|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-778 |
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: 1437.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTapsssntFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN-------IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd14920 154 VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETME 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd14920 234 AMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14920 314 QTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRD 578
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFR 658
Cdd:cd14920 474 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 659 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 739 TPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14920 634 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
855-1935 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1360.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 855 TRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDL 934
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 935 EARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDR 1014
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1015 IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLAR 1094
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1095 KEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 1174
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1175 LRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAK 1254
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1255 QDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEE 1334
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1335 TRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQR 1414
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1415 FDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALS 1494
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1495 LSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEV 1574
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1575 NMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQL 1654
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1655 KKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSAL 1734
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1735 LDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDST 1814
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1815 MRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLE 1894
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1785379713 1895 EAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRL 1935
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-778 |
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: 1312.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEhtapssSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKE------SGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGF-NQYRFLSNGNLPIPGQQDREIFQETM 337
Cdd:cd01377 155 STGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDpSYYFFLSQGELTIDGVDDAEEFKLTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 417
Cdd:cd01377 235 EAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 418 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd01377 315 GQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 498 MFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPK-FQKPRQL 576
Cdd:cd01377 394 MFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 577 RDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmgEMSFGSSYKTKKGM 656
Cdd:cd01377 472 KSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 657 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 736
Cdd:cd01377 541 FRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYS 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1785379713 737 ILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd01377 621 ILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-778 |
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: 1239.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSSntfYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALS---HGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd14932 158 VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRD 578
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGsSYKTKKGMFR 658
Cdd:cd14932 478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 659 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 739 TPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14932 637 TPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-778 |
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: 1194.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHtapsssntfyGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd14919 151 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd14919 231 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14919 311 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRD 578
Cdd:cd14919 391 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFR 658
Cdd:cd14919 471 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 659 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 739 TPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14919 631 TPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-778 |
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: 1183.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEhtapsssNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKD-------TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd14921 154 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd14921 234 AMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14921 314 QTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRD 578
Cdd:cd14921 394 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFR 658
Cdd:cd14921 474 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 659 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14921 554 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 739 TPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14921 634 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-778 |
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: 1174.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSSntfYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALS---HGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd15896 158 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRD 578
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSfgSSYKTKKGMFR 658
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP--GAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 659 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 739 TPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd15896 636 TPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-778 |
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: 1160.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPsssntfyGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQdREIFQETME 338
Cdd:cd14930 154 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQLRD 578
Cdd:cd14930 393 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSsyKTKKGMFR 658
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 659 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 739 TPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14930 631 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-778 |
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: 1159.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASShKGRKEHTAPS---SSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHpavNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 256 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQE 335
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 336 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 415
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 416 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 496 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKpRQ 575
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrIVGLDQvSGMGEMSFGSsyKTKKG 655
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGA--RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 656 MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379713 736 EILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-778 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1105.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEhtapsssntfyGELEHQLLQANPILEAFGNAKTVKNDNS 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV-----------GRLEEQILQSNPILEAFGNAKTVRNNNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 247 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIP 325
Cdd:pfam00063 150 SRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 326 GQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILM 405
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 406 PRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINY 485
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 486 TNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELG 565
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 566 NHPKFQKPRQlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMs 645
Cdd:pfam00063 467 KHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 646 fgsSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 725
Cdd:pfam00063 545 ---PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 726 IVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:pfam00063 622 ITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-790 |
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: 1010.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 80 NPPKFTKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 160 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkehtapsssntfyGELEHQLLQANPILEAFGNAK 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV-------------GSVEDQILESNPILEAFGNAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 240 TVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSN 319
Cdd:smart00242 148 TLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 320 GNLP-IPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNT-AAQKLCHLLGLNVT 397
Cdd:smart00242 228 GGCLtVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 398 EFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNS 477
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 478 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFV 557
Cdd:smart00242 387 FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 558 EKVIQELGNHPKFQKPRQlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldq 637
Cdd:smart00242 464 EKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS--------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 638 vsgmgemsfGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRI 717
Cdd:smart00242 534 ---------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRI 604
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 718 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 790
Cdd:smart00242 605 RRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
35-1252 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 926.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 35 QVWVPSEKHGFEAASIKEERGEEVIVELA---ENGKRVPVAKDDIQ--KMNPPKFTKVEDMAELTCLNEASVLHNLKDRY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 110 YSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGESGAGKTENTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 190 KVIQYLAHVASSHkgrkehtapsssNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIE 269
Cdd:COG5022 171 RIMQYLASVTSSS------------TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 270 TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IPGQQDREIFQETMESMKIMGFNHE 348
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 349 EIMSMLKMVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAV 428
Cdd:COG5022 319 EQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 429 EALAKALYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQR 508
Cdd:COG5022 398 DSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 509 EGIEWNFIDFgLDLQPCIDLIERpANPPGVLSLLDEECWFPKATDKSFVEKVIQEL--GNHPKFQKPRQLRDKadLCIIH 586
Cdd:COG5022 477 EGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQRLnkNSNPKFKKSRFRDNK--FVVKH 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 587 YAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVgldqvsgmgemsfgssyktKKGMFRTVGQLYKE 666
Cdd:COG5022 553 YAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKE 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 667 SLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA---- 742
Cdd:COG5022 614 SLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtg 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 743 IPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIVFFQAAARGYLARRAFYKKQQQMSA 822
Cdd:COG5022 694 EYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKK 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 823 LKVVQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKvvelqkvkdtqvkteselKEMANKYQQLFEEKSILAEQ 902
Cdd:COG5022 774 IQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSY------------------LACIIKLQKTIKREKKLRET 835
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 903 LQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEeeertlqLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVT 982
Cdd:COG5022 836 EEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS-------AQRVELAERQLQELKIDVKSISSLKLVNLELESEI 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 983 TESRLKKMEEDILLLEDQNAKLAKERKLLDDR-IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEME 1061
Cdd:COG5022 909 IELKKSLSSDLIENLEFKTELIARLKKLLNNIdLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGN 988
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1062 KMKRKLDGETTDLQDQLLELQQQIEELKQ--QLARKEEELQAALARV---DDEVGQKNNLLKQLRDLQSQLAELhedles 1136
Cdd:COG5022 989 KANSELKNFKKELAELSKQYGALQESTKQlkELPVEVAELQSASKIIsseSTELSILKPLQKLKGLLLLENNQL------ 1062
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1137 ekAARAKAEKQRRDLGEELEALKTELEDT--LDSTAAQQELRAKReqevTDLKKTIEEDVKVRDAQVTemrqrhNQVVEE 1214
Cdd:COG5022 1063 --QARYKALKLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTN----RNLVKPANVLQFIVAQMIK------LNLLQE 1130
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|
gi 1785379713 1215 ISEQLEQArrfKGNLEKVKQTLESENTDL--IKEVKNLQA 1252
Cdd:COG5022 1131 ISKFLSQL---VNTLEPVFQKLSVLQLELdgLFWEANLEA 1167
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-778 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 856.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApsssntfyGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA--------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL-----SNGNLPIPGQQDREI 332
Cdd:cd00124 153 DPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 333 FQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKV 410
Cdd:cd00124 233 FQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFeeDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 411 GRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEK 489
Cdd:cd00124 313 GGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 490 LQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPK 569
Cdd:cd00124 393 LQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 570 FQKPRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkdvdrivgldqvsgmgemsfgss 649
Cdd:cd00124 470 FFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------ 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 650 yktkkgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 729
Cdd:cd00124 519 --------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFD 584
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1785379713 730 EFRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd00124 585 EFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 774.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSSNTfYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKT-GGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKtDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQET 336
Cdd:cd14927 160 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 337 MESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPR- 574
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYdNHLGKSPNFQKPRp 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 575 --QLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQVsgmGEMSFGSSYKT 652
Cdd:cd14927 475 dkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---EDPKSGVKEKR 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 653 KKGM-FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14927 549 KKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADF 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1785379713 732 RQRYEILTPNAIPK-GFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14927 629 KQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-778 |
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: 764.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTApsssnTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDS-----KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYR--FLSNGNLPIPGQQDREIFQETM 337
Cdd:cd14913 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14913 236 SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14913 315 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQ 575
Cdd:cd14913 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDKAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvSGMGEMSFGSSYKTK 653
Cdd:cd14913 471 VKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA--------TADADSGKKKVAKKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14913 543 GSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 734 RYEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14913 623 RYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 753.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPsssntfyGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSK-------GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLL-EGFNQYRFLSNGNLPIPGQQDREIFQETM 337
Cdd:cd14909 154 PTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 417
Cdd:cd14909 234 QAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 418 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14909 314 GRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 498 MFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQL 576
Cdd:cd14909 393 MFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTnTHLGKSAPFQKPKPP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 577 R---DKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivGLDQVSGMGEMSFGSsyKTK 653
Cdd:cd14909 470 KpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAKGGR--GKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14909 543 GGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379713 734 RYEILTPNAIpKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14909 623 RYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-778 |
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: 724.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKgrkehtapsSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK---------QSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAG-EHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETM 337
Cdd:cd14934 152 TTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 417
Cdd:cd14934 232 VAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 418 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14934 312 GQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 498 MFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQL 576
Cdd:cd14934 391 MFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYdNHLGKSSNFLKPKGG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 577 RDK---ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgEMSFGSSYKTK 653
Cdd:cd14934 468 KGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSKKQK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KGM-FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd14934 534 RGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFK 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 733 QRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14934 614 QRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-778 |
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: 723.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASShkgrkehtapSSSNTfygELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS----------SSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP-IPGQQDREIFQETM 337
Cdd:cd01380 149 KNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 417
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 418 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPK--FQKPR 574
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 575 qLRDKADLcIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKytaelwkdvdrivgldqvsgmgemsfgssyktKK 654
Cdd:cd01380 465 -FSNTAFI-VKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KK 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 655 gmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 734
Cdd:cd01380 511 ----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSR 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1785379713 735 YEILTPNAIPKGfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd01380 587 YRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-778 |
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: 705.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEhtapsssntfYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK----------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd14929 151 ARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQLR 577
Cdd:cd14929 390 FVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFdNHFGKSVHFQKPKPDK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 578 DK--ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKdvdrivglDQVSGMGEMSFGSSYKTKKG 655
Cdd:cd14929 467 KKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFE--------NYISTDSAIQFGEKKRKKGA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 656 MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14929 539 SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRY 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1785379713 736 EILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14929 619 CILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-778 |
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: 704.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSsntfyGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK-----GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETM 337
Cdd:cd14917 157 TGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14917 315 KGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQ 575
Cdd:cd14917 394 HMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSNNFQKPRN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDK--ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQV--SGMGEMSFGSSyk 651
Cdd:cd14917 471 IKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPieKGKGKAKKGSS-- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 652 tkkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14917 546 -----FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1785379713 732 RQRYEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14917 621 RQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTapsSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEI---TSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETM 337
Cdd:cd14912 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPEL-IEMLLITTNpyDYPFVSQGEISVASIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14912 238 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14912 317 KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQ 575
Cdd:cd14912 396 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDKAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGldQVSGMGEMSFGssyKTK 653
Cdd:cd14912 473 VKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--ASAGGGAKKGG---KKK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14912 548 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 734 RYEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14912 628 RYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-778 |
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: 688.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 181 GAGKTENTKKVIQYLAHVASSHKGRKEHtapssSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE-----SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 261 GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd14918 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDL-IEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 417
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 418 AQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 498 MFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQL 576
Cdd:cd14918 395 MFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 577 RDKAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqVSGMGEMSFGSSYKTKK 654
Cdd:cd14918 472 KGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 655 GMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 734
Cdd:cd14918 544 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379713 735 YEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14918 624 YKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-778 |
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: 686.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKEhtapsSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKE-----NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQET 336
Cdd:cd14916 157 ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 337 MESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNTA-AQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 415
Cdd:cd14916 236 DSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 416 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14916 315 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 496 HTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPR 574
Cdd:cd14916 394 HHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 575 QLRDK--ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSykt 652
Cdd:cd14916 471 NVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS--- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 653 kkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd14916 548 ----FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379713 733 QRYEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14916 624 QRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-778 |
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: 683.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTapsSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEA---TSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFN--QYRFLSNGNLPIPGQQDREIFQETM 337
Cdd:cd14910 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDL-IEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14910 317 KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQ 575
Cdd:cd14910 396 HMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDK--ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqVSGMGEMSFGSSYKTK 653
Cdd:cd14910 473 AKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGKK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KG-MFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd14910 545 KGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379713 733 QRYEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14910 625 QRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-778 |
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 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEhtapSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKE----QQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYR--FLSNGNLPIPGQQDREIFQETM 337
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14923 237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14923 316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQ 575
Cdd:cd14923 395 HMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDKAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdriVGLDQVSGMGEMSFGssyKTK 653
Cdd:cd14923 472 AKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---KKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14923 546 GSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 734 RYEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14923 626 RYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-778 |
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: 676.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHtapSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEE---AASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMkTDLLLEGFNQYRF--LSNGNLPIPGQQDREIFQETM 337
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmPDNT-AAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14915 317 KGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 497 TMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVI-QELGNHPKFQKPRQ 575
Cdd:cd14915 396 HMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDKAD--LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIvgldQVSGMGEMSFGssyKTK 653
Cdd:cd14915 473 AKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTA----EAEGGGGKKGG---KKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14915 546 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 734 RYEILTPNAIPKG-FMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14915 626 RYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-778 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 652.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKgrkehtapsssntfygELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS----------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQET 336
Cdd:cd14883 146 SGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 337 MESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRK-ERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 415
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 416 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 496 HTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQ 575
Cdd:cd14883 385 HYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrIVGLDQVSGMGEMSfGSSYKTKKG 655
Cdd:cd14883 462 RRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGTSKG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 656 MfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14883 540 K-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRY 618
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379713 736 EILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14883 619 LCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-778 |
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: 645.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRgkKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGrkehtapsssntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETME 338
Cdd:cd01383 144 AGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPrqlRD 578
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSsyktkkgMFR 658
Cdd:cd01383 458 GA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS-------QKQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 659 TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd01383 529 SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 739 TPNAIpKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd01383 609 LPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-778 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 641.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEHTapsssntfygelEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERV------------KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETME 338
Cdd:cd01378 150 KGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFNHEEIMSMLKMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVG---RDYV 415
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 416 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFn 495
Cdd:cd01378 309 EVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 496 hTMFVL--EQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLSLLDEECWFP-KATDKSFVEKVIQELGNHPKFQK 572
Cdd:cd01378 388 -IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFEC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 573 PRQLRDKADLC--IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmgemsfgssy 650
Cdd:cd01378 464 PSGHFELRRGEfrIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 651 KTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:cd01378 525 LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEK 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1785379713 731 FRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd01378 605 FLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-778 |
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: 611.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHkgrkehtapsSSntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH----------SW------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQETM 337
Cdd:cd01381 145 KNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRK--ERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 415
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 416 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 493
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 494 FNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQK 572
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 573 PRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivgldqvsgmgEMSFGSSYKT 652
Cdd:cd01381 461 PKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE--------------DISMGSETRK 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 653 KKgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd01381 526 KS---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFV 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 733 QRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd01381 603 ERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-778 |
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: 611.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVAsshkGRKEHTAPSssntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS--------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDREIFQET 336
Cdd:cd01384 149 DDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 337 MESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKL---CHLLGLNVTEFSRAiLMPRIKVGRD 413
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIVTPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 414 -YVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 492
Cdd:cd01384 308 gIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 493 LFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQK 572
Cdd:cd01384 387 HFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 573 PRqlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRivgldqvsgmGEMSfgSSYKt 652
Cdd:cd01384 464 PK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR----------EGTS--SSSK- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 653 kkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd01384 529 ----FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 733 QRYEILTPNAiPKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 778
Cdd:cd01384 605 DRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-778 |
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: 572.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVASSHKGrkehtapsssntfygELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG---------------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLegfnqyrflsngnlpIPGQQDREIFQETM 337
Cdd:cd01382 146 NEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNT-------DQASMPDNTAAQKlchLLGLNVTEF-----SRAILM 405
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 406 PRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLCINY 485
Cdd:cd01382 288 TRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 486 TNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELG 565
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 566 NHPKFQKPRQ--------LRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGldq 637
Cdd:cd01382 443 NHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 638 vsgmgemsfGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRI 717
Cdd:cd01382 520 ---------DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379713 718 CRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd01382 591 MQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-778 |
1.15e-178 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 557.08 E-value: 1.15e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGrkehtapsssntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGfnQYRFLSNGN-LPIPGQQDREIFQETM 337
Cdd:cd14872 145 NRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCH---LLGLNVTEFSRAILMPRIKV-GRD 413
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkGCD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 414 YVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 493
Cdd:cd14872 303 PTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 494 FNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKP 573
Cdd:cd14872 383 FNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 574 RQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdvdrivgldqvsgmgEMSFGSSyKTK 653
Cdd:cd14872 460 EVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF----------------PPSEGDQ-KTS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 KGmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14872 523 KV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLK 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 734 RYEILtPNAIPKGFM-DGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14872 600 RYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-778 |
1.42e-177 |
|
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: 555.16 E-value: 1.42e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 174 ILCTGESGAGKTENTKKVIQYLAHVASSHK--GRKEHTAPSSSN-TFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAqgASGEGEAASEAIeQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 251 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDR 330
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 331 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASmpDNTAAQKLCH---LLGLNVTEFSRAILMPR 407
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 408 IKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 487
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 488 EKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLSLLDeECWFPKAT--DKSFVEKVIQEL 564
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 565 G-------------NHPKFQKPRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkytaelwkdvdr 631
Cdd:cd14890 476 GrksgsggtrrgssQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 632 ivgldqvSGMGEMSFGSSYKTkkgmfrtvgqlykeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGV 711
Cdd:cd14890 542 -------RSIREVSVGAQFRT--------------QLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379713 712 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-778 |
3.28e-172 |
|
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: 540.11 E-value: 3.28e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVasshkgrkehtAPSSSNTfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV-----------NQRRNNL----VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 vAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNG-NLPIPGQQDREIFQETM 337
Cdd:cd01387 146 -GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQ---ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDY 414
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 415 VQKAQTKEQADFAVEALAKALYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 494
Cdd:cd01387 305 IFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 495 NHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPR 574
Cdd:cd01387 384 NKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 575 QlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgLDQVSGMGEMSFGSSYKTKK 654
Cdd:cd01387 461 M--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFVTMK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 655 GMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 734
Cdd:cd01387 534 PRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDR 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379713 735 YEILTPNAIPKGfMDGKQACAIMIRALELDP-NLYRIGQSKIFFR 778
Cdd:cd01387 614 YRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-778 |
3.26e-167 |
|
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: 526.65 E-value: 3.26e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVAsshkgrkehtapsssntfyGELEH----QLLQANPILEAFGNAKTVKNDNSSRFGKFI 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-------------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 254 RINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgeHMKTDLLLEGFNQYRFL-SNGNLPIPGQQDREI 332
Cdd:cd14903 142 QLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGMSDRKH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 333 FQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASM--PDNTAAQKLCHLLGLNVTEFSRAILMPRIKV 410
Cdd:cd14903 220 FARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 411 GRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKL 490
Cdd:cd14903 300 AGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 491 QQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKVIqelGNHPKF 570
Cdd:cd14903 379 QQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 571 QK----PRQlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrIVGLDQVSGMGEMSF 646
Cdd:cd14903 452 QDviefPRT--SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 647 GSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 726
Cdd:cd14903 527 ARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRL 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 727 VFQEFRQRYEILTPNAiPKGFMDGKQACAIMIRALELD-PNLYRIGQSKIFFR 778
Cdd:cd14903 607 LHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-778 |
1.70e-166 |
|
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: 526.17 E-value: 1.70e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLahVASSHKGrkehtapsssntfYGE-LEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG-------------YGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQET 336
Cdd:cd01385 146 RENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 337 MESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKER-NTDQASMPDNTAAQKL-CHLLGLNVTEFSRAILMPRIKVGRDY 414
Cdd:cd01385 226 KQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 415 VQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKL 490
Cdd:cd01385 306 LILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 491 QQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKF 570
Cdd:cd01385 385 QYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 571 QKPrQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdriVGLDQV------------ 638
Cdd:cd01385 462 EKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlraff 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 639 --------SGM----------------GEMSFGSSYKTKKGMfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKA 694
Cdd:cd01385 533 ramaafreAGRrraqrtaghsltlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKP 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 695 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACAIMIRALELDPNLYRIGQSK 774
Cdd:cd01385 611 LRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTK 686
|
....
gi 1785379713 775 IFFR 778
Cdd:cd01385 687 VFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-776 |
1.58e-163 |
|
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: 516.65 E-value: 1.58e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMY------RGKKRHEIPPHIYAISETAYRSMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKehTAPSSSNtfygeLEHQLLQANPILEAFGNAKTVKNDNSSR 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQ--NATEREN-----VRDRVLESNPILEAFGNARTNRNNNSSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 249 FGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPI--PG 326
Cdd:cd14901 154 FGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrrDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 327 QQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-RKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILM 405
Cdd:cd14901 234 VDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 406 PRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQLCIN 484
Cdd:cd14901 314 REIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 485 YTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKV 560
Cdd:cd14901 394 FANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 561 IQELGNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsg 640
Cdd:cd14901 467 YDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 641 mgemsfgssyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQ 720
Cdd:cd14901 531 ------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 721 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRA------LELDPNLYrIGQSKIF 776
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-778 |
1.49e-162 |
|
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: 512.98 E-value: 1.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLahvasshkgrkehTAPSSSNTfyGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd01379 82 SGAGKTESANLLVQQL-------------TVLGKANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTD---LLLEGFNQYRFLSNGNLPIPGQQD--REIFQ 334
Cdd:cd01379 147 TGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSgnREKFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 335 ETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFR---KERNTDQASM-PDNTAAQKLCHLLGLNVTEFSRAILMPRIKV 410
Cdd:cd01379 227 EIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADELQEALTSHSVVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 411 GRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 488
Cdd:cd01379 307 RGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 489 KLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNH 567
Cdd:cd01379 387 QIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 568 PkFQKPRqlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfg 647
Cdd:cd01379 463 Y-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ----------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 648 ssyktkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 727
Cdd:cd01379 517 -----------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRIL 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1785379713 728 FQEFRQRYEILTPNAIPKGFMDgKQACAIMIRALELDPnlYRIGQSKIFFR 778
Cdd:cd01379 586 FADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-778 |
1.96e-162 |
|
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: 512.70 E-value: 1.96e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKK-RHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVASSHKGRkehtapsssntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD---------------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQD-------R 330
Cdd:cd14897 146 TENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 331 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKV 410
Cdd:cd14897 226 QMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 411 GRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 486
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 487 NEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGN 566
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 567 HPKFQKPrqLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdvdrivgldqvsgmgemsf 646
Cdd:cd14897 463 SPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF-------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 647 gSSYktkkgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 726
Cdd:cd14897 521 -TSY-------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRI 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 727 VFQEFRQRYEILTPNAiPKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 778
Cdd:cd14897 587 KYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-740 |
6.10e-162 |
|
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: 512.70 E-value: 6.10e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRgKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEhtapsssntfygELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 D---------VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLP----- 323
Cdd:cd14888 148 SklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidm 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 324 -------------------IPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTA 384
Cdd:cd14888 228 ssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 385 AQKL---CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASF 461
Cdd:cd14888 308 TDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 462 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSL 541
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 542 LDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKY 621
Cdd:cd14888 465 LDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 622 TAELWKD-VDRIVGLdqvsgmgemsfgssyKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPH 700
Cdd:cd14888 543 ISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRI 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1785379713 701 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 740
Cdd:cd14888 608 SVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-778 |
3.06e-160 |
|
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: 507.41 E-value: 3.06e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSsntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC-------VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLS-NGNLPIPGQQDREIFQET 336
Cdd:cd14873 154 CQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 337 MESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFrkeRNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQ 416
Cdd:cd14873 234 ITAMEVMQFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 417 KAQTKEQADFAVEALAKALYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14873 311 TPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 496 HTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRQ 575
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRDkaDLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvSGMGEMSFGSSYKTKKg 655
Cdd:cd14873 464 AVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 656 mfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14873 533 --PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRY 610
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1785379713 736 EILTPNAIPKGFMDGKqaCAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14873 611 KVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-778 |
1.43e-159 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 505.83 E-value: 1.43e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEI---PPHIYAISETAYRSMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 172 QSILCTGESGAGKTENTKKVIQYLAhVASSHkgRKEHTAPSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGK 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLA-TASKL--AKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 252 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDR 330
Cdd:cd14892 158 YIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 331 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFrkERNTDQ----ASMPDNTAAQKLCHLLGLNVTEFSRAILMP 406
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 407 RIKVGRDYV-QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFELN 476
Cdd:cd14892 316 TTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 477 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLSLLDEECWFP-KATDKS 555
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 556 FVEKVIQE-LGNHPKFQKPrqlRDKADLCII-HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkdvdriv 633
Cdd:cd14892 473 LLTIYHQThLDKHPHYAKP---RFECDEFVLrHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 634 gldqvsgmgemsfgssyktkkgmFRTvgqlykeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLE 713
Cdd:cd14892 536 -----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLE 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 714 GIRICRQGFPNRIVFQEFRQRYEIL---------TPNAIPkGFMDGKQACAIMIRALEldPNLYRIGQSKIFFR 778
Cdd:cd14892 586 VVRIRREGFPIRRQFEEFYEKFWPLarnkagvaaSPDACD-ATTARKKCEEIVARALE--RENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-738 |
5.76e-149 |
|
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: 475.57 E-value: 5.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY-----------RGKKRHEIPPHIYAISETAYRSM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHvASSHKGRKEHTAPSSSNTfygeLEHQLLQANPILEAFGNAKTVKN 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ-AGDNNLAASVSMGKSTSG----IAAKVLQTNILLESFGNARTLRN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 244 DNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhmktdlllegfnqyrflsngnlp 323
Cdd:cd14900 157 DNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE----------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 324 ipGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD-QASMPDNTAAQKL------CHLLGLNV 396
Cdd:cd14900 214 --AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 397 TEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEI 472
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 473 FELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKAT 552
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 553 DKSFVEKVIQELGNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSTdkytaelwkdVDri 632
Cdd:cd14900 449 DTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD-- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 633 vgldqvsgmgemsfgssyktkkgMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVL 712
Cdd:cd14900 509 -----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVM 564
|
650 660
....*....|....*....|....*.
gi 1785379713 713 EGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14900 565 EAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-741 |
9.87e-142 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 456.80 E-value: 9.87e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH--------EIPPHIYAISETAYRSMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAP--SSSNTFYGE--LEHQLLQANPILEAFGNAKTVKNDN 245
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLtsSIRATSKSTksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 246 SSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEG---FNQYRFLS-NG 320
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 321 NLPIPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASMPDNTAAQKLCHLLGLNVTE 398
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 399 FSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 471
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 472 IFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLSLLDEECWFP 549
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 550 KATDKSFVEKVIQELGNHPKFQKPRQLRdKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWkdv 629
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 630 driVGLDQVSGMGEMSFGSSYKTKKgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCN 709
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 1785379713 710 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 741
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-778 |
1.69e-141 |
|
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: 455.91 E-value: 1.69e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkehtapsssntfygELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS----------------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 257 FDvAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHMKTDLLLEGFnqYRFLSN--GNLPIPgQQDREI 332
Cdd:cd14889 147 FR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNgaGCKREV-QYWKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 333 FQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFrkERNTDQASMPDNTAAQKL---CHLLGLNVTEFSRAILMPRIK 409
Cdd:cd14889 223 YDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKTLTCTVTF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 410 VGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTN 487
Cdd:cd14889 301 TRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLAN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 488 EKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNH 567
Cdd:cd14889 381 EQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 568 PKFQKPRqlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWK-DVDRIVGLDQVSGM---GE 643
Cdd:cd14889 458 SYYGKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLpqaGS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 644 MSFGSSYKtkkgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 723
Cdd:cd14889 536 DNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFS 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379713 724 NRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACAIMIRALELDPnlYRIGQSKIFFR 778
Cdd:cd14889 610 WRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-778 |
2.62e-138 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 446.41 E-value: 2.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiytEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 172 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKEHTAPSSSNTFYG-ELEHQLLQANPILEAFGNAKTVKNDNSSR 248
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 249 FGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPI-PG 326
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSdDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 327 QQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRK----ERNTDQASMPDNTAAQKLCHLLGLNVTEFSRA 402
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 403 ILMPRIkVGRDYVQKAQ-TKEQADFAVEALAKALYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFEQ 480
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 481 LCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKV 560
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 561 IQELGNHPKFQKPRQlRDKADLCII-HYAGKVDYKADEWLMKNMDPLNDNVATLLHQStdkytaelwkdvdrivgldqvs 639
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREMFIVkHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS---------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 640 gmgemsfgssyktkkgmfrtvgQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICR 719
Cdd:cd14891 528 ----------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 720 QGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14891 586 VGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-778 |
8.02e-137 |
|
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: 442.84 E-value: 8.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVASshkGRKEHTAPsssntfygelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL--SNGNLPIPGQQDREIFQE 335
Cdd:cd14904 146 DGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 336 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYV 415
Cdd:cd14904 226 TQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 416 QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14904 305 TVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 496 HTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLSLLDEECWFPKATDKSFVEKV---IQELGNHPKFQK 572
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 573 PRQLRDKadLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDrivgldqvsGMGEMSFGSSYKT 652
Cdd:cd14904 461 PKVKRTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 653 KKGMfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd14904 530 TKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELA 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379713 733 QRYEILTPNAIPKGfmDGKQACAIMIRAL-ELDPNLYRIGQSKIFFR 778
Cdd:cd14904 609 TRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-778 |
3.74e-134 |
|
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: 436.26 E-value: 3.74e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR--GKKRHE-------IPPHIYAISETAYRSMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSSntfyGELEHQLLQANPILEAFGNAKTVKNDNSSR 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGK----LSIMDRVLQSNPILEAFGNARTLRNDNSSR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 249 FGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HMKTDLLLEGFNQYRFLSNG 320
Cdd:cd14908 157 FGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 321 NLPIPGQ-QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNtDQASMPDNTAAQK----LCHLLGLN 395
Cdd:cd14908 237 GAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 396 VTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIF 473
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 474 ELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFP-KAT 552
Cdd:cd14908 395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 553 DKSFVEKVI--------QELGNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqstdkyta 623
Cdd:cd14908 472 DANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP---------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 624 elwkdvdrivgldqvsgmgemsfgssyKTKKGMFRTvGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVL 703
Cdd:cd14908 536 ---------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 704 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPKGFM-------DGKQACA--------------IMIRALE 762
Cdd:cd14908 588 EQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVkkmckdlvkgvlspAMVSMKN 666
|
730
....*....|....*.
gi 1785379713 763 LDPNLYRIGQSKIFFR 778
Cdd:cd14908 667 IPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-778 |
1.12e-133 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 435.54 E-value: 1.12e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyteqivEMYRGKKRHE-------IPPHIYAISETAYRSMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 168 --DREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrKEHTAPSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDN 245
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESS------KHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 246 SSRFGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFN--QYRFLS 318
Cdd:cd14895 149 SSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 319 NGNLPI--PGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD---------------QASMPD 381
Cdd:cd14895 229 GGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 382 NTAAQKL---CHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTK--- 455
Cdd:cd14895 309 LTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfal 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 456 -------RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDlQPCIDL 528
Cdd:cd14895 389 npnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 529 IErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKPRqlRDKADLC--IIHYAGKVDYKADEWLMKNMDPL 606
Cdd:cd14895 468 LE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADVAfqIHHYAGAVRYQAEGFCEKNKDQP 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 607 NDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGmfrtVGQLYKESLSKLMSTLRNTNPNFVRCI 686
Cdd:cd14895 544 NAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYIRCI 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 687 IPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELdpn 766
Cdd:cd14895 620 KPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL--- 696
|
730
....*....|..
gi 1785379713 767 lyriGQSKIFFR 778
Cdd:cd14895 697 ----GKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-778 |
2.65e-133 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 432.28 E-value: 2.65e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHV---ASSHKGRkehtapsssntfygelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLyqdQTEDRLR------------------QPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 256 NFDvAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNL-PIPGQQDREIFQ 334
Cdd:cd14896 143 HLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 335 ETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQ--ASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGR 412
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 413 DYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 491
Cdd:cd14896 302 GRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 492 QLFNHTMFVLEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQ 571
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 572 KPRQlrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQvsgmgemsfGSSyk 651
Cdd:cd14896 459 KPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQ---------GKP-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 652 tkkgmfrTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14896 526 -------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379713 732 RQRYEILTpNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14896 599 LARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-831 |
3.07e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 438.31 E-value: 3.07e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEI-PPHIYAISETAYRSMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTApsssntfygelehqLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNA--------------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 256 NFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQE 335
Cdd:PTZ00014 254 QLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEE 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 336 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF--RKERNTDQASM--PDNTAA-QKLCHLLGLNVTEFSRAILMPRIKV 410
Cdd:PTZ00014 334 VMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYA 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 411 GRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKL 490
Cdd:PTZ00014 414 GNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEML 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 491 QQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKF 570
Cdd:PTZ00014 493 QKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKY 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 571 qKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqvsgmgEMSFGssy 650
Cdd:PTZ00014 570 -KPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV-------------EVEKG--- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 651 KTKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:PTZ00014 633 KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAE 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 731 FRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIVFFQAAARGY 807
Cdd:PTZ00014 711 FLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKI 790
|
730 740
....*....|....*....|....
gi 1785379713 808 LARRAFykkqqqMSALKVVQRNCA 831
Cdd:PTZ00014 791 KKKRKV------RKNIKSLVRIQA 808
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-740 |
3.98e-129 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 423.15 E-value: 3.98e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYR--------GKKRHEIPPHIYAISETAYRSMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSsntfygELEHQLLQANPILEAFGNAKTVKNDNSSR 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV------EIGKRILQTNPILESFGNAQTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 249 FGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFL-----SNGNLP 323
Cdd:cd14902 155 FGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygpSFARKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 324 IPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKE-RNTDQASMPDNTAAQ--KLCHLLGLNVTEFS 400
Cdd:cd14902 235 AVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 401 RAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEI 472
Cdd:cd14902 315 TLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFES 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 473 FELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLSLLDEECWFPKAT 552
Cdd:cd14902 395 LNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 553 DKSFVEKVIQELGNHPKFqkprqlrdkadlCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDkytaelwkDVDRI 632
Cdd:cd14902 472 NQALSTKFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 633 VGLDQVSGMGEMSFGSSYKTKKGMFRT--VGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNG 710
Cdd:cd14902 532 IGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611
|
650 660 670
....*....|....*....|....*....|
gi 1785379713 711 VLEGIRICRQGFPNRIVFQEFRQRYEILTP 740
Cdd:cd14902 612 VLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-776 |
2.50e-125 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 410.15 E-value: 2.50e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRH-EIPPHIYAISETAYRSMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLAHVASSHKGRKEHTApsssntfygelehqLLQANPILEAFGNAKTVKNDNSSRFGKFIRInf 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQTA--------------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DVA--GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQE 335
Cdd:cd14876 145 DVAseGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 336 TMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKErntDQASMPDntAA----------QKLCHLLGLNVTEFSRAILM 405
Cdd:cd14876 225 VLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 406 PRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCIN 484
Cdd:cd14876 300 KVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 485 YTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQEL 564
Cdd:cd14876 378 ITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 565 GNHPKFqKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVdrivgldqvsgmgEM 644
Cdd:cd14876 455 KSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV-------------VV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 645 SFGssyKTKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 724
Cdd:cd14876 521 EKG---KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSY 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 725 RIVFQEFRQRYEILTPNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIF 776
Cdd:cd14876 596 RRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-778 |
2.06e-123 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 405.93 E-value: 2.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVasshkgrkehtAPSSSNTFYGElehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTA-----------AGSVGGVLSVE---KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNqyrflSNGNLPIPGQQDREIFQETM- 337
Cdd:cd01386 147 QAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLA-----ESNSFGIVPLQKPEDKQKAAa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ------ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMP----- 406
Cdd:cd01386 222 afsklqAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHhlsgg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 407 -------RIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN--- 476
Cdd:cd01386 302 pqqsttsSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsq 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 477 ---SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLSL 541
Cdd:cd01386 381 rgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 542 LDEECWFPKATDKSFVEKVIQELG--NHPKFQKPRQLRDKADLCII-HYAGK--VDYKADEWLMK-NMDPLNDNVATLLH 615
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPLQFVLgHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 616 QSTDKYTAelwkdvdrivgldqvsgmgemsfgssyKTKKGMFRTVgqlyKESLSKLMSTLRNTNPNFVRCIIPNHE---- 691
Cdd:cd01386 541 ESQKETAA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkd 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 692 --KKAGKLEPHLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACAIMI 758
Cdd:cd01386 590 erSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELL 669
|
730 740
....*....|....*....|
gi 1785379713 759 RALELDPNLYRIGQSKIFFR 778
Cdd:cd01386 670 EELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-740 |
5.37e-117 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 386.51 E-value: 5.37e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEIPPHIYAISETAYRSMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 175 LCTGESGAGKTENTKKVIQYLAHVASShkgrkehTAPSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS-------PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 255 INFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSN--GNLpipgqqDREI 332
Cdd:cd14880 154 LQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNpeRNL------EEDC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 333 FQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTA---AQKLCHLLGLNVTEFSRAILMPRIK 409
Cdd:cd14880 228 FEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 410 VGRDYV--QKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTN 487
Cdd:cd14880 308 AGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 488 EKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQE-LGN 566
Cdd:cd14880 388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESaLAG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 567 HPKFQKPRqLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGmgemsf 646
Cdd:cd14880 465 NPCLGHNK-LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG------ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 647 gssykTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 726
Cdd:cd14880 538 -----QSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRV 612
|
650
....*....|....
gi 1785379713 727 VFQEFRQRYEILTP 740
Cdd:cd14880 613 SHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-741 |
1.02e-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: 387.80 E-value: 1.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKR-HEIPPHIYAISETAYRSMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 177 TGESGAGKTENTKKVIQYLAHVASSHKGRKehtapSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQN-----NNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 257 FDVAGYIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEG-FNQYRFL--------------SN 319
Cdd:cd14906 156 FRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 320 GNLPIPGQQDR-EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQAS--MPDNTAA-QKLCHLLGLN 395
Cdd:cd14906 236 KNSNHNNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 396 VTEFSRAILMPRIKV-GRDYVQ-KAQTKEQADFAVEALAKALYERLFRWLVHRINKALDR----------TKRQGASFIG 463
Cdd:cd14906 316 ESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 464 ILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLSLLD 543
Cdd:cd14906 396 VLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 544 EECWFPKATDKSFVEKVIQELGNHPKFQKpRQLrDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTA 623
Cdd:cd14906 473 DECIMPKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 624 ELwkdvdrivgldqvSGMGEMSFGSSYKTKKGMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVL 703
Cdd:cd14906 551 SL-------------FQQQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616
|
650 660 670
....*....|....*....|....*....|....*...
gi 1785379713 704 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 741
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-778 |
2.26e-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: 373.07 E-value: 2.26e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRH-----EIPPHIYAISETAYRSMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 173 SILCTGESGAGKTENTKKVIQYLAHvasshkgrkehtAPSSSNTfygELEHQLLQANPILEAFGNAKTVKNDNSSRFGKF 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY------------GHSTSST---DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 253 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGN-LPIPGQQDRE 331
Cdd:cd14886 146 IKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKcYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 332 IFQETMESMKIMgFNHEEIMSMLKMVSAVLQFGNIVFRKERN--TDQASMPDNTAA-QKLCHLLGLNVTEFSRAILMPRI 408
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 409 KVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLCINY 485
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 486 TNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLSLLDEECWFPKATDKSFVEKVIQELG 565
Cdd:cd14886 381 ANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCKSKIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 566 NHpkfqkpRQLRDKADLC---IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLdqvsgmg 642
Cdd:cd14886 458 NN------SFIPGKGSQCnftIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 643 emsfgssyktKKGMFrtVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGF 722
Cdd:cd14886 525 ----------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGF 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379713 723 PNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14886 593 AYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-778 |
4.42e-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: 366.83 E-value: 4.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRG-KKRHEIPPHIYAISETAYRSM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRkehtapSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSN------TSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 256 NFD-VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDL-LLEGFNQYRFLSNGNL----PIPGQ-- 327
Cdd:cd14875 155 YFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 328 QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNtDQASMPDNTAAQKLCHLLGLNVTEFSRAILmpr 407
Cdd:cd14875 235 DDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 408 IKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 486
Cdd:cd14875 311 VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 487 NEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLSLLDEECWFPKATDKSFVEKVIQELGN 566
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWAN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 567 H------PKFQKPRQLRdkadlcIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdrivgldqvsg 640
Cdd:cd14875 468 KspyfvlPKSTIPNQFG------VNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL--------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 641 mgemsfgssYKTKKGMFR---TVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRI 717
Cdd:cd14875 527 ---------LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIAL 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379713 718 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK---QACAIMIRALEL----DPNlYRIGQSKIFFR 778
Cdd:cd14875 598 KRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKyseAAKDFLAYYQRLygwaKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-735 |
4.32e-106 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 357.10 E-value: 4.32e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMY----------RGKKRHEIPPHIYAISETAYRSMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 168 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSSSNTFYGE--LEHQLLQANPILEAFGNAKTVKNDN 245
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASPSRttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 246 SSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG----AGEHMKTDLLLEGFNQYRFLSNG 320
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 321 NLPIP---GQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-----RKERNT--DQASMPDNTAA----- 385
Cdd:cd14899 241 SLCSKrrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 386 QKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRT----------- 454
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 455 ---KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLIER 531
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 532 paNPPGVLSLLDEECWFPKATDKSFVEKVIQEL---GNHPKFQKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLND 608
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 609 NVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIP 688
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379713 689 NHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14899 638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-778 |
2.73e-101 |
|
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: 343.55 E-value: 2.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkehtapSSSNTfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHG-------ADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 251 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLlegfnqyrflsngnlpiPGQQDR 330
Cdd:cd14887 150 KMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 331 EIFQ-----ETMESMKIMGFNHEEImsmLKMVSAVLQFGNIVFRKERNTDQASMPDNTA--------AQKLCHLL----- 392
Cdd:cd14887 213 ESTDlrritAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkcl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 393 --GLNVTEFSRAIL--------MPRIKVGRDYV------------QKAQTKEQADFAVEALAKALYERLFRWLVHRINKA 450
Cdd:cd14887 290 ssGLKVTEASRKHLktvarllgLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 451 LDRTKR-------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWN 514
Cdd:cd14887 370 LQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 515 FI--DFGLDLQPCIDLIERPAN---------------------PPGVLSLLDE------ECWFPKATDKSFVEKVIQELG 565
Cdd:cd14887 450 QDcsAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNII 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 566 NHPKFQK--PRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSTDKYTaelwkdvdRIVGLDQVSGMge 643
Cdd:cd14887 530 NSAKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV-- 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 644 msfgSSYKTKKgmfRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 723
Cdd:cd14887 599 ----RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1785379713 724 NRIVFQEFRQRYEILTPNAIpKGFMDGKQACAIMIRALELDPNLYRIGQSKIFFR 778
Cdd:cd14887 672 CRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-742 |
1.15e-99 |
|
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: 333.79 E-value: 1.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYTEQIVEMYRGKKRHeIPPHIYAISETAYRSMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAhvasshkgrkEHTAPSSSntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDv 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV----------ERTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 aGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDlllegFNQYRF-LSNGNLPIPGQQDREIFQETME 338
Cdd:cd14898 141 -GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFnhEEIMSMLKmvsAVLQFGNIVFRKERNTDQASmpdNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQKA 418
Cdd:cd14898 215 SLGIANF--KSIEDCLL---GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 419 QTKEQADFAVEALAKALYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14898 287 NTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 499 FVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLSLLDEECWFPKATDKSFVEKvIQELGNHpkfqkprQLRD 578
Cdd:cd14898 364 FRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVK-IKKYLNG-------FINT 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 579 KADLCII--HYAGKVDYKADEWLMKNMDplndnvatllhqstdkytaelwkdvdrivgldqvsGMGEMSFGSSYKTKKGM 656
Cdd:cd14898 432 KARDKIKvsHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDEGS 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 657 FRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 736
Cdd:cd14898 477 KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYR 556
|
....*.
gi 1785379713 737 ILTPNA 742
Cdd:cd14898 557 ILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-777 |
8.90e-94 |
|
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: 319.11 E-value: 8.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYTEQIVEMYR-------GKKRHEIPPHIYAISETAYRSM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKehtapsssntfygeLEHQLLQANPILEAFGNAKTVKND 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK--------------LSSQISAAEFVLDSFGNAKTLTNP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 245 NSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNL-- 322
Cdd:cd14879 145 NASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGChp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 323 --PIPGQQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFR--KERNTDQASMpDNTAA-QKLCHLLGLNVT 397
Cdd:cd14879 225 lpLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVV-KNTDVlDIVAAFLGVSPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 398 EFsRAILMPRIK-VGRD----YVQKAQTKEQADfaveALAKALYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEI 472
Cdd:cd14879 304 DL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 473 F---ELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLSLLDEEC-WF 548
Cdd:cd14879 379 RsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRM 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 549 PKATDKSFVEKVIQELGNHPKF---QKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhqstdkytael 625
Cdd:cd14879 456 PKKTDEQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL----------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 626 wkdvdrivgldqvsgmgemsfgssyktkkgmfRTVGQLyKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQ 705
Cdd:cd14879 525 --------------------------------RGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQ 571
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 706 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACAIMIRALELDPNLYRIGQSKIFF 777
Cdd:cd14879 572 IRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-778 |
8.32e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 316.37 E-value: 8.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR---GKKRHEIPPHIYAISETAYRSMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 176 CTGESGAGKTENTKKVIQYLAHVASShkgrkehtapsSSNTFYGELEHqllqANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-----------SRTTFDSRFKH----VNCILEAFGHAKTTLNDLSSCFIKYFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 256 NF-DVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGnlpIPGQ------- 327
Cdd:cd14878 146 QFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT---MREDvstaers 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 328 QDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPR 407
Cdd:cd14878 223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 408 IKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCIN 484
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 485 YTNEKLQQLFNHTMFVLEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLSLLDEECWFPKATD 553
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 554 KSFVEKV--IQELGNHPKFQKPRQ-------LRDK-ADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTA 623
Cdd:cd14878 450 PNLPKKLqsLLESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 624 ELwkdvdrivgldqvsgmgemsFGSSYKTkkgmfrTVGQLYKeSLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVL 703
Cdd:cd14878 530 HL--------------------FQSKLVT------IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVS 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 704 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACAIMIRALELDPnlYRIGQSKIFFR 778
Cdd:cd14878 583 AQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-778 |
2.50e-90 |
|
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: 308.87 E-value: 2.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQivemYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAhvasshKGRKEHTapsssntfygELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN----------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQETME 338
Cdd:cd14937 141 EYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 339 SMKIMGFnHEEIMSMLKMVSAVLQFGNIVFR---KERNTDQASMPDNT--AAQKLCHLLGLNVTEFSRAILMPRIKVGRD 413
Cdd:cd14937 221 SFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 414 YVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 493
Cdd:cd14937 300 KIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 494 FNHTMFVLEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQKP 573
Cdd:cd14937 379 YLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYAST 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 574 RQLRDKaDLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRIVGLDQVSGMgemsfgsSYKtk 653
Cdd:cd14937 455 KKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLI-------TFK-- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 654 kgmfrtvgqlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQ 733
Cdd:cd14937 525 ----------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLS 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1785379713 734 RYEILTPNAIPKGFMDGKQACAIMIRAlELDPNLYRIGQSKIFFR 778
Cdd:cd14937 594 YFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-730 |
6.32e-77 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 271.01 E-value: 6.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYRGKKRHE-------IPPHIYAISETAYRSMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKEHTapsssntfygELEHQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT----------ERIDKLIYINNILESMSNATTIKNNNSSRCG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 251 KFIRINFD---------VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHMKTDLLLEGFNQYRFLSN- 319
Cdd:cd14884 147 RINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 320 ---------GNLPIPG----------QQDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKerntdqasmp 380
Cdd:cd14884 227 eshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA---------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 381 dntaaqkLCHLLGLNVTEFSRAILMPRIKVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGA- 459
Cdd:cd14884 297 -------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEs 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 460 ----------SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGlDLQPCIDLI 529
Cdd:cd14884 370 dnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 530 ERpanppgVLSLLDE-----ECWFPKATDKSFV-----EKVIQELGNH------PKFQK---PRQLRDKADLCIIHYAGK 590
Cdd:cd14884 449 AK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 591 VDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAElwkdvdrivgldqvsgmgemsfgSSYKTKKGMFRTVGQLYKESLSK 670
Cdd:cd14884 523 VTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDN 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 671 LMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:cd14884 580 LFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-765 |
6.32e-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: 266.21 E-value: 6.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyteqiveMYRGKKRHEIPPHIYA-------ISETAYRSMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 173 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkehtAPSSSNTFygelEHqLLQANPILEAFGNAKTVKNDNSSRFGKF 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG---------GGPETDAF----KH-LAAAFTVLRSLGSAKTATNSESSRIGHF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 253 IRINFdVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFN--QYRFLSNGNLPIPGQQDR 330
Cdd:cd14881 136 IEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 331 EIFQETMESMKIMGFNHEEIMSMLkmvSAVLQFGNIVFrKERNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKV 410
Cdd:cd14881 215 ARFQAWKACLGILGIPFLDVVRVL---AAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 411 GRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFELNSFEQLC 482
Cdd:cd14881 291 RGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 483 INYTNEKLQQLFNHTMFVLEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLSLLDEECwFPKATDKSFVEKVI 561
Cdd:cd14881 367 INLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 562 QELGNHPKFQKPRQLRDKAdLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTdkytaelwkdvdrivgldqvsgm 641
Cdd:cd14881 443 VQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN----------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 642 geMSFGssyktkkgmFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQG 721
Cdd:cd14881 499 --CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGG 567
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1785379713 722 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACA--IMIRALELDP 765
Cdd:cd14881 568 YPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCalILQFLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-731 |
3.58e-72 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 256.56 E-value: 3.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYTEQIVEMYrgKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAhvaSSHKGRKEHtapsssntfygeLEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSKY------------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 259 VAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSN-GNLPIPGQQDREIFQETM 337
Cdd:cd14905 145 LYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 338 ESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNtdQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRIKVGRDYVQK 417
Cdd:cd14905 225 MSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVEN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 418 AqtkeqadfavEALAKALYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14905 303 R----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 498 MFVLEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLSLLDEECWFPKATDKSFVEKVIQELGNHPKF-QKPRQ 575
Cdd:cd14905 371 VLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 576 LRdkadlcIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKY-------------TAELWKDVD----------RI 632
Cdd:cd14905 444 FG------IEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakksplSI 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 633 V------------------------GLDQVSGMGEMSFGSSYKTKKGMFRTVGQlykeslsklmstlRNTNPNFVRCIIP 688
Cdd:cd14905 518 VkvllscgsnnpnnvnnpnnnsgggGGGGNSGGGSGSGGSTYTTYSSTNKAINN-------------SNCDFHFIRCIKP 584
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1785379713 689 NHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFP----NRIVFQEF 731
Cdd:cd14905 585 NSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-743 |
1.00e-69 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 247.86 E-value: 1.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYrgkkrheippHIYAISETAYRSMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 178 GESGAGKTENTKKVIQYLahvaSSHKGRKEHTAPSSSNTFygelehqllqanpILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYL----TSQPKSKVTTKHSSAIES-------------VFKSFGCAKTLKNDEATRFGCSIDLLY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 258 DvAGYIVGANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDREIFQET 336
Cdd:cd14874 134 K-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 337 MESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKERNTD---QASMPDNTAAQK-LCHLLGLNVTEFSrAILMPRIKVGr 412
Cdd:cd14874 213 EDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDG- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 413 dyvqKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 492
Cdd:cd14874 291 ----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIEN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 493 LFNHTMFVLEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLSLLDEECWFPKATDKSFVEKVIQELGNHPKFQ 571
Cdd:cd14874 365 LFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 572 KPRQlRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELwkdvdrivgldqvsgmgemsFGSSYK 651
Cdd:cd14874 443 KARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESYSS 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 652 TKKGMFRTVGQLYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14874 502 NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
650
....*....|..
gi 1785379713 732 RQRYEILTPNAI 743
Cdd:cd14874 582 ARQYRCLLPGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-736 |
1.60e-65 |
|
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: 238.33 E-value: 1.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYT----------EQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTpdhmqaynksREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkeHTAPSSSNTFYgELEHQLLQANPILEAFGNAKTVKNDNSSRFGK 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPR--PDSEGASGVLH-PIGQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 252 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---MKTDLLL-EGFNQYRFLSN-----GNL 322
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 323 PIpgqqDREIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVF-------------RKERNTDQASMPDNTAAQKL- 388
Cdd:cd14893 240 AL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQSCALKDPAQILl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 389 -CHLLGLNVTEFSRaILMPRIKVGRDYVQ-----KAQTKEQADFAVEALAKALYERLFRWLVHRINKAL----DRTKRQG 458
Cdd:cd14893 316 aAKLLEVEPVVLDN-YFRTRQFFSKDGNKtvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 459 ----ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IEWNFIDFGLDLQPC 525
Cdd:cd14893 395 ivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 526 IDLIERPanPPGVLSLLDEECWFPKATDKSFVEKVIQ-----------ELGNHPKFQKPRQLRDKADLCII-HYAGKVDY 593
Cdd:cd14893 475 LQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpNMGADTTNEYLAPSKDWRLLFIVqHHCGKVTY 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 594 KADEWLMKNMDPLNDNVATLLHQSTDKytaelwkdVDRIVGLDQVSGMGEMSFGSSY---KTKKGMFRTVGQLYKESLS- 669
Cdd:cd14893 553 NGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAAASSEKAAKQTeerGSTSSKFRKSASSARESKNi 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 670 -------------KLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 736
Cdd:cd14893 625 tdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-778 |
3.08e-64 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 232.32 E-value: 3.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 180 SGAGKTENTKKVIQYLAHVASSHKGRKEhtapsssntfygelehQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATG----------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 260 AGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHMKTDLLLEGFNqYRFL--SNGNLPIPGQQDR----- 330
Cdd:cd14882 146 TGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKLKYRRddpeg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 331 --EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNIVFRKerNTDQASMPDNTAAQKLCHLLGLNVTEFSRAILMPRI 408
Cdd:cd14882 225 nvERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 409 KVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNSFEQLCI 483
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 484 NYTNEKLQQLFNHTMFV---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLSLLDEECwfPKATDKSFVEKV 560
Cdd:cd14882 380 NTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYIMDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 561 IQElgNHPKFQKPRQlrdKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDvdrivglDQVSG 640
Cdd:cd14882 452 IKE--KHSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 641 MgemsfgssyKTKKGMFRTVgqlykeSLSKLMSTLRNTNP---NFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVLEGIRI 717
Cdd:cd14882 520 M---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKA 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379713 718 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACAIMIRALELDPnlYRIGQSKIFFR 778
Cdd:cd14882 585 RQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-262 |
3.28e-61 |
|
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: 207.20 E-value: 3.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 121 FCVVINPYKNLPIYTEQIV-EMYRGKKRHEIPPHIYAISETAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 200 SSHKGRKEHTAPSSSNTFYGELEHQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 262
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 ... |
100-776 |
1.08e-56 |
|
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: 211.23 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYTEQIVEMYR-GKKRHEIPPHIYAISETAYRSMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 179 ESGAGKTENTKKVIQYLAHVASSHKGRKEHTAPSS-------SNTFY-GELEHQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEednihneENTDYqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 251 KFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHMKTDLLLEGFNQYRFLSNGNLPIPGQQDR 330
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 331 EIFQETMESMKIMGFNHEEIMSMLKMVSAVLQFGNI----VFRKE----------------------RNTDQASMPDNTA 384
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 385 AQKL-CHLLGLNVTEFSRAILMPRIkVGRDYVQKAQTKEQADFAVEALAKALYERLFRWLVHRINKALDRTKR--QGASF 461
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 462 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLSL 541
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 542 LDEECWFPKATDKS-FVEKVIQELGNHPKF-QKPRQLRDKADLCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTD 619
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 620 KYTAELWKDVDRIVGLDQVSGMGEMSFGSSYKTKKGMFRTVGQ----LYKESLSKLMSTLRNTNPNFVRCIIPNHEKKA- 694
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 695 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACAIMIRALELDPNLYRIGQSK 774
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1785379713 775 IF 776
Cdd:cd14938 710 IF 711
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-719 |
2.19e-28 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 124.47 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 105 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYTEQIVEMYRGKKRHE--IPPHIYAISE---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 160 ----TAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVASS--HKGRKEHTAPSSSNT----------------- 216
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPalSKGSEETCKVSGSTRqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 217 ------------------------------------------------------FYGELEHQ------------------ 224
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgFYEKLEHLedeeqlrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 225 ---LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDERTFHV 290
Cdd:cd14894 246 lsiVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 291 FYQLLAGAGEH-----MKTDLLLEGFN--QYRFLSNGNLPIPG--------QQDREIFQETMESMKIMGFNHEEIMSMLK 355
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 356 MVSAVLQFGNIVFRKERNTDQASMPDN---TAAQKLCHLLGLNVTEFSRAILMPR---IKVGRDYVQKAQTKEQADFAVE 429
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 430 ALAKALYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQql 493
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 494 fnhtmfvleQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLSLLDEECWFPKAT----------DKSFVEKVIQE 563
Cdd:cd14894 564 ---------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 564 lgNHPKFQKPRQLRDKAD-----------LCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSTDKYTAELWKDVDRi 632
Cdd:cd14894 635 --NSSRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 633 vgLDQVSGMGEMSFGSSYKTKKGMFRTVGQlYKESLSKLMSTLRNTNPNFVRCIIPNHEKKAGKLEPHLVLDQLRCNGVL 712
Cdd:cd14894 712 --LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLI 788
|
....*..
gi 1785379713 713 EGIRICR 719
Cdd:cd14894 789 RQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
868-1720 |
1.90e-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: 119.01 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 868 LQKVKD------TQVKTESELKEMANKYQQLFEEKSILaeQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE 941
Cdd:TIGR02168 188 LDRLEDilneleRQLKSLERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 942 EERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLddrigeftst 1021
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL---------- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1022 maeeEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQA 1101
Cdd:TIGR02168 336 ----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1102 ALARVDDEVGQKNNLLKQLRDlqSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtldstAAQQELRAKREQ 1181
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1182 evtdlkktiEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESEN--------------TDLIkeV 1247
Cdd:TIGR02168 484 ---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalggrlQAVV--V 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1248 KNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQklqaELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDT 1327
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK----NIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1328 QELLQE-ETRQKLNFSSRVRQLEEEKNNLMENLeeeesakaqlsrqlqalqqqlleSKKRMEDQGGMVEAMEEAKKKSyK 1406
Cdd:TIGR02168 629 DDLDNAlELAKKLRPGYRIVTLDGDLVRPGGVI-----------------------TGGSAKTNSSILERRREIEELE-E 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1407 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR 1486
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1487 EKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIE 1566
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1567 DGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLfkqvremeveleeerKQKSQILAAKKKLEMDLQDMESQMDSANKG 1646
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALL---------------NERASLEEALALLRSELEELSEELRELESK 909
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379713 1647 RDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEK-KLKSLEAELLQLQEDLAAAERAKRQAQQERDDL 1720
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1089-1941 |
1.82e-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: 108.99 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 KQQLARKEEELQAALARVDDEVgqkNNLLKQLRDLQSQ------LAELHEDLESEKAARAKAEKQrrDLGEELEALKTEL 1162
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDIL---NELERQLKSLERQaekaerYKELKAELRELELALLVLRLE--ELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1163 EDTLDSTAAQQELRAKREQEVTDLKKTIEEDvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTD 1242
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1243 LIKEVKNLQAAKQDSEQRRKKLEQ---QVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLST 1319
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1320 VQSQLQDTQELLQeetrqklNFSSRVRQLEEEKNNLMENLEEEESAkaqlsrqlqalqqqllESKKRMEDQGGMVEAMEE 1399
Cdd:TIGR02168 405 LEARLERLEDRRE-------RLQQEIEELLKKLEEAELKELQAELE----------------ELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1400 AkkksykeLEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEEKNISARYGEERD 1479
Cdd:TIGR02168 462 A-------LEELREELEEAEQALDAAERELAQLQARLDSL-------ERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1480 RAEAEAReketkalsLSRALEEAidlkdeldrqnkqLRAEMDDLV-SSKDDVGKNVHELERS---KRALEQQVQEMKTQI 1555
Cdd:TIGR02168 528 LISVDEG--------YEAAIEAA-------------LGGRLQAVVvENLNAAKKAIAFLKQNelgRVTFLPLDSIKGTEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1556 EELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNR----------DDSNDEKKKLLFKQV---------REMEVELEEER 1616
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRPGYRivtldgdlvRPGGVITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1617 KQKSQILAAK---KKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLE 1693
Cdd:TIGR02168 667 KTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1694 AELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQV 1773
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1774 ETITTELSAERsfsQKAENARQQMERQNKELkvklnemdstmrSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRR 1853
Cdd:TIGR02168 827 ESLERRIAATE---RRLEDLEEQIEELSEDI------------ESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1854 AEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSN-RRRLQRELEDVTESAESMNREVTTLR 1932
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEAR 971
|
....*....
gi 1785379713 1933 SRLSKLERQ 1941
Cdd:TIGR02168 972 RRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
977-1745 |
3.26e-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: 108.23 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 977 QLEKVTTEsRLKKMEEDILLLEDQNAK---LAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLkke 1053
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL--- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1054 ekgRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVddevgqkNNLLKQLRDLQSQLAELHED 1133
Cdd:TIGR02169 275 ---EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-------AKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1134 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVvE 1213
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-A 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1214 EISEQLEQARrfkgnlEKVKQtLESENTDLIKEVK----NLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKL 1289
Cdd:TIGR02169 424 DLNAAIAGIE------AKINE-LEEEKEDKALEIKkqewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1290 QKLQAELDGVSGALGSTE--GKSIK----LTKDLSTVQSQLQDTQE-----------------------LLQEETRQKLN 1340
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEvlKASIQgvhgTVAQLGSVGERYATAIEvaagnrlnnvvveddavakeaieLLKRRKAGRAT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1341 FS--SRVRQLEEEKNNLMENLEEEES----------AKAQLSRQLQALQQQLLESKKRMEDQGGMVE----------AME 1398
Cdd:TIGR02169 577 FLplNKMRDERRDLSILSEDGVIGFAvdlvefdpkyEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTlegelfeksgAMT 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1399 EAKKKSYKELEFLQQRFDEKHQINDKLEKtrnrLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEER 1478
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1479 DRAEAEAREKETKALSLSRALEEAIDLKDELD-------RQNKQLRAEMDDLVSSKDDVGknVHELERSKRALEQQVQEM 1551
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEarieeleEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1552 KTQIEELEDELQAIEDGKLRLEVNMQAMKAQfERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEM 1631
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1632 DLQDMESQMDSANKGRDEA---VKQLKKLQLQFKEVWREVEETRAARDEIF---VQSRDNEKKLKSLEAELLQLQEDLAA 1705
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPKgedEEIPEEELSLEDVQAELQRVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1785379713 1706 AERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRI 1745
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
975-1726 |
3.29e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.22 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 975 KLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDdrigeftstmaEEEEKVKSLNKLRNKYEAV-IADLEDRLKKE 1053
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLE-----------RQAEKAERYKELKAELRELeLALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1054 EKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHED 1133
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1134 LESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQvVE 1213
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1214 EISEQLEQarrfkgnlekvkqtLESENTDLIKEVKNLQAakQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQ 1293
Cdd:TIGR02168 397 SLNNEIER--------------LEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1294 AELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEetrqKLNFSSRVRQLEEEKNNLMENLEEEES--------A 1365
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSElisvdegyE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1366 KAQLSRQLQALQQQLLESKkrmEDQGGMVEAMEEAK---------------KKSYKELEFLQQRFDEKHQINDkLEKTRN 1430
Cdd:TIGR02168 537 AAIEAALGGRLQAVVVENL---NAAKKAIAFLKQNElgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKD-LVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1431 RLQQELDDL-----MVD-----------LDHQRQIVS----------NLEKKQKKFDQMLAEEKNISARYGEERDRAEAE 1484
Cdd:TIGR02168 613 KLRKALSYLlggvlVVDdldnalelakkLRPGYRIVTldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1485 AREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQA 1564
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1565 IEDGKLRLEVNMQAMKAQFERDLQN-----------RDDSNDEKKKLLFKQVREMEVELEEERKQKS--QILAAKKKLEM 1631
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEElkalrealdelRAELTLLNEEAANLRERLESLERRIAATERRleDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1632 DLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKR 1711
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810
....*....|....*
gi 1785379713 1712 QAQQERDDLADELSN 1726
Cdd:TIGR02168 933 GLEVRIDNLQERLSE 947
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1119-1975 |
1.63e-20 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 99.42 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1119 QLRDLQSQLAELHEdlesekaaraKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1198
Cdd:pfam15921 86 QVKDLQRRLNESNE----------LHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1199 AQvtemRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLiKEVKNLQAAKQDS-------------EQRRKKLE 1265
Cdd:pfam15921 156 AA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDF-EEASGKKIYEHDSmstmhfrslgsaiSKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1266 QQVSEFQIRT----NESEKVKFELAEKLQKL-QAELDGVSGALGSTEGKSIKLTKDLSTVQSQ---LQDTQELLQEETRQ 1337
Cdd:pfam15921 231 TEISYLKGRIfpveDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1338 KlnFSSRVRQLEEeknnlmenleeeesakaqLSRQLQALQQQLLESKKRMEDQggmVEAMEeakkksyKELEFLQQRFDE 1417
Cdd:pfam15921 311 Q--NSMYMRQLSD------------------LESTVSQLRSELREAKRMYEDK---IEELE-------KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1418 KHQINDKLEKTRNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKNIsarygeERDRAEAEAREKETKALsl 1495
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITI------DHLRRELDDRNMEVQRL-- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1496 sRALEEAidLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVN 1575
Cdd:pfam15921 432 -EALLKA--MKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1576 MQAMKAQFER--DLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANK-GRDEAVK 1652
Cdd:pfam15921 509 ERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhGRTAGAM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1653 QLKKLQLQfKEV---WREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVS 1729
Cdd:pfam15921 589 QVEKAQLE-KEIndrRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1730 GKSALLDEKRALEMRISQLeeeldeeqsnTELINDRYRKLTLQVETITTELSAERSFSQKAENArqqmerQNKELKVKLN 1809
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNK----------SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS------DGHAMKVAMG 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1810 eMDSTMRSKyKITIASLEAKISQLEEQMEQESKERII----ANKL--------------------VRRAEKRLKEVLLQV 1865
Cdd:pfam15921 732 -MQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFlkeeKNKLsqelstvateknkmagelevLRSQERRLKEKVANM 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1866 EEERRNAD-QFKE------QLEKANIRMKqLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNreVTTLRSRLSKL 1938
Cdd:pfam15921 810 EVALDKASlQFAEcqdiiqRQEQESVRLK-LQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSN--VPSSQSTASFL 886
|
890 900 910
....*....|....*....|....*....|....*....
gi 1785379713 1939 ERQQRKRAPI-QFTTRTIRQVYQ-LEAVSDEEPESHSGE 1975
Cdd:pfam15921 887 SHHSRKTNALkEDPTRDLKQLLQeLRSVINEEPTVQLSK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1005-1829 |
6.41e-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: 97.45 E-value: 6.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1005 AKERKLLDDRI---GEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKM------------------ 1063
Cdd:TIGR02169 152 PVERRKIIDEIagvAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYqallkekreyegyellke 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1064 KRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEV--------GQKNNLLKQLRDLQSQLAELhEDLE 1135
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASL-ERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1136 SEKAARAK-AEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEE---DVKVRDAQVTEMRQRHNQV 1211
Cdd:TIGR02169 311 AEKERELEdAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1212 VEEIseqlEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQK 1291
Cdd:TIGR02169 391 REKL----EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1292 LQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSR-------VRQLEEEKNNLMENLEEEES 1364
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtVAQLGSVGERYATAIEVAAG 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1365 AKAQLSRqlqalqqqlleskkrMEDQGGMVEAMEEAKKKSYKELEFLQQRfdekhQINDK-LEKTRNRLQQELDDLM--V 1441
Cdd:TIGR02169 547 NRLNNVV---------------VEDDAVAKEAIELLKRRKAGRATFLPLN-----KMRDErRDLSILSEDGVIGFAVdlV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1442 DLDHQRQ-----------IVSNLEKKQKKFDQ--MLAEEKNISARYG------EERDRAEAEAREKETKALSLSRALEEA 1502
Cdd:TIGR02169 607 EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKyrMVTLEGELFEKSGamtggsRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1503 IDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQ---AM 1579
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1580 KAQFERDLQN-RDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQ 1658
Cdd:TIGR02169 767 IEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1659 LQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEK 1738
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1739 RALEMRISQLEEELDEEQSNTELINDrYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMdSTMRSK 1818
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL-EEERKA 1004
|
890
....*....|.
gi 1785379713 1819 YKITIASLEAK 1829
Cdd:TIGR02169 1005 ILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
862-1567 |
2.40e-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: 95.51 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 862 QAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE 941
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 942 EERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEedillLEDQNAKLAKERKLLDDRIGEFTST 1021
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1022 MAEEEEKVKSLNKLRNKYEAVIADLEdrlkkEEKGRQEM-EKMKRKLDGETTDLQDQLLELQQQIEELKQ--QLARKEEE 1098
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELA-----QLQARLDSlERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1099 LQAALARV------------DDEVGQKNNLLKQLRDLQSQLAEL----HEDLESEKAARAKAEKQRRDLGEELEALKTEL 1162
Cdd:TIGR02168 535 YEAAIEAAlggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLdsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1163 E-------------DTLDSTAAQQELRAKREQEVTDLKKTIEED------VKVRDAQVTEMRQRHNQVVEEISEQLEQAR 1223
Cdd:TIGR02168 615 RkalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1224 rfkgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGAL 1303
Cdd:TIGR02168 695 ----ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1304 GSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLES 1383
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1384 KKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEkhqindkLEKTRNRLQQELDDLMVDLDhqrqivsNLEKKQKKFDQM 1463
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELR-------ELESKRSELRRE 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1464 LAEEKNISARYGEERDRAEAEAREKETKALSL-SRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGkNVHEL-ERSK 1541
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG-PVNLAaIEEY 995
|
730 740
....*....|....*....|....*.
gi 1785379713 1542 RALEQQVQEMKTQIEELEDELQAIED 1567
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
904-1523 |
3.60e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 904 QAET-----ELFAEAEEMRARLASKK-QELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQ 977
Cdd:COG1196 208 QAEKaeryrELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 978 LEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGR 1057
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1058 QEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESE 1137
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1138 KAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVtDLKKTIEEDVKVRDAQVTEMRQRHNQvvEEISE 1217
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYEGFLEGVKAALLLAGL--RGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1218 QLEQARRFKGNLEKVKQTLESENTDLIkEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELD 1297
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNI-VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1298 GVSgalgstegksikLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQ 1377
Cdd:COG1196 604 VAS------------DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1378 QQLLESKKRMEDQggmveamEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEkkq 1457
Cdd:COG1196 672 AALLEAEAELEEL-------AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL--- 741
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1458 kkFDQMLAEEKNISARYGEERDRAEAEAREKETKAlSLSR-------ALEEAIDLK---DELDRQNKQLRAEMDDL 1523
Cdd:COG1196 742 --LEEEELLEEEALEELPEPPDLEELERELERLER-EIEAlgpvnllAIEEYEELEeryDFLSEQREDLEEARETL 814
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
874-1726 |
4.94e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 874 TQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEA---EEMRARLASKKQE----LEEILHDLEARVEEEEERTL 946
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkktETGKAEEARKAEEakkkAEDARKAEEARKAEDARKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 947 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKllddrigeftstMAEEE 1026
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR------------KAEEE 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1027 EKVKSLNKLRN--KYEAVIADLEDRLKKEEKGRQEMEkmkRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALA 1104
Cdd:PTZ00121 1212 RKAEEARKAEDakKAEAVKKAEEAKKDAEEAKKAEEE---RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1105 RVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVT 1184
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1185 DLKKTIEEDVKVRDA-QVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTdlIKEVKNLQAAKQDSEQRRKK 1263
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAkKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1264 LEQQVSEFQIRTNESEKVKFELAEKLQKL--QAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKlnf 1341
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAkkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK--- 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1342 SSRVRQLEE----EKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDE 1417
Cdd:PTZ00121 1524 ADEAKKAEEakkaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1418 KHQINDKLEKTRNRLQQELDDLMVDLDHQR---QIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKET--KA 1492
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKkveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKA 1683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1493 LSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEEL---EDELQAIEDGK 1569
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLK 1763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1570 LRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQ--KSQILAAKKKLEMDLQDMESQMDSANKGR 1647
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1648 DEAvkqlkklqlqfkevwREVEETRAARDEIFVQSRDNEKKLKSleaELLQLQEDLAAAERAKRQAQQERDDLADELSN 1726
Cdd:PTZ00121 1844 EEA---------------DAFEKHKFNKNNENGEDGNKEADFNK---EKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1440 |
1.61e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 867 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTL 946
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 947 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEE 1026
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1027 EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV 1106
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1107 DDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1186
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1187 KKTIEEDVKVRDAQVT-----EMRQRHNQVVEEISEQLEQARRFkgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRR 1261
Cdd:COG1196 560 AAAIEYLKAAKAGRATflpldKIRARAALAAALARGAIGAAVDL---VASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1262 KKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNF 1341
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1342 SSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKK-------SYKELEFLQQR 1414
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEER 796
|
570 580 590
....*....|....*....|....*....|
gi 1785379713 1415 FDE-KHQINDkLEKTRNRLQQ---ELDDLM 1440
Cdd:COG1196 797 YDFlSEQRED-LEEARETLEEaieEIDRET 825
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
851-1562 |
2.60e-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: 88.97 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 851 LLQVTRQDEVMQAKVVElqkvKDTQVKTESELKEMANKYQQLFEEK-----SILAEQLQAeteLFAEAEEMRARLASKKQ 925
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE----KRQQLERLRREREKAERYQALLKEKreyegYELLKEKEA---LERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 926 ELEEI---LHDLEARVEEEEERTLQLQNEKKKMHQHIQdleeqleeeegARQKLQLEKVTTEsrLKKMEEDILLLEDQNA 1002
Cdd:TIGR02169 252 ELEKLteeISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----------LRVKEKIGELEAE--IASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1003 KLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRL-----------KKEEKGRQEMEKMKRKLDgET 1071
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeleevdKEFAETRDELKDYREKLE-KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1072 TDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDevgQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDL 1151
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEA---KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1152 GEELEALKTELE------DTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRH-------------NQVV 1212
Cdd:TIGR02169 475 KEEYDRVEKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnNVVV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1213 EEIS---EQLEQARRFKGN------LEKVKQtlESENTDLIKE------------------------------VKNLQAA 1253
Cdd:TIGR02169 555 EDDAvakEAIELLKRRKAGratflpLNKMRD--ERRDLSILSEdgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1254 K-QDSEQRRKKLEQQVSEFQ-------IRTNESEKVKFELAEKLQKLQAELDGVSGALGStegksikLTKDLSTVQSQLQ 1325
Cdd:TIGR02169 633 RrLMGKYRMVTLEGELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1326 DTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSY 1405
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1406 KELefLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLdhqrqivsnlekKQKKFDQMLAEEKnisaRYGEERDRAEAEA 1485
Cdd:TIGR02169 786 ARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKL------------NRLTLEKEYLEKE----IQELQEQRIDLKE 847
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379713 1486 REKETKalslsRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDEL 1562
Cdd:TIGR02169 848 QIKSIE-----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1191-1952 |
1.42e-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: 86.66 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1191 EEDVKVRDA-----QVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTL----ESENTDLIKEVKNLQAAKQDSEQRR 1261
Cdd:TIGR02169 167 EFDRKKEKAleeleEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1262 KKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVsgalgsTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNF 1341
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1342 SSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDE-KHQ 1420
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1421 INDkLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqmlaeeknisarygEERDRAEAEAREKETKalslsraLE 1500
Cdd:TIGR02169 401 INE-LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWK-------LE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1501 EAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAI-----------EDGK 1569
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgERYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1570 LRLEV--------------------------------------NMQAMKA------------------QFERDLQN---- 1589
Cdd:TIGR02169 539 TAIEVaagnrlnnvvveddavakeaiellkrrkagratflplnKMRDERRdlsilsedgvigfavdlvEFDPKYEPafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1590 --RD----DSNDEKKKL------------LFKQVREMEVELEEERKQKSQILAAKKKLEM---DLQDMESQMDSANKGRD 1648
Cdd:TIGR02169 619 vfGDtlvvEDIEAARRLmgkyrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1649 EAVKQLKKLQLQFKEVWREVEETRAARDEIfvqsrdnEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGV 1728
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQL-------EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1729 SGKSALLDEKRALEMRISQLEEELDEEQSNTelINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKL 1808
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1809 N------EMDSTMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKA 1882
Cdd:TIGR02169 850 KsiekeiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1883 NIRMKQLKRQLEEAEEEASRANS------NRRRLQRE---LEDVTESAESMNREVTTLRSRL-SKLERQQRKRAPIQFTT 1952
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 ... |
1006-1878 |
4.13e-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: 85.02 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1006 KERKLLDDRIGEFTSTMAEEE------EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLL 1079
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEalkkliEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1080 ELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALK 1159
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1160 TELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRdaqvtemRQRHNQVVEEISEQLEQARRFKGNLEKvKQTLESE 1239
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK-------REAEEEEEEELEKLQEKLEQLEEELLA-KKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1240 NTDLIKEVKNLQAAKQDSEQRRKKLEQQVSE-----FQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLT 1314
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARqledlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1315 KDLSTVQSQLQDTQELLQEETRQKLNFSS---RVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQG 1391
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQkleERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1392 GMVEAMEEAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS 1471
Cdd:pfam02463 545 ISTAVIVEVSATA-DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1472 ARYGEERDRAEAEAREKETKALSLSRA---LEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQV 1548
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1549 QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQIL-AAKK 1627
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEeREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1628 KLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKL----KSLEAELLQLQEDL 1703
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEqkleKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1704 AAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAE 1783
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1784 RSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLL 1863
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
890
....*....|....*
gi 1785379713 1864 QVEEERRNADQFKEQ 1878
Cdd:pfam02463 1024 ELFVSINKGWNKVFF 1038
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1672 |
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 1785379713 864 KVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMR-----ARLASKKQELEEILHDLEARV 938
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKkdaeeAKKAEEERNNEEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 939 EEEEERTLQLQNEKKKMHQHIQDleeqleeeegARQKLQLEKVTTESRLKKMEEdiLLLEDQNAKLAKERKllddrigef 1018
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKK----------AEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADEAK--------- 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1019 tstmAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGEttdlqdqllelqqqieELKQQLARKEEE 1098
Cdd:PTZ00121 1322 ----KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA----------------EKKKEEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1099 lqaALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAA---RAKAEKQRRdlgeeLEALKTELEDTLDSTAAQQEL 1175
Cdd:PTZ00121 1382 ---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKA 1453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1176 RAKREQEvtDLKKTIEEDVKVRDAQVTEMRQRH----NQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1251
Cdd:PTZ00121 1454 EEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKadeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1252 AAKQDSEQRR----KKLEQQVSEFQIRTNEsEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDT 1327
Cdd:PTZ00121 1532 EAKKADEAKKaeekKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1328 QELLQEETRQKlnfSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQL---LESKKRMEDQGGMVEAMEEAKKKS 1404
Cdd:PTZ00121 1611 EAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1405 YKELEFLQQRFDEKHqindKLEKTRNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEknisARYGEERDRAE 1482
Cdd:PTZ00121 1688 KKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEEEKKKI 1759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1483 AEAREKETKALSLSRALEEAIdLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMktqieELEDEL 1562
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM-----EDSAIK 1833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1563 QAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKkllfkqvreMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDS 1642
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEAD---------FNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
810 820 830
....*....|....*....|....*....|.
gi 1785379713 1643 AN-KGRDEAVKQLKKLQLQFKEvwREVEETR 1672
Cdd:PTZ00121 1905 NNmAGKNNDIIDDKLDKDEYIK--RDAEETR 1933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
877-1681 |
2.26e-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: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 877 KTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEE-EERTLQLQNEKKKM 955
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 956 H--------------QHIQDLEEQleeeegaRQKLQLEKVTTESRLKKMEEDIlllEDQNAKLAKerkllddrigeftsT 1021
Cdd:TIGR02169 300 EaeiaslersiaekeRELEDAEER-------LAKLEAEIDKLLAEIEELEREI---EEERKRRDK--------------L 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1022 MAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdQLLELQQQIEELKQQLARKEEELQA 1101
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN--------ELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1102 ALARVDDevgQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtldstaAQQELRAKREQ 1181
Cdd:TIGR02169 428 AIAGIEA---KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK------LQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1182 evtdlKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKV-----------KQTLESENTDLIKEVKN- 1249
Cdd:TIGR02169 499 -----ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAagnrlnnvvveDDAVAKEAIELLKRRKAg 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1250 ------LQAAKQDSEQRRKKLEQQVSEFQIRTNESEKvKFELAeklqklqaeldgVSGALGST-------EGKSIKLTKD 1316
Cdd:TIGR02169 574 ratflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDP-KYEPA------------FKYVFGDTlvvedieAARRLMGKYR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1317 LSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEA 1396
Cdd:TIGR02169 641 MVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1397 MEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKniSARYGE 1476
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1477 ERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIE 1556
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1557 ELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKS------------QILA 1624
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsleDVQA 958
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1625 AKKKLEMDLQDMES-------QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQ 1681
Cdd:TIGR02169 959 ELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1218-1889 |
6.50e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1218 QLEQARRfkgNLEKVkqtlesenTDLIKEVknlqaakqdsEQRRKKLEQQVSE----FQIRTNESEKVKFELAEKLQKLQ 1293
Cdd:COG1196 180 KLEATEE---NLERL--------EDILGEL----------ERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1294 AELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQL 1373
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1374 QALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNL 1453
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1454 EKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKN 1533
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1534 VHELErskRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQnRDDSNDEKKKLLFKQVREMEVELE 1613
Cdd:COG1196 479 LAELL---EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-GVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1614 EERKQKSQILAAKKK---------LEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRD 1684
Cdd:COG1196 555 DDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1685 NEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELsngvsgksaLLDEKRALEMRISQLEEELDEEQSNTELIND 1764
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL---------LEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1765 RYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKitIASLEAKISQLEEQME------ 1838
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD--LEELERELERLEREIEalgpvn 783
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1839 -------QESKERI--IANKL--VRRAEKRLKEVLLQVEEERRnaDQFKEQLEKANIRMKQL 1889
Cdd:COG1196 784 llaieeyEELEERYdfLSEQRedLEEARETLEEAIEEIDRETR--ERFLETFDAVNENFQEL 843
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1723 |
1.50e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 854 VTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRArlASKKQELEEILHD 933
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 934 LEARveeeeertLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVttesrlKKMEEDILLLEDQNAKLAKERKLLDD 1013
Cdd:pfam02463 242 LQEL--------LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK------KLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1014 RIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKrkldgettdlqdqllelqqqieelKQQLA 1093
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE------------------------EELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1094 RKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQ 1173
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1174 ELRAKREQEVTDLKKTIEEDvKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAA 1253
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKD-ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1254 KQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLstVQSQLQDTQELLQE 1333
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK--LKLPLKSIAVLEID 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1334 ETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQ 1413
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1414 RFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEA----REKE 1489
Cdd:pfam02463 681 LQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEeksrLKKE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1490 TKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGK 1569
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1570 LRLEVNMQAMKAQFErdlQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDE 1649
Cdd:pfam02463 841 ELKEEQKLEKLAEEE---LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1650 AVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADE 1723
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1132-1883 |
1.79e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1132 EDLESEKAARAKAEKQRRdlGEELEALKtELEDTLDSTAAQQELRAKREQEVTDLKKtIEEDVKVRDAQVTEMRQRHNQV 1211
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARK--AEEARKAE-DARKAEEARKAEDAKRVEIARKAEDARK-AEEARKAEDAKKAEAARKAEEV 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1212 VE-------EISEQLEQARRFKgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFE 1284
Cdd:PTZ00121 1188 RKaeelrkaEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1285 LAEKLQKLQA--ELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKlnfssrvrQLEEEKNNLMENLEEE 1362
Cdd:PTZ00121 1267 RRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK--------KAEEAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1363 ESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSykelEFLQQRFDEKHQInDKLEKTRNRLQQELDDLMVD 1442
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKA 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1443 LDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR---------EKETKALSLSRALEEAIDlKDELDRQN 1513
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeeakkkaEEAKKADEAKKKAEEAKK-ADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1514 KQLRAEMDDLvSSKDDVGKNVHEL---ERSKRALEQQVQEMKTQIEELE--------DELQAIEDGKLRLEVNMQAMKAQ 1582
Cdd:PTZ00121 1493 EEAKKKADEA-KKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKK 1571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1583 FERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQilAAKKKLEMDLQDMESqmdsanKGRDEAVKQLKKLQLQFK 1662
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEEL------KKAEEEKKKVEQLKKKEA 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1663 EVWREVEETRAARDEIFVQSRDNEKKlkslEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKR-AL 1741
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkAE 1719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1742 EMRISQLEEELDEEQSNTELINDRYRKLTLQVEtitTELSAERSFSQKAENARQQMERQNKELKVK--LNEMDSTMRSKY 1819
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEV 1796
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1820 KITIASLEakiSQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKAN 1883
Cdd:PTZ00121 1797 DKKIKDIF---DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1633-1946 |
3.04e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1633 LQDMESQMDSAnkgRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQ 1712
Cdd:COG1196 195 LGELERQLEPL---ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1713 AQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAEN 1792
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1793 ARQQMERQNKELKVKLNEMDSTMRSKyKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNA 1872
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1873 DQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKRA 1946
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
912-1557 |
3.07e-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: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 912 EAEEMRARLASKKQEL---EEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLK 988
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 989 KMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLD 1068
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1069 GETTDLQDQLLELQQQIEELKqQLARKEEELQAALARVDDEVGQKNnllKQLRDLQSQLAELHEDLESEKAARAKAEKQR 1148
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQ---QEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1149 RDLGEELEALKTELEDTLDS-TAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQR---HNQVVEEISEQLEQARR 1224
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQlNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1225 FKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSgalg 1304
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1305 stegKSIKLTKdlSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKaqlsrqlqalqQQLLESK 1384
Cdd:TIGR04523 426 ----KEIERLK--ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK-----------QNLEQKQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1385 KRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDL--DHQRQIVSNLEKKQKKFDQ 1462
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNK 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1463 MLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDvgknvheLERSKR 1542
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN-------IKSKKN 641
|
650
....*....|....*
gi 1785379713 1543 ALEQQVQEMKTQIEE 1557
Cdd:TIGR04523 642 KLKQEVKQIKETIKE 656
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
835-1533 |
5.89e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 835 KLRHWQWWRLFTKVKPLLQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAEtELFAEAE 914
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 915 EMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQlEKVTTESRLKKMEEDI 994
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 995 LLLEDQNAKLAKERKllddriGEFTSTMAEEEEKVKSLNKlrnkyEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdl 1074
Cdd:PTZ00121 1405 KKADELKKAAAAKKK------ADEAKKKAEEKKKADEAKK-----KAEEAKKADEAKKKAEEAKKAEEAKKKAE------ 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1075 qdqlLELQQQIEELKQQLARKEEELQaalaRVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRdlgEE 1154
Cdd:PTZ00121 1468 ----EAKKADEAKKKAEEAKKADEAK----KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK---KA 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1155 LEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEI-----------SEQLEQAR 1223
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeekkmkAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1224 RFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKfeLAEKLQKLQAELDGVSGAL 1303
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEAL 1694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1304 GSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMEnleeeesAKAQLSRQLQALQQQLLES 1383
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE-------AKKDEEEKKKIAHLKKEEE 1767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1384 KKRMEDQGGMVEAMEEAKKKsykelEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLeKKQKKFDQM 1463
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDE-----EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI-KEVADSKNM 1841
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1464 LAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKN 1533
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKN 1911
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1143-1724 |
6.39e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1143 KAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRdaqvtemrqrhnqvvEEISEQLEQA 1222
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL---------------PELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1223 RRFKGNLEKVKQTLES---ENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKfELAEKLQKLQAELDgv 1299
Cdd:PRK03918 227 EKEVKELEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYE-- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1300 sgalgSTEGKSIKLTKDLSTVQSQLQDTQELLQ--EETRQKLN-FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQAL 1376
Cdd:PRK03918 304 -----EYLDELREIEKRLSRLEEEINGIEERIKelEEKEERLEeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1377 QQQLLESKKRMEDqggMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQ---------------------- 1434
Cdd:PRK03918 379 KRLTGLTPEKLEK---ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelle 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1435 ----ELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELD 1510
Cdd:PRK03918 456 eytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1511 RQNKQLRAEMDDLvSSKDDVGKNVHELERSKRALEQQVQEMKTQI--------EELEDELQAIE----------DGKLRL 1572
Cdd:PRK03918 536 KLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEpfyneylelkDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1573 EVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVK 1652
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 1653 QLKKLQlqfkevwREVEETRAARDEIfvqsrdneKKLKSLEAELLQLQEDLAAAE-RAKRQAQQERDDLADEL 1724
Cdd:PRK03918 695 TLEKLK-------EELEEREKAKKEL--------EKLEKALERVEELREKVKKYKaLLKERALSKVGEIASEI 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
856-1562 |
8.18e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 856 RQDEVmqAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHdle 935
Cdd:PRK03918 133 RQGEI--DAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 936 aRVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEgarqKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLddri 1015
Cdd:PRK03918 208 -EINEISSELPELREELEKLEKEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1016 geftstmaeeEEKVKSLNKLRNK---YEAVIADLEDRLKKEEKGRQEMEKMKRKLDGettdlQDQLLELQQQIEELKQQL 1092
Cdd:PRK03918 279 ----------EEKVKELKELKEKaeeYIKLSEFYEEYLDELREIEKRLSRLEEEING-----IEERIKELEEKEERLEEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1093 ARKEEELQAALARVDDEVgqknNLLKQLRDLQSQLAELHEDLESEKAARAKAEKqrrdlgEELEALKTELEDTLDSTAAQ 1172
Cdd:PRK03918 344 KKKLKELEKRLEELEERH----ELYEEAKAKKEELERLKKRLTGLTPEKLEKEL------EELEKAKEEIEEEISKITAR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1173 qelRAKREQEVTDLKKTIEEDVKVRD------AQVTEmrqrhnqvvEEISEQLEQARRFKGNLEKVKQTLESENTDLIKE 1246
Cdd:PRK03918 414 ---IGELKKEIKELKKAIEELKKAKGkcpvcgRELTE---------EHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1247 VKNLQaaKQDSEQRRKKLEQQVSEfQIRTNESEKVKFELaEKLQKLQAELDGVsgalgstEGKSIKLTKDLSTVQSQLQD 1326
Cdd:PRK03918 482 LRELE--KVLKKESELIKLKELAE-QLKELEEKLKKYNL-EELEKKAEEYEKL-------KEKLIKLKGEIKSLKKELEK 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1327 TQELLQEetrqKLNFSSRVRQLEEEKnnlmenleeeesakaqlsrqlqalqqqlLESKKRMEDQGgmVEAMEEAKKKsYK 1406
Cdd:PRK03918 551 LEELKKK----LAELEKKLDELEEEL----------------------------AELLKELEELG--FESVEELEER-LK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1407 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEEKNISARYGEErdraeaEAR 1486
Cdd:PRK03918 596 ELEPFYNEYLELKDAEKELEREEKELKKLEEEL-------DKAFEELAETEKRLEELRKELEELEKKYSEE------EYE 662
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1487 EKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEqQVQEMKTQIEELEDEL 1562
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1179-1892 |
1.91e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1179 REQEVTDLKKTIEEDVKV-RDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDL--IKEVKNLQAAKQ 1255
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAeAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1256 DSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQ--SQLQDTQELLQE 1333
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDARKA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1334 ETRQKlnfSSRVRQLEEEKNNlmenleeeesakaqlsrqlqalqqqllESKKRMEDqggmVEAMEEAKKKSYKEleflqq 1413
Cdd:PTZ00121 1203 EAARK---AEEERKAEEARKA---------------------------EDAKKAEA----VKKAEEAKKDAEEA------ 1242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1414 rfdekhqinDKLEKTRNRLQ-QELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS--ARYGEERDRAEAEAR--EK 1488
Cdd:PTZ00121 1243 ---------KKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKkaEE 1313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1489 ETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELE---DELQAI 1565
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKA 1393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1566 EDGKLRLEVNMQamKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQilAAKKKLEMDLQDMESQMDSANK 1645
Cdd:PTZ00121 1394 DEAKKKAEEDKK--KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEA 1469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1646 GRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAK-----RQAQQERDdl 1720
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkadeaKKAEEKKK-- 1547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1721 ADELSNGVSGKSA-----LLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQ 1795
Cdd:PTZ00121 1548 ADELKKAEELKKAeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1796 QMERQNKELKVKLNEMDSTMRSK--------YKITIASLEAKISQ----LEEQMEQESKERIIANKLVRRAE--KRLKEV 1861
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEelkkaeeeNKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAAEALKKEAEeaKKAEEL 1707
|
730 740 750
....*....|....*....|....*....|.
gi 1785379713 1862 LLQVEEERRNADQFKEQLEKANIRMKQLKRQ 1892
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1945 |
3.04e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1382 ESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEkhqINDKLEKTRNRLQqELDDLMVDLDHQRQIVSNLEKKQKKFD 1461
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINE---ISSELPELREELE-KLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1462 QmlaEEKNISARYGEERDRAEaEAREKETKALSLSRALEEAIDLKDELDRqnkqLRAEMDDLVSSKDDVGKNVHELERSK 1541
Cdd:PRK03918 252 G---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1542 RALEQQVQE---MKTQIEELEDELQAIEDGKLRLEVNMQAmkaqFERDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQ 1618
Cdd:PRK03918 324 NGIEERIKEleeKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1619 KSQILAAKKKLEmdlqDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEEtraardeifvqsRDNEKKLKSLEAELLQ 1698
Cdd:PRK03918 400 KEEIEEEISKIT----ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE------------EHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1699 LQEDLAAAERAKRQAQQERDDLADELSNG--VSGKSALLDEKRALEMRISQ-LEEELDEEQSNTELINDRYRKLTLQVET 1775
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1776 ITTELSAERSFsqkaENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKeriianklVRRAE 1855
Cdd:PRK03918 544 LKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE--------LKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1856 KRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEAS-----RANSNRRRLQRELEDVTESAESMNREVTT 1930
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELAGLRAELEELEKRREE 691
|
570
....*....|....*
gi 1785379713 1931 LRSRLSKLERQQRKR 1945
Cdd:PRK03918 692 IKKTLEKLKEELEER 706
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1286-1944 |
4.34e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 71.74 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1286 AEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEeknnlmenleeeesa 1365
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEE--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1366 kaqlsrqlqalqqQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDH 1445
Cdd:pfam01576 76 -------------ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1446 QRQIVSNLEKKQKKFDQMLAEeknISARYGEErdraeaearEKETKALSLSRALEEAI--DLKDELDRQNKQlRAEMDdl 1523
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISE---FTSNLAEE---------EEKAKSLSKLKNKHEAMisDLEERLKKEEKG-RQELE-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1524 vsskddvgKNVHELERSKRALEQQVQEMKTQIEEL-------EDELQAIEDgklRLEvNMQAMKAQFERDLQNRDDSNDE 1596
Cdd:pfam01576 208 --------KAKRKLEGESTDLQEQIAELQAQIAELraqlakkEEELQAALA---RLE-EETAQKNNALKKIRELEAQISE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1597 KKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKgRDEAVKQLKKLQlqfkevwreVEETRAARD 1676
Cdd:pfam01576 276 LQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK-REQEVTELKKAL---------EEETRSHEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1677 EIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQ 1756
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1757 SNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEmDSTMRSKYKITIASLEAKISQLEEQ 1836
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1837 MEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELED 1916
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDD 584
|
650 660
....*....|....*....|....*...
gi 1785379713 1917 VTesaesmnREVTTLRSRLSKLERQQRK 1944
Cdd:pfam01576 585 LL-------VDLDHQRQLVSNLEKKQKK 605
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
899-1236 |
4.44e-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: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 899 LAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQL 978
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 979 EKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQ 1058
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1059 EMEKMKRK-------LDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH 1131
Cdd:TIGR02168 842 DLEEQIEElsediesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1132 EDLESEKAARAKAEKQRRDLGEEL-EALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIE-------------EDVKVR 1197
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyEELKER 1001
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1785379713 1198 -------DAQVTEMRQRHNQVVEEISEQLEQarRFKGNLEKVKQTL 1236
Cdd:TIGR02168 1002 ydfltaqKEDLTEAKETLEEAIEEIDREARE--RFKDTFDQVNENF 1045
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
867-1541 |
5.54e-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: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 867 ELQKVKDTQVKTESELKEMANKYQqlfEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHD----------LEA 936
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 937 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEkvTTESRLK---KMEEDILLLEDQNAKLAKERKLLDD 1013
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQ--AENARLEmhfKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1014 RIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELkqqla 1093
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL----- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1094 rkEEELQAALARVDDEVGQKNNLLKQLR-----------DLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTEL 1162
Cdd:pfam05483 316 --EEDLQIATKTICQLTEEKEAQMEELNkakaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1163 EDtldstaaQQELRAKREQEVTDLKKTIEEDVKVRD--AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESEN 1240
Cdd:pfam05483 394 EE-------MTKFKNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1241 TDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSgalgSTEGKSIKLTKDLSTV 1320
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK----KQEERMLKQIENLEEK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1321 QSQLQDTQELLQEETRQKLN-FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEE 1399
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1400 AKKKSYKELEFLQQRFD----EKHQINDKLEKTRNRLQQELDD-------LMVDLDHQRQIVSNLEKKQKKFDQ------ 1462
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNklelELASAKQKFEEIIDNYQKEIEDkkiseekLLEEVEKAKAIADEAVKLQKEIDKrcqhki 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1463 -----MLAEEKNISARYGEERDRAEAEAREKETKALSLSRALE-EAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHE 1536
Cdd:pfam05483 703 aemvaLMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEiELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAI 782
|
....*
gi 1785379713 1537 LERSK 1541
Cdd:pfam05483 783 LKDKK 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1423-1939 |
5.65e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.20 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1423 DKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEA 1502
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1503 IDLKDELDRQNKQLRAEMDDLVSSK---DDVGKNVHELERSKRALEQQVQ-----EMKTQIEELEDELQAIEDGKLRLEV 1574
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNkkiKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1575 NMQAMK---AQFERDLQNRDDSNDEKKKllfkQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAV 1651
Cdd:TIGR04523 336 IISQLNeqiSQLKKELTNSESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1652 KQLKKLQLQFKEVWREVEETRAAR-------DEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADEL 1724
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIiknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1725 SNGVSGKSALLDEKRALEMrisqleeeldeeqsntelindryrkltlQVETITTELSAERSFSQKAENARQQMERQNKEL 1804
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEE----------------------------KVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1805 KVKLNEMDSTM-RSKYKITIASLEAKISQLEEqmeqeskeriiANKLVRRAEKRLKEVLLQVEEERRNadqFKEQLEKAN 1883
Cdd:TIGR04523 544 EDELNKDDFELkKENLEKEIDEKNKEIEELKQ-----------TQKSLKKKQEEKQELIDQKEKEKKD---LIKEIEEKE 609
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1884 IRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLE 1939
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1005-1539 |
5.85e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1005 AKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMK---RKLDGETTDLQDQLLEL 1081
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1082 QQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLE----SEKAARAKAEKQRRD------- 1150
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddleer 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1151 ---LGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIE------EDVKVRDAQVTEMRQRHNQVVEEISEQLEQ 1221
Cdd:PRK02224 358 aeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREERDELREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1222 ARrfkGNLEKVKQTLES----ENTDLIKEVKNLQAAkQDSEQRRKKLEQQVSEFQIRTNESEKvKFELAEKLQKLQAELD 1297
Cdd:PRK02224 438 AR---ERVEEAEALLEAgkcpECGQPVEGSPHVETI-EEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1298 gvsgalgstegksiKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQ 1377
Cdd:PRK02224 513 --------------RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1378 QQLLESKKRMEDQGGMVEAMEEAKKKSyKELEFLQQRFDEKHQIND----KLEKTRNR---LQQELDDLMVDLDHQR--Q 1448
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIADAE-DEIERLREKREALAELNDerreRLAEKRERkreLEAEFDEARIEEAREDkeR 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1449 IVSNLEKKQKKFDQMLAEEKNISARYGE-ERDRAEAEAREKETKALSLSR-ALEEAIDLKDELDRQNKQLRAEMDDlvss 1526
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAvENELEELEELRERREALENRVeALEALYDEAEELESMYGDLRAELRQ---- 733
|
570
....*....|...
gi 1785379713 1527 kddvgKNVHELER 1539
Cdd:PRK02224 734 -----RNVETLER 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
857-1158 |
6.12e-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: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 857 QDEVMQAKVVELQKVKDTQvktESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA 936
Cdd:TIGR02168 706 ELEELEEELEQLRKELEEL---SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 937 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIG 1016
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1017 EFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKE 1096
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379713 1097 E--------ELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH-------EDLESEKAARAKAEKQRRDLGEELEAL 1158
Cdd:TIGR02168 943 ErlseeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1043-1601 |
1.34e-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: 70.25 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1043 IADLEDRLKKEEKGRQEMEKMKR-KLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV----DDEVGQKNNLL 1117
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1118 KQLRDLQSQLAELHEDLE--SEKAARAKAEKQRRDLGEELEaLKTELEDTLDSTAAQQELRakreqevtDLKKTIEEDVk 1195
Cdd:pfam12128 347 EQLPSWQSELENLEERLKalTGKHQDVTAKYNRRRSKIKEQ-NNRDIAGIKDKLAKIREAR--------DRQLAVAEDD- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1196 vRDAQVTEMRQRHNQVVEEISEQleqARRFKGNLEKVK------QTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVS 1269
Cdd:pfam12128 417 -LQALESELREQLEAGKLEFNEE---EYRLKSRLGELKlrlnqaTATPELLLQLENFDERIERAREEQEAANAEVERLQS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1270 EFQI----RTNESEKVKF------ELAEKLQKLQAELDGVSGAL-----GSTEGKSIKLTKDLSTVQSQLQDTQ-ELLQE 1333
Cdd:pfam12128 493 ELRQarkrRDQASEALRQasrrleERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKVISPELLHRTDLDpEVWDG 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1334 ETRQKLNFSS---RVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESK-KRMEDQGGMVEAMEEAKKKSYKELE 1409
Cdd:pfam12128 573 SVGGELNLYGvklDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQlVQANGELEKASREETFARTALKNAR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1410 FLQQR-FDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIvsnLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREK 1488
Cdd:pfam12128 653 LDLRRlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1489 ETKALSLSRALEEAidlkdELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQV-------------------- 1548
Cdd:pfam12128 730 QLALLKAAIAARRS-----GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriavrrqevlryfdwyqet 804
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379713 1549 -----QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLL 1601
Cdd:pfam12128 805 wlqrrPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENL 862
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1629-1943 |
2.36e-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: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1629 LEMDLQDMESQMDSANKGRdEAVKQLKKLQLqfkEVW-REVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAE 1707
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYK-ELKAELRELEL---ALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1708 RAKRQAQQERDDLADELSNgvsgksaLLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFS 1787
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYA-------LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1788 QKAENARQQMERQNKELKVKLNEMDSTMRSKYKiTIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEE 1867
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEE-QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1868 ERRNADqfKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQR 1943
Cdd:TIGR02168 426 LLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
880-1890 |
2.59e-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: 69.31 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 880 SELKEMANKYQQLFEEksilaeqlqaeTELFAEAEEMRARLASKKQELEEilHDLEarveeeeertLQLQNEKKKMHQHI 959
Cdd:TIGR00606 166 SEGKALKQKFDEIFSA-----------TRYIKALETLRQVRQTQGQKVQE--HQME----------LKYLKQYKEKACEI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 960 QDLEEQLEEEEGARQKLQLEKvttESRLKKMEEDILLLEDQNAKLAKerklLDDRIGEFTSTMAEEEEKVKSLNKLRnky 1039
Cdd:TIGR00606 223 RDQITSKEAQLESSREIVKSY---ENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSRKKQMEKDNSELELKM--- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1040 EAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVgQKNNLLKQ 1119
Cdd:TIGR00606 293 EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI-RARDSLIQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1120 LRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDA 1199
Cdd:TIGR00606 372 SLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1200 QVTEMRQRHNQV------VEEISEQLEQARRFKGNLEKVKQTLESENtdLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQI 1273
Cdd:TIGR00606 452 KQEELKFVIKELqqlegsSDRILELDQELRKAERELSKAEKNSLTET--LKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1274 RTNESEKVKFELAEKLQKLQA-------ELDGVSGALGSTEGKSI------KLTKDLSTVQSQLQDTQELLQEETRQKLN 1340
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKELASLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1341 FSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRmedqggmveAMEEAKKKSYKelEFLQQRFDEKHQ 1420
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQR---------AMLAGATAVYS--QFITQLTDENQS 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1421 ---INDKLEKTRNRLQQELDDLMVDL----DHQRQIVSNLEKKQKKFDQMLAeeknISARYGEERDRAEAEAREKETKAL 1493
Cdd:TIGR00606 679 ccpVCQRVFQTEAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMLG----LAPGRQSIIDLKEKEIPELRNKLQ 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1494 SLSRALEEaidLKDELDRQNKQLRAEMDDLVSSKdDVGKNVHELERskraLEQQVQEMKTQIEELEDELQAIEDGKLRLE 1573
Cdd:TIGR00606 755 KVNRDIQR---LKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMER----FQMELKDVERKIAQQAAKLQGSDLDRTVQQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1574 VNmqamkaQFERDLQNRDDSNDEKKKLLFKqvremeveleEERKQKSQILAAKKKLEmDLQDMESQMDSANKGRDEAVKQ 1653
Cdd:TIGR00606 827 VN------QEKQEKQHELDTVVSKIELNRK----------LIQDQQEQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQ 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1654 LKKLQLQFKEVWREVEEtraARDEIFVQSrdnekklKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSA 1733
Cdd:TIGR00606 890 LVELSTEVQSLIREIKD---AKEQDSPLE-------TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1734 LL--------DEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVET--ITTELSAERSFSQKAENARQQMERQNKE 1803
Cdd:TIGR00606 960 IEnkiqdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1804 LKVKLNEMDST-MRSKYKI------TIASLEAKISQLEEQMEQESK--ERIIANKLVRRAEKRLKEVLLQV---EEERRN 1871
Cdd:TIGR00606 1040 HLKEMGQMQVLqMKQEHQKleenidLIKRNHVLALGRQKGYEKEIKhfKKELREPQFRDAEEKYREMMIVMrttELVNKD 1119
|
1050
....*....|....*....
gi 1785379713 1872 ADQFKEQLEKANIRMKQLK 1890
Cdd:TIGR00606 1120 LDIYYKTLDQAIMKFHSMK 1138
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1206-1945 |
7.13e-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: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1206 QRHNQVVEEISEQLEQARRFKgNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEqqvsEFQIRTNESEKVKFEL 1285
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKE-ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE----YYQLKEKLELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1286 AEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFssrvrqLEEEKNNLMENLEEEESA 1365
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL------QEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1366 KAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDH 1445
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1446 QRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDEldrqNKQLRAEMDDLVS 1525
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG----KLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1526 SKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMK-AQFERDLQNRDDSNDEKKKLLFKQ 1604
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLlALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1605 VREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSaNKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRD 1684
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPL-GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1685 NEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDD--LADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELI 1762
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1763 NDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLE-EQMEQES 1841
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1842 KERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMkqlKRQLEEAEEEASRANSNRRRLQRELEDVTESA 1921
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740
....*....|....*....|....
gi 1785379713 1922 ESMNREVTTLRSRLSKLERQQRKR 1945
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEE 877
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
8.21e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 58.60 E-value: 8.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1785379713 31 TAKRQVWVPSEKHGFEAASIKEERGEEVIVELaENGKRVPVAKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1726 |
1.02e-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: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 845 FTKVKPLLQVTRQD--EVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSIlAEQLQAETELFAEAEEMRARLAS 922
Cdd:TIGR00606 184 YIKALETLRQVRQTqgQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 923 KKQELEEILHDLEArveeeeeRTLQLQNEKKKMHQhiqdleEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNA 1002
Cdd:TIGR00606 263 KIMKLDNEIKALKS-------RKKQMEKDNSELEL------KMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1003 KLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLK------------------KEEKGRQEME-KM 1063
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpfserqiknfhTLVIERQEDEaKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1064 KRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAK 1143
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1144 AEKQR--RDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKT--IEEDVKVRDAQVTEMRQRHNQVVEEISEQL 1219
Cdd:TIGR00606 490 AEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMemLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1220 EQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRR---KKLEQQVSEFQIRTNESEKVKfELAEKLQKLQAEL 1296
Cdd:TIGR00606 570 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINnelESKEEQLSSYEDKLFDVCGSQ-DEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1297 DGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESakaqlsrqlqal 1376
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES------------ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1377 qqQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRF--------DEKHQI--NDKLEKTRNRLQQELDDLMVDLDHQ 1446
Cdd:TIGR00606 717 --ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqkvnrdiqRLKNDIeeQETLLGTIMPEEESAKVCLTDVTIM 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1447 RQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEarEKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSS 1526
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1527 KDDVGKNVHElersKRALEQQVQEMKTQIEELedeLQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVR 1606
Cdd:TIGR00606 873 KLQIGTNLQR----RQQFEEQLVELSTEVQSL---IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1607 EMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVE----ETRAARDEIFVQS 1682
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkiQERWLQDNLTLRK 1025
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1785379713 1683 RDNEkkLKSLEAELLQLQEDLaaAERAKRQAQQERDDLADELSN 1726
Cdd:TIGR00606 1026 RENE--LKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDL 1065
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1090-1724 |
2.38e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1090 QQLARKEEELQAALARVDDEVGQ-KNNLLKQ-LRDLQSQLAELHEDLESEKAARAKAEKQRRDL--------GEELEALK 1159
Cdd:COG4913 265 AAARERLAELEYLRAALRLWFAQrRLELLEAeLEELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1160 TELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESE 1239
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPAS----AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1240 NTDLIKEVKNLQAAK----QDSEQRRKKLEQQVSefqirtNESEKVKFeLAEKLQKLQAELD---GVSGALGstegkSIK 1312
Cdd:COG4913 421 LRELEAEIASLERRKsnipARLLALRDALAEALG------LDEAELPF-VGELIEVRPEEERwrgAIERVLG-----GFA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1313 LT-----KDLSTVQSQLQDTQellqeeTRQKLNFsSRVRQLEEEKNNLMEnleeeesakaqlsrqlqalqqqlleskkrm 1387
Cdd:COG4913 489 LTllvppEHYAAALRWVNRLH------LRGRLVY-ERVRTGLPDPERPRL------------------------------ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1388 eDQGGMVEAMEEAKKKSYKELEF-LQQRFD---------------------------EKHQINDKLEKTRN--------- 1430
Cdd:COG4913 532 -DPDSLAGKLDFKPHPFRAWLEAeLGRRFDyvcvdspeelrrhpraitragqvkgngTRHEKDDRRRIRSRyvlgfdnra 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1431 ---RLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALsLSRALEEAIDLKd 1507
Cdd:COG4913 611 klaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE-LERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1508 ELDRQNKQLRAEMDDLVSSKDdvgknvhELERSKRALEQQVQEMKTQIEELEDELQAIEDGKlrlevnMQAMKAQFERDL 1587
Cdd:COG4913 689 ALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA------RLELRALLEERF 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1588 QNRDDSNDEKKKllfkqvremeveleeerkqksqilaakkklemdLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWR- 1666
Cdd:COG4913 756 AAALGDAVEREL---------------------------------RENLEERIDALRARLNRAEEELERAMRAFNREWPa 802
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1667 EVEETRAARDEIfvqsRDNEKKLKSLEAE-LLQLQEDLaaAERAKRQAQQERDDLADEL 1724
Cdd:COG4913 803 ETADLDADLESL----PEYLALLDRLEEDgLPEYEERF--KELLNENSIEFVADLLSKL 855
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1089-1296 |
2.48e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtlds 1168
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1169 taAQQELRAKREQEVTDLKKTIEEDVKVRD---AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDL-- 1243
Cdd:COG4942 101 --AQKEELAELLRALYRLGRQPPLALLLSPedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELea 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379713 1244 -----IKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAEL 1296
Cdd:COG4942 179 llaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
861-1574 |
2.90e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.91 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 861 MQAKVVELQKVKDTQV---KTESELKE-----MANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILH 932
Cdd:pfam15921 115 LQTKLQEMQMERDAMAdirRRESQSQEdlrnqLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 933 DLEarveeeeertlqlQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMeedILLLEDQNAKLAKERK--- 1009
Cdd:pfam15921 195 DFE-------------EASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGR---IFPVEDQLEALKSESQnki 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1010 --LLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLK--KEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQI 1085
Cdd:pfam15921 259 elLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1086 ------EELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKqrRDLGEEL--EA 1157
Cdd:pfam15921 339 myedkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWD--RDTGNSItiDH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1158 LKTELEDtldstaaqqelRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKV----- 1232
Cdd:pfam15921 417 LRRELDD-----------RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVveelt 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1233 --KQTLESE-------NTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES----------EKVKFELAEK---LQ 1290
Cdd:pfam15921 486 akKMTLESSertvsdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKdkvIE 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1291 KLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLS 1370
Cdd:pfam15921 566 ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1371 RQLQALQQQLLESKKRMEDQGGMVEAMEEakkksykELEFLQQRFDEKhqiNDKLEKTRNRLQQELDDLMVDLDHQRQIV 1450
Cdd:pfam15921 646 RAVKDIKQERDQLLNEVKTSRNELNSLSE-------DYEVLKRNFRNK---SEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1451 SNLEKKQ-KKFDQMLAEEKNISARYGeerdraeaEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDD 1529
Cdd:pfam15921 716 KSMEGSDgHAMKVAMGMQKQITAKRG--------QIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNK 787
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1530 VGKNVHELERSKRALEQQVQEMKT-------QIEELEDELQAIEDGKLRLEV 1574
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
879-1346 |
4.02e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 879 ESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA----------RVEEEEERTLQL 948
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereelaeEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 949 QNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRL--------------KKMEEDILLLEDQNAKLAKERKLLDDR 1014
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeecrvaaqahneeaESLREDADDLEERAEELREEAAELESE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1015 IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIeelkqqlaR 1094
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV--------E 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1095 KEEELQAA---------------LARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAArAKAEKQRRDLGEELEALK 1159
Cdd:PRK02224 444 EAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1160 TELEDTLDSTAAQQELRAKREQEVTDLkktieedvkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESE 1239
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAEL-----------EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1240 NT---------DLIKEVKNLQAAKQD----SEQRRKKL---------------EQQVSEFQIRTNESEKVKFELAEKLQK 1291
Cdd:PRK02224 592 ERirtllaaiaDAEDEIERLREKREAlaelNDERRERLaekrerkreleaefdEARIEEAREDKERAEEYLEQVEEKLDE 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379713 1292 LQAELDGVSGALGSTEGkSIKLTKDLSTVQSQLQDTQELLQ---EETRQKLNFSSRVR 1346
Cdd:PRK02224 672 LREERDDLQAEIGAVEN-ELEELEELRERREALENRVEALEalyDEAEELESMYGDLR 728
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1409-1945 |
7.98e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1409 EFLQQRFDEKHQINDKLEKTRnrlqQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEArek 1488
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERR----EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1489 etkalSLSRALEEAI-DLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQ---- 1563
Cdd:PRK02224 303 -----GLDDADAEAVeARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEeare 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1564 AIEDGKLRLEvnmqamkaqferDLQNRDDSNDEkkkllfkqvremeveleeerkqksqilaAKKKLEMDLQDMESQMDSA 1643
Cdd:PRK02224 378 AVEDRREEIE------------ELEEEIEELRE----------------------------RFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1644 NKGRDEAVKQLKKLQLQFKEVWREVEETRAARDE--------------IFVQSRDNEKKLKSLEAELLQLQEDLAAAEra 1709
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVE-- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1710 krqaqqERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRyrkltlqVETITTELSAERSFSQK 1789
Cdd:PRK02224 496 ------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1790 AENARQQMERQNKELKVKLNEMDSTMRSKYKI-----TIASLEAKISQLEEQ------MEQESKERiIANKLVRRAEKRL 1858
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLERIrtllaAIADAEDEIERLREKrealaeLNDERRER-LAEKRERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1859 KEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQR------ELEDVTESAESMNREVTTLR 1932
Cdd:PRK02224 642 EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEElrerreALENRVEALEALYDEAEELE 721
|
570
....*....|...
gi 1785379713 1933 SRLSKLERQQRKR 1945
Cdd:PRK02224 722 SMYGDLRAELRQR 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1439 |
1.15e-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: 63.93 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 859 EVMQAKVVELQKV-------KDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEIL 931
Cdd:TIGR02169 364 EELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 932 HDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQnaklakeRKLL 1011
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV-------EEVL 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1012 DDRIGEFTSTMAE----EEEKVKSL-----NKLRN---KYEAVIADLEDRLKKEEKGR---------------------- 1057
Cdd:TIGR02169 517 KASIQGVHGTVAQlgsvGERYATAIevaagNRLNNvvvEDDAVAKEAIELLKRRKAGRatflplnkmrderrdlsilsed 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1058 ------------------------------QEMEKMKR--------KLDGETTDLQDQLLELQQQIEELKQQLARKEEEL 1099
Cdd:TIGR02169 597 gvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1100 QAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKR 1179
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1180 EQEVTDLKKTI---EEDVKVRDAQVTEMRQRHN-QVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQ 1255
Cdd:TIGR02169 757 KSELKELEARIeelEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1256 DSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDtqellQEET 1335
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-----LEAQ 911
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1336 RQKLNfsSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMvEAMEEAKKKSYKELEFLQQRF 1415
Cdd:TIGR02169 912 IEKKR--KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRL 988
|
650 660
....*....|....*....|....
gi 1785379713 1416 DEKHQINDKLEKTRNRLQQELDDL 1439
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEY 1012
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1126-1742 |
1.21e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1126 QLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtldstaaqqelraKREQEVTDLKKTIEEDVKVRDAQvtemr 1205
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEE-------------KEEKDLHERLNGLESELAELDEE----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1206 qrhnqvVEEISEQLEQARRFKGNLEKV----KQTLEsENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNesekv 1281
Cdd:PRK02224 222 ------IERYEEQREQARETRDEADEVleehEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE----- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1282 kfELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEE 1361
Cdd:PRK02224 290 --ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1362 EESAkaqlsrqlqalqqqLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMV 1441
Cdd:PRK02224 368 LESE--------------LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1442 DLdhqrqivSNLEKKQKKFDQMLAEEK-----------NISARYGEERDRAEAEAREKETKALSLSrALEEAIDLKDELd 1510
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVE-EVEERLERAEDL- 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1511 rqnKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMK---AQFERDL 1587
Cdd:PRK02224 505 ---VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKL 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1588 QNRDDSNDEKKKLlfkqvremeveleeerkqkSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWRE 1667
Cdd:PRK02224 582 AELKERIESLERI-------------------RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1668 VEETRA----ARDEIFVQSRDN-EKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLaDELSNGVSGKSALLDEKRALE 1742
Cdd:PRK02224 643 FDEARIeearEDKERAEEYLEQvEEKLDELREERDDLQAEIGAVENELEELEELRERR-EALENRVEALEALYDEAEELE 721
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1089-1881 |
2.08e-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: 62.73 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKaarakaeKQRRDLGEELEALKTELEDtlds 1168
Cdd:TIGR04523 46 KNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-------DKINKLNSDLSKINSEIKN---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1169 taaQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVvEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVK 1248
Cdd:TIGR04523 115 ---DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL-EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1249 NLQAAKQDSE----------QRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLS 1318
Cdd:TIGR04523 191 KIKNKLLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1319 TVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKnnlmenleeeesakaqlsrqlqalqqqlleskkrmeDQGGMVEAME 1398
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK------------------------------------EQDWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1399 EAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELddlmvdldhqrqivSNLEKKQKKFDQMLAEEKNisarygeer 1478
Cdd:TIGR04523 315 ELKNQE-KKLEEIQNQISQNNKIISQLNEQISQLKKEL--------------TNSESENSEKQRELEEKQN--------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1479 dRAEAEAREKETKALSLSRALEEAIDLKDELDRQnKQLRAEMDdlvsskddvgKNVHELERSKRALEQQVQEMKTQIEEL 1558
Cdd:TIGR04523 371 -EIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-EKLNQQKD----------EQIKKLQQEKELLEKEIERLKETIIKN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1559 EDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEErKQKSQILAAKKKLEMDLQDMES 1638
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE-KELKKLNEEKKELEEKVKDLTK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1639 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEEtraarDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERD 1718
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNK-----DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1719 DLADElsngvsgKSALLDEKRALEMRISQleeeldeEQSNTELINDRYRKLTLQVETIttelsaeRSFSQKAENARQQME 1798
Cdd:TIGR04523 593 QKEKE-------KKDLIKEIEEKEKKISS-------LEKELEKAKKENEKLSSIIKNI-------KSKKNKLKQEVKQIK 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1799 RQNKELKVKLNEMDSTMR-SKYKITiasleaKISQLEEQMEQESKERI---IANKLVRRAEKRLKEVLLQVEEERRNADQ 1874
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKeSKTKID------DIIELMKDWLKELSLHYkkyITRMIRIKDLPKLEEKYKEIEKELKKLDE 725
|
....*..
gi 1785379713 1875 FKEQLEK 1881
Cdd:TIGR04523 726 FSKELEN 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1203-1940 |
3.02e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1203 EMRQRHNQVVEEISeQLEQARRFKGNLEKVKQTLESEntdlIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVK 1282
Cdd:PRK03918 142 ESDESREKVVRQIL-GLDDYENAYKNLGEVIKEIKRR----IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1283 FELAEKLQKLQAELDgvsgalgstegksikltkdlstvqsQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEee 1362
Cdd:PRK03918 217 PELREELEKLEKEVK-------------------------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1363 esakaqlsrqlqalqqqllESKKRMEDQGGMVEAMEEAKKKSyKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLmvd 1442
Cdd:PRK03918 270 -------------------ELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI--- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1443 ldhQRQIvSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAeareketkalslsraLEEAIDLKDELDRQNKQLRAEmdd 1522
Cdd:PRK03918 327 ---EERI-KELEEKEERLEELKKKLKELEKRLEELEERHEL---------------YEEAKAKKEELERLKKRLTGL--- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1523 lvsSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvnmqamKAQFERDLQNRDDSNDEKKKLLF 1602
Cdd:PRK03918 385 ---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELLE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1603 K---QVREMEVELEEERKQKSQILAAKKKLEMDLQDME--SQMDSANKGRDEAVKQLKKLQLQ-FKEVWREVEETRAARD 1676
Cdd:PRK03918 456 EytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLI 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1677 EIFVQSRDNEKKLKSLEAellqLQEDLAAAERAKRQAQQERDDLADELSNgVSGKSALLDEKRALEMrisqleeeldeeq 1756
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERLKEL------------- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1757 sntELINDRYRKLtlqvetittelsaersfsqkaENARQQMERQNKELKVKLNEMDST--MRSKYKITIASLEAKISQLE 1834
Cdd:PRK03918 598 ---EPFYNEYLEL---------------------KDAEKELEREEKELKKLEEELDKAfeELAETEKRLEELRKELEELE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1835 EQMEQESKERIiaNKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKanirmkqLKRQLEEAeeeaSRANSNRRRLQREL 1914
Cdd:PRK03918 654 KKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEK-------LKEELEER----EKAKKELEKLEKAL 720
|
730 740
....*....|....*....|....*..
gi 1785379713 1915 EDVTESAESMNREVTTLRSR-LSKLER 1940
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERaLSKVGE 747
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
868-1332 |
3.05e-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: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 868 LQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQ 947
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 948 LQNEKKKMHQHIQDLEEQLEEEEGARQKLQLE-----KVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTM 1022
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1023 AEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdqllelqqqieelkQQLARKEEELQAA 1102
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD---------------------EQIKKLQQEKELL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1103 LARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTldstaaQQELRAKREQ- 1181
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK------QKELKSKEKEl 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1182 -EVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENtdLIKEVKNLQAAKQDSEQR 1260
Cdd:TIGR04523 499 kKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQT 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1261 RKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQ 1332
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
857-1252 |
3.26e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 857 QDEVMQAKVVELQKVKDTQVKTEsELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEA 936
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 937 RVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQ--------------LEKVTTESRLKKMEEDILLLEDQNA 1002
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1003 KLAKERKLLDDRIgEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQ 1082
Cdd:PRK02224 486 DLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1083 QQIEELKQQLARKEEELQAALARVDDevgqknnlLKQLRDLQSQLAELHEDLES---EKAARAKAEKQRRDLGEELEALK 1159
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIES--------LERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1160 TELEDTLDStAAQQELRAKREQEVTDLKKtIEEDVKVRDAQVTEMRQRHNQVVEEIsEQLEQARRFKGNLEKVKQTLESe 1239
Cdd:PRK02224 637 RELEAEFDE-ARIEEAREDKERAEEYLEQ-VEEKLDELREERDDLQAEIGAVENEL-EELEELRERREALENRVEALEA- 712
|
410
....*....|...
gi 1785379713 1240 ntdLIKEVKNLQA 1252
Cdd:PRK02224 713 ---LYDEAEELES 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1407-1893 |
6.21e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1407 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKkqkkfdQMLAEEKNISARYGEERDRAEAEAR 1486
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA------QIRGNGGDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1487 EKETKALSLSRALE----EAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQvqemktqIEELEDEL 1562
Cdd:COG4913 356 ERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE-------LRELEAEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1563 QAIEDGKLRLEVNMQAMKAQFERDLQNRD------------------------------------------------DSN 1594
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEALGLDEaelpfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvNRL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1595 DEKKKLLFkQVREMEVELEEERKQKSQILAAKkkleMDLQD------MESQMdsankGRD------EAVKQLKK------ 1656
Cdd:COG4913 509 HLRGRLVY-ERVRTGLPDPERPRLDPDSLAGK----LDFKPhpfrawLEAEL-----GRRfdyvcvDSPEELRRhprait 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1657 LQLQFKEVWReveeTRAARDEIFVQSR-----DNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLAD--ELSNGVS 1729
Cdd:COG4913 579 RAGQVKGNGT----RHEKDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1730 GKSALLDEKRALEMRISQleeeldeeqsntelINDRYRKLTL---QVETITTELsaersfsQKAENARQQMERQNKELKV 1806
Cdd:COG4913 655 EYSWDEIDVASAEREIAE--------------LEAELERLDAssdDLAALEEQL-------EELEAELEELEEELDELKG 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1807 KLNEMDStmrskykiTIASLEAKISQLEEQmeQESKERIIANKLVRRAEKRLKEVLLQvEEERRNADQFKEQLEKANIRM 1886
Cdd:COG4913 714 EIGRLEK--------ELEQAEEELDELQDR--LEAAEDLARLELRALLEERFAAALGD-AVERELRENLEERIDALRARL 782
|
....*..
gi 1785379713 1887 KQLKRQL 1893
Cdd:COG4913 783 NRAEEEL 789
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1007-1886 |
6.54e-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: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1007 ERKLLDDR--IGEFTSTMAEEEEKVKSLNKLrNKYEAVIADLEDRLkkeEKGRQEMEKMKRKLDGETTDLQDQLLELQQQ 1084
Cdd:TIGR01612 889 EKKFNDSKslINEINKSIEEEYQNINTLKKV-DEYIKICENTKESI---EKFHNKQNILKEILNKNIDTIKESNLIEKSY 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1085 IEELKQQLARKEEELQAAL--ARVDDEVGQKNNLLKQLRDLQSQLAELHEDL------ESEKAAR---AKAEKQRRDLGE 1153
Cdd:TIGR01612 965 KDKFDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfdEKEKATNdieQKIEDANKNIPN 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1154 ELEALKTELEDTLDstaaqqELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQR--HNQVVEEISEQleqARRFKGNLEK 1231
Cdd:TIGR01612 1045 IEIAIHTSIYNIID------EIEKEIGKNIELLNKEILEEAEINITNFNEIKEKlkHYNFDDFGKEE---NIKYADEINK 1115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1232 VKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES---EKVKfELAEKLQKLQAELDgvsgalgstEG 1308
Cdd:TIGR01612 1116 IKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKID---------KK 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1309 KSI--KLTKDLSTVqSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNlmenleeeesakaqlsrqlqalqqqllESKKR 1386
Cdd:TIGR01612 1186 KNIydEIKKLLNEI-AEIEKDKTSLEEVKGINLSYGKNLGKLFLEKID---------------------------EEKKK 1237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1387 MEDqggMVEAME-------EAKKKSYKELEFLQQRFDEKHQINdklekTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1459
Cdd:TIGR01612 1238 SEH---MIKAMEayiedldEIKEKSPEIENEMGIEMDIKAEME-----TFNISHDDDKDHHIISKKHDENISDIREKSLK 1309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1460 FDQMLAEEKNISarygEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQN-KQLRAEMDDLVSSKDDVGKNVH-EL 1537
Cdd:TIGR01612 1310 IIEDFSEESDIN----DIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKiKKIIDEVKEYTKEIEENNKNIKdEL 1385
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1538 ERSKRaLEQQVQEmKTQIEELEDELQAIEDGKLRLEV--NMQAMKAQFERDLQNRD------DSNDEKKKLLFKQVREME 1609
Cdd:TIGR01612 1386 DKSEK-LIKKIKD-DINLEECKSKIESTLDDKDIDECikKIKELKNHILSEESNIDtyfknaDENNENVLLLFKNIEMAD 1463
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1610 VELEEERKQKSQilAAKKKLEMDLQDMESQMDSANKGRDEA---VKQLKKLQLQFKEVWREVEE------TRAARDEIFV 1680
Cdd:TIGR01612 1464 NKSQHILKIKKD--NATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEllnkysALAIKNKFAK 1541
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1681 QSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALE------MRISQLEEELDE 1754
Cdd:TIGR01612 1542 TKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEnfenkfLKISDIKKKIND 1621
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1755 EQSNTELINDRYRklTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDStMRSKykitIASLEAKISQLE 1834
Cdd:TIGR01612 1622 CLKETESIEKKIS--SFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE-LDSE----IEKIEIDVDQHK 1694
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379713 1835 EQME----QESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFK-----EQLEKANIRM 1886
Cdd:TIGR01612 1695 KNYEigiiEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEgidpnEKLEEYNTEI 1755
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
867-1323 |
6.56e-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: 61.19 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 867 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEemrarlaskkqELEEILHDLEARVEEEEERTL 946
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS-----------ELKKQNNQLKDNIEKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 947 QLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKllDDRIGEFTSTMAEEE 1026
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1027 EKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARV 1106
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1107 DDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1186
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1187 KKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQtLESENTDLIKEVKNLQAA--KQDSEQRRKKL 1264
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK-LESEKKEKESKISDLEDElnKDDFELKKENL 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1265 EQQVSEFQIR-------TNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQ 1323
Cdd:TIGR04523 560 EKEIDEKNKEieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1089-1493 |
6.87e-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: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 KQQLARKEEELQAALARVDDEVGQkNNLLKQLRD---------------LQSQLAELHEDLESEKAARAKAEKQRRDLGE 1153
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQ-NSDCKQHIEvlkesltakeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1154 ELEALKTELEDTLDSTAAqqelrakREQEVTDLKKTIE---EDVKVRDAQVTEMRQRHNQVVEEISEQ------LEQARR 1224
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGLKERVKSLQTDSSNTdtalttLEEALS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1225 FKGN-LEKVKQTLESENTDLIKEVknlqaakQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGAL 1303
Cdd:pfam10174 447 EKERiIERLKEQREREDRERLEEL-------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1304 GSTEGKSIKLTKDLSTVQSQLQDTQELlQEETRQKLNFSSRVRQLEEEknnlmENLEEEESAKAQLSRQLQALQQQLLES 1383
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRIRLLEQE-----VARYKEESGKAQAEVERLLGILREVEN 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1384 KKRMEDQggMVEAMEEAKKKSYKELEFLQQRFDEKHQI-------------NDKLEKTRNRLQQELDDLMVDLDHQRQIV 1450
Cdd:pfam10174 594 EKNDKDK--KIAELESLTLRQMKEQNKKVANIKHGQQEmkkkgaqlleearRREDNLADNSQQLQLEELMGALEKTRQEL 671
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379713 1451 SNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKAL 1493
Cdd:pfam10174 672 DATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1113-1945 |
2.40e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1113 KNNLLKQLRDLQSQLAELHEdleSEKAARaKAEKQRRDLgEELEALKTELEDTLDSTAAQQELRAKREQEvtdlkkTIEE 1192
Cdd:COG4913 220 EPDTFEAADALVEHFDDLER---AHEALE-DAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLW------FAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1193 DVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLI----KEVKNLQAAKQDSEQRRKKLEQQV 1268
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeqleREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1269 SEFQIRTNESEKvkfELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQl 1348
Cdd:COG4913 369 AALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1349 eeeknnlmenleeeesakaqlsrqlqalqqqlleskkrmedqggMVEAMEEAKKKSYKEL----EFLQQRFDEkhqindk 1424
Cdd:COG4913 445 --------------------------------------------LRDALAEALGLDEAELpfvgELIEVRPEE------- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1425 lEKTRNRLQQELD----DLMVDLDHQRQIVSNLEkkQKKFDQMLaeeknisaRYGEERDRAEAEAREKETKAlSLSRale 1500
Cdd:COG4913 474 -ERWRGAIERVLGgfalTLLVPPEHYAAALRWVN--RLHLRGRL--------VYERVRTGLPDPERPRLDPD-SLAG--- 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1501 eaidlkdELDRQNKQLRAEMDDLVSSKDDVGK--NVHELERSKRALEQQVQemktqieeledelqaiedgklrlevnMQA 1578
Cdd:COG4913 539 -------KLDFKPHPFRAWLEAELGRRFDYVCvdSPEELRRHPRAITRAGQ--------------------------VKG 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1579 MKAQFERDLQNRDDS-------NDEKKKLLfkqvremeveleeeRKQKSQILAAKKKLEMDLQDMESQMDSANKgRDEAV 1651
Cdd:COG4913 586 NGTRHEKDDRRRIRSryvlgfdNRAKLAAL--------------EAELAELEEELAEAEERLEALEAELDALQE-RREAL 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1652 KQLKKLQLQFKEVW---REVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSngv 1728
Cdd:COG4913 651 QRLAEYSWDEIDVAsaeREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE--- 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1729 sgksALLDEKRALEMRISQLEEELDEEQsnTELINDRYRkltlqvetittELSAERSFSQKAENARQQMERQNKELKVKL 1808
Cdd:COG4913 724 ----QAEEELDELQDRLEAAEDLARLEL--RALLEERFA-----------AALGDAVERELRENLEERIDALRARLNRAE 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1809 NEMDSTMR---SKYKITIASLEAKISQLEEQMEQesKERIIANKLVRRaEKRLKEVLLQVEEERRN--ADQFKEQLEKAN 1883
Cdd:COG4913 787 EELERAMRafnREWPAETADLDADLESLPEYLAL--LDRLEEDGLPEY-EERFKELLNENSIEFVAdlLSKLRRAIREIK 863
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1884 IRMKQLKRQLEEAE---------EEASRANSNRRRLQRELEDVTESