------VEEEARHEA--AVLIKEIEEE 181
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1428-1651 |
2.68e-03 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 42.32 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1428 ELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREketkalsLSRALEEAIDLKDELDRQNK 1507
Cdd:COG4372 75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAA-------ARQNLAKAQQELARLTKQAQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1508 QLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQfERDLQNRDDSn 1587
Cdd:COG4372 148 DLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQAR-TEELARRAAA- 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379715 1588 dekkkllFKQVREMEVELEEERKQKSQILAAKkklEMDLQDMESQMDSANKGRDEAVKQLKKLQ 1651
Cdd:COG4372 226 -------AQQTAQAIQQRDAQISQKAQQIAAR---AEQIRERERQLQRLETAQARLEQEVAQLE 279
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1211-1912 |
3.12e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 42.57 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1211 QLEQARRFKGNLEKVKQTLESEN---TDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKF------ELAEK 1281
Cdd:COG3096 284 HLDQALEFRRELYTSRQQLAAEQyrhVDMSRELAELNGAEGDLEADYQAASDHLNLVQTALRQQEKIERyqadleELTIR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1282 LQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQ 1361
Cdd:COG3096 364 LEEQNEVVEEANERQEENEARAEAAELEVDELKSQLADYQQALDVQQTRAIQYQQAIAALERAKELCHLPDLTADSAEEW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1362 LSRQLQALQQQLlESKKRMEDQGGMVEAMeeakkksykeleflQQRFDEKHQINDKL--EKTRNRLQQELDDLM---VDL 1436
Cdd:COG3096 444 LETFQAKEEEAT-EKLLSLEQKMSMAQAA--------------HSQFEQAYQLVVAIagELARSEAWDVARELLregPDQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1437 DHQRQIVSNLEKKQKKFDQMLAEEK---------NISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNK 1507
Cdd:COG3096 509 RHLAEQVQPLRMRLSELEQRLRQQQsaerlladfCKRQGKNLDAEELEALHQELEALIESLSDSVSNAREQRMALRQEQE 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1508 QLRAEMDDLVS------SKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDgklRLEVNMQAMKAQFERdLQ 1581
Cdd:COG3096 589 QLQSRIQSLMQrapvwlAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLEREREATVERD---ELGARKNALDEEIER-LS 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1582 NRDDSNDEKKKLLFK-----------------------------QVREMEVELEEERKQKSQILAAKKKL---EMDLQDM 1629
Cdd:COG3096 665 QPGGSEDQRLNALAErfggvllseiyddvtiedapyfsalygpsRHAIVVPDLSQVKEHLEGLTDCPEDLyliEGDPQSF 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1630 ESQMDSANKGRDEAVKQLKKLQLQ---------FKEVWRE--VEETRAARDEI---FVQSRDNEKKLKSLEAELLQ-LQE 1694
Cdd:COG3096 745 DDSVFSVDELEKAVVVKIADRQWRysrfpeiplFGRAAREqrLESLHAERDVLserHATLSFDVQKTQRLHQAFSRfIGS 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1695 DLAAA-----ERAKRQAQQERDDLADELSNGVSGK------------------------SALLDEkrALEMRISQLEEEL 1745
Cdd:COG3096 825 HLAVAfeadpEAEIRQLNSRRNELERALSNHENDNqqqriqfdqakegvtalnrlipqlNLLADE--SLADRVEEIRERL 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1746 DEEQSNTELINDRYRKLTlQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITI---ASLEAK 1822
Cdd:COG3096 903 DEAQEAARFIQQHGNTLS-KLEPIASVLQSDPEQFEQLKEDYAQAQQMQRQARQQAFALTEVVQRRAHFSYsdsAEMLSE 981
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1823 ISQLEEQM----EQESKERIIANKLVRRAEKRLKE---VLLQV------------------------------EEERRNA 1865
Cdd:COG3096 982 NSDLNEKLrqrlEQAEAERTRAREQLRQHQAQLSQynqVLASLkssydtkkellnelqqelqdigvradsgaeERARIRR 1061
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1785379715 1866 DQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTE 1912
Cdd:COG3096 1062 DELHAQLSTNRSRRNQLEKQLTFCEAEMDNLTRKLRKLERDYFEMRE 1108
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
1120-1432 |
3.15e-03 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 42.28 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1120 LAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKReQEVTDLKKTIEEDVKVRDAQVTEMRQ 1199
Cdd:COG5185 245 LKLEDNYEPSEQELKLGFEKFVHIINTDIANLKTQNDNLYEKIQEAMKISQKI-KTLREKWRALKSDSNKYENYVNAMKQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1200 RH-------NQVVEEISEQLEQARRFKGNLEKVKQTLESE----------NTDLIKEVKNLQAAKQDSEQRRKKLEQQVS 1262
Cdd:COG5185 324 KSqewpgklEKLKSEIELKEEEIKALQSNIDELHKQLRKQgisteqfelmNQEREKLTRELDKINIQSDKLTKSVKSRKL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1263 EFQIRTNESEKVKFE-------------------------------------LAEKLQKLQAELDGVSGALGSTE-GKSI 1304
Cdd:COG5185 404 EAQGIFKSLEKTLRQydsliqnitrsrsqighnvndsslkinieqlfpkgsgINESIKKSILELNDEIQERIKTEeNKSI 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1305 KLTKDLSTVQSqlqDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEeeeSAKAQLSRQLQALQQQLLESKKRMEDQG 1384
Cdd:COG5185 484 TLEEDIKNLKH---DINELTQILEKLELELSEANSKFELSKEENERELV---AQRIEIEKLEKELNDLNLLSKTSILDAE 557
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1385 GMVEAME-----------EAKKKSYKEL-EFLQQRFDEKHQINDKLEKTRNRLQQELDDL 1432
Cdd:COG5185 558 QLVQSTEikldelkvdlnRKRYKIHKQViHVIDITSKFKINIQSSLEDLENELGKVIEEL 617
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
928-1326 |
3.46e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 428520 [Multi-domain] Cd Length: 660 Bit Score: 42.41 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 928 EARVEEEEERTLQLQNEKKKMhqhiqdleeqleEEEGARQKLQLEKVTTESRLKKMEEdilllEDQNAKLAKERKLLDDR 1007
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQM------------ELEHKRARIELERKASALARQLERE-----SDRNQELQKRIRLLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1008 IGEFTSTMAEEEEkvksLNKLRNKYEAVIADLEdrlKKEEKGRQEMEKMKRKLDGETtdlqdqlLELQQQIEELKQQLAR 1087
Cdd:pfam05557 64 EAEAEEALREQAE----LNRLKKKNLEALNKKL---NEKESQLADAREVISCLKNEL-------SELRRQIQRQELELSS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1088 KEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDlGEELEALKTELEDTLDSTAAQQE 1167
Cdd:pfam05557 130 TNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELERELER 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1168 LRAKREQ-------------EVTDLKKTIEEDVKVRDAQVT-EMRQRHNQVVEEISEQLEQ-----------ARRFKGNL 1222
Cdd:pfam05557 209 LREHNKHlnenienklllkeEVEDLKRKLEREEGYREELATlELEKEKLEQELKSWEKLAQdtglnlrspedLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1223 EKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGS---- 1298
Cdd:pfam05557 289 QQREITLKEENSSLTSSARQLEKAQRELEQELAQYLKNIEDLNKKLKRHKALVRRLQRRVLLLTKERDGMRAILESydke 368
|
410 420 430
....*....|....*....|....*....|
gi 1785379715 1299 --TEGKSIKLTKDLSTVQSQLQDTQELLQE 1326
Cdd:pfam05557 369 ltPSNYSPQLLERIEEAEDMTQDMQAHNEE 398
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1105-1693 |
4.16e-03 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 42.14 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1105 QKNNLLKQLRDLQSQLAELhedlESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQEL--RAKREQEvtdlKKT 1182
Cdd:COG4717 182 QINQLLEKLKQERNEIDEA----EKEYATYHKLLESRRAEHARLAELRSELRADRDHIRALRDAveLWPRLQE----WKQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1183 IEEdvkvrdaQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVs 1262
Cdd:COG4717 254 LEQ-------ELTRRREELATFPRDGVLRLEKREAHLQKTEAEIDALLVRLAELKDLASQLIPAKEAVLQALVRLHQQL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1263 efqirtNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLE 1342
Cdd:COG4717 326 ------SEIKASAFELTETLAGIEADLRDKEEAAGNGFEAERVHDLRSLECMLRYQSSQRELKQTEAAYCKRLDEKRLFE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1343 EEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEflQQRFDEKHqindKLEKTR 1422
Cdd:COG4717 400 DEAEEEARQRLADDEEEVRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTAWQKQRFLRE--KQTAFERQ----KTEHTK 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1423 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLK--D 1500
Cdd:COG4717 474 IIALRLAGMLLVALSRLLTSLIFQIIFAVAQIVFLSAEIKSSSRAVREEKAAVTDIPEELARLLITDELPELAVDLLvqS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1501 ELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQI--------EELEDELQAIEDGKlRLEVNMQAM 1572
Cdd:COG4717 554 RIRQHWQQLRKALDQLEAAYEALEGRFAAAEAAMAEWQSEWEEALDELglsrelspEQQLDILSTMKDLK-KLMQKKAEL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1573 KAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILA------AKKKLEMDLQDMESQMDSANKGRDEAVKQ 1646
Cdd:COG4717 633 THQVARLREEQAAFEERVEGLLAVLEAQFIDLSTLFCVQRLRVAAelqkeeARLALEGNIERTKELNDELRAELELHRKE 712
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1785379715 1647 LKKLqLQFKEVWREVEETRAARDEifVQSRDNEKKLKSLEAELLQLQ 1693
Cdd:COG4717 713 ILDL-FDCGTADTEDAFREAAREE--QQLTQRESRLESLEAQLEGVA 756
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1402-1925 |
4.45e-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: 42.12 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1402 EFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaEEKNISARYGEERDR-----AEA 1476
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML-QSKGLPKKSGEEDWErtrriAEA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1477 EAREKETKALsLSRALEEAIDLKDELDRQNK--QLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQE----------- 1543
Cdd:pfam10174 191 EMQLGHLEVL-LDQKEKENIHLREELHRRNQlqPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhted 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1544 -----------------MKTQIEELEDELQAIE------------------DGKLRLEVNMQAMKAQFERD--LQNRDDS 1586
Cdd:pfam10174 270 reeeikqmevykshskfMKNKIDQLKQELSKKEsellalqtkletltnqnsDCKQHIEVLKESLTAKEQRAaiLQTEVDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1587 ----NDEKKKLLFKQVremeveleeerKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVE 1662
Cdd:pfam10174 350 lrlrLEEKESFLNKKT-----------KQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1663 ETRAARDEIFVQSRDNEKKLKSLEaELLQLQEDLAAA-----ERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMR 1737
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLE-EALSEKERIIERlkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESS 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1738 ISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQmERQNKELKVKLNEMDSTMrSKYKITIA 1817
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQEV-ARYKEESG 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1818 SLEAKISQL-----EEQMEQESKERIIANkLVRRAEKRLKEV--------LLQVEEERRNADQFKEQL-EKANIRMKQLK 1883
Cdd:pfam10174 576 KAQAEVERLlgilrEVENEKNDKDKKIAE-LESLTLRQMKEQnkkvanikHGQQEMKKKGAQLLEEARrREDNLADNSQQ 654
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1785379715 1884 RQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLR 1925
Cdd:pfam10174 655 LQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR 696
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1537-1937 |
4.50e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1537 LEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKllfkqvremeveleeerkQKSQIl 1616
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK------------------NKDKI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1617 aakKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWR-------EVEETRAARDEIFVQSRDNEKKLKSLEAEL 1689
Cdd:TIGR04523 99 ---NKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKnidkfltEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1690 LQLQEDLAAAERAKRQAQQERDDLADELSNGVSgksaLLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETI 1769
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK----KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1770 TTELSAERSFSQKA----ENARQQMERQNKELKVKLNEMdstmrSKYKITIASLEAK-----ISQLEEQMEQESKERIIA 1840
Cdd:TIGR04523 252 QTQLNQLKDEQNKIkkqlSEKQKELEQNNKKIKELEKQL-----NQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1841 NKLVRRAEK---RLKEVLLQVEEERRNAD----QFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTES 1913
Cdd:TIGR04523 327 QNQISQNNKiisQLNEQISQLKKELTNSEsensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420
....*....|....*....|....
gi 1785379715 1914 AESMNREVTTLRSRLSKLERQQRK 1937
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIER 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1006-1935 |
4.95e-03 |
|
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: 41.96 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1006 DRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETtdlqDQLLELQQQIEELKQQL 1085
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL----DPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1086 ARKEEELQAALARVDDEVGQKNNL-LKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtLDSTAA 1164
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKDNSELeLKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL-LNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1165 QQELRAKREQEVTDLkktIEEDVKVRDAQVTEMRQRHNqvVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1244
Cdd:TIGR00606 344 ELLVEQGRLQLQADR---HQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1245 AAKQDSEQRRKKLEQQVSEFQiRTNESEKvkfelaEKLQKLQAELDGVSGALGSTEGKS---IKLTKDLSTVQSQLQDTQ 1321
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLG-RTIELKK------EILEKKQEELKFVIKELQQLEGSSdriLELDQELRKAERELSKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1322 ELLQEETRQKlnfssRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQggmvEAMEEAKKKSYKEL 1401
Cdd:TIGR00606 492 KNSLTETLKK-----EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD----EQIRKIKSRHSDEL 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1402 EFLQQRFDEKHQINDKLEKTRNRLQQ---ELDDLMVDLDHQRQIVSNLEKKQKKFD-QMLAEEKNISARYGEERDRAEAE 1477
Cdd:TIGR00606 563 TSLLGYFPNKKQLEDWLHSKSKEINQtrdRLAKLNKELASLEQNKNHINNELESKEeQLSSYEDKLFDVCGSQDEESDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1478 AREKETKALSLSRALEEAidLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQA 1557
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAG--ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1558 IEdgKLRLEVNMQAMKAQFERDLqnrddsndeKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSAN 1637
Cdd:TIGR00606 721 KE--KRRDEMLGLAPGRQSIIDL---------KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1638 KgrdeaVKQLKKLQLQFKEVWREVEETRAArdeifVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADEL 1717
Cdd:TIGR00606 790 D-----VTIMERFQMELKDVERKIAQQAAK-----LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1718 SNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKEL 1797
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1798 KVKLNEMDSTMRSKYkITIASLEAKIsqleeqmeQESKERIIANKlvrraEKRLKEVLLQVEEERRNADQFKEQLEKANI 1877
Cdd:TIGR00606 940 QDKVNDIKEKVKNIH-GYMKDIENKI--------QDGKDDYLKQK-----ETELNTVNAQLEECEKHQEKINEDMRLMRQ 1005
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379715 1878 RMKQLKRQleeaeEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQ 1935
Cdd:TIGR00606 1006 DIDTQKIQ-----ERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK 1058
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1457-1558 |
5.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1457 LAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAE------------------MDDLVS 1518
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElqklekrllqkeenldrkLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1785379715 1519 SKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAI 1558
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1682-1937 |
5.18e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 41.63 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1682 LKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQleeeldeeqsntelINDRYRK 1761
Cdd:COG4942 33 AAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKK--------------LRKQIAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1762 LTLQVETITTELSAERSFSQKAENARQQMERqNKELKVKLNEMDSTMrskykitiaslEAKISQLEEQMEQESKERIIAN 1841
Cdd:COG4942 99 LNARLNALEVQEREQRRRLAEQLAALQRSGR-NPPPALLVSPEDAQR-----------SVRLAIYYGALNPARAERIDAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1842 KLVRRAEKRLKEVLLQVEEERRNA----DQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESM 1917
Cdd:COG4942 167 KATLKQLAAVRAEIAAEQAELTTLlseqRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAA 246
|
250 260
....*....|....*....|
gi 1785379715 1918 NREVTTLRSRLSKLERQQRK 1937
Cdd:COG4942 247 AAKAREAAAAAEAAAARARA 266
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1471-1698 |
5.23e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1471 RDRAEAEAREKETKALSLSRALEEAID-LKDELDRQNKQLRAEMDDLVSSKDDVGKnvhELERSKRALEQQVQEMKTQIE 1549
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEALDkLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1550 ELEDELQAIEDGKLRLEVnmqaMKAqFERDLQNRDDS----------NDEKKKLLFKQVREMEVELEEERKQKSQILAAK 1619
Cdd:PRK05771 111 ELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVVVV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379715 1620 KKlemdlqdmesqmdsanKGRDEAVKQLKKlqLQFKEVwrEVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLAA 1698
Cdd:PRK05771 186 LK----------------ELSDEVEEELKK--LGFERL--ELEEEGTPSELI----REIKEELEEIEKERESLLEELKE 240
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1083-1251 |
5.35e-03 |
|
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: 41.67 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1083 QQLARKEEELQA-ALARVDDEVGQKNNLLKQLRDLQSQLAELH-------EDLESEKAARAKAEKQRRDLGEELEALKTE 1154
Cdd:pfam09731 297 DQLSKKLAELKKrEEKHIERALEKQKEELDKLAEELSARLEEVraadeaqLRLEFEREREEIRESYEEKLRTELERQAEA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1155 LEDTLDSTAAQQELRAKREQEvTDLKKTIEEDVKVRDAQVTEMRQRHN---QVVEEISEQLEQARRFK---GNLEKVKQT 1228
Cdd:pfam09731 377 HEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRKAQqlwLAVEALRST 455
|
170 180
....*....|....*....|....*...
gi 1785379715 1229 LESENTD-----LIKEVKNLQAAKQDSE 1251
Cdd:pfam09731 456 LEDGSADsrprpLVRELKALKELASDDE 483
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1082-1284 |
5.83e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1082 KQQLARKEEELQ-------AALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEK----QRRDLGEELEA 1150
Cdd:PRK11637 53 QQDIAAKEKSVRqqqqqraSLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQqqaaQERLLAAQLDA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1151 L-----KTELEDTLDSTAAQQE---------LRAKREQEVTDLKKTIEEdvkvRDAQVTEMRQRHNQVVEEISEQLEQAR 1216
Cdd:PRK11637 133 AfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREE----LAAQKAELEEKQSQQKTLLYEQQAQQQ 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379715 1217 RFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTN----ESEKVKFELAEKLQK 1284
Cdd:PRK11637 209 KLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAErearEAARVRDKQKQAKRK 280
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
992-1181 |
5.84e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 992 DQNAKLAKERK----LLDDRIGEFTSTMAEEEEkvkSLNKLRNKYEAVIADLEdRLKKEEKgrqemekMKRKlDGETTDL 1067
Cdd:PHA02562 223 DELVEEAKTIKaeieELTDELLNLVMDIEDPSA---ALNKLNTAAAKIKSKIE-QFQKVIK-------MYEK-GGVCPTC 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1068 QDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQ---LRDLQSQLAELHEDLESE-------KAARAKA 1137
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLvdkakkvKAAIEEL 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1785379715 1138 EKQRRDLGEELEALKTELEDtLDSTAAQQELRAKREQEVTDLKK 1181
Cdd:PHA02562 371 QAEFVDNAEELAKLQDELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1379-1940 |
7.69e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1379 RMEDQGGMVEAMEEAKKKSYKELEFLQQRfdekhqinDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1458
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQK--------REAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1459 EEK--NISARYGE-ERDRAEAEAREKETKALSLSRALEEAIDLKDELD----RQNKQLRAEMDDLVSSKDDVGKNVHELE 1531
Cdd:TIGR00618 292 AAPlaAHIKAVTQiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeqRRLLQTLHSQEIHIRDAHEVATSIREIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1532 RSKRALEQQVQEMKTQIEELEDELQAI--EDGKLRLEVNMQAMKAQFERDLQN-----RDDSNDEKKKLLFKQVREMEVE 1604
Cdd:TIGR00618 372 CQQHTLTQHIHTLQQQKTTLTQKLQSLckELDILQREQATIDTRTSAFRDLQGqlahaKKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1605 LEEERKQKSQI-----LAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSR--- 1676
Cdd:TIGR00618 452 QCEKLEKIHLQesaqsLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmq 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1677 ---DNEKKLKSLEAELL-QLQEDLAAAERAKRQAQQERDDLAdELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNT 1752
Cdd:TIGR00618 532 rgeQTYAQLETSEEDVYhQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1753 ELINDRyRKLTLQVETITTELSA-ERSFSQKAENARQQMERQNKEL-KVKLNEMDSTMRSKYKITIASLEAKISQLEEQM 1830
Cdd:TIGR00618 611 ACEQHA-LLRKLQPEQDLQDVRLhLQQCSQELALKLTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMQSEK 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1831 EQESKERII---ANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEA--SRANSNRRRLQR 1905
Cdd:TIGR00618 690 EQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEE 769
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1785379715 1906 ---------ELEDVTESAESMNREVTTLRSRLSKLERQQRKRAP 1940
Cdd:TIGR00618 770 vtaalqtgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1246-1525 |
7.83e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 40.86 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1246 AKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQ 1325
Cdd:COG4942 32 SAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQER 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1326 EETRQ---KLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKsykELE 1402
Cdd:COG4942 112 EQRRRlaeQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQA---ELT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1403 FLQQRFDEKHQINDKLEKTRNRLQQELDdlmvdldhqrqivSNLEKKQKKFDQMLAEEKNIsaryGEERDRAEAEAREKE 1482
Cdd:COG4942 189 TLLSEQRAQQAKLAQLLEERKKTLAQLN-------------SELSADQKKLEELRANESRL----KNEIASAEAAAAKAR 251
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1785379715 1483 TKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGK 1525
Cdd:COG4942 252 EAAAAAEAAAARARAAEAKRTGETYKPTAPEKMLISSTGGFGA 294
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1111-1286 |
9.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1111 KQLRDLQSQLAELHEDLESEKAARAkaekqrrDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVR 1190
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQ-------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379715 1191 DAQVTEMRQRHNQvVEEISEQLEQARRfkgnlekvkqtlesentdlikEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNE 1270
Cdd:PRK09039 126 DSEKQVSARALAQ-VELLNQQIAALRR---------------------QLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
170
....*....|....*.
gi 1785379715 1271 SekvkfeLAEKLQKLQ 1286
Cdd:PRK09039 184 A------LAQRVQELN 193
|
|
|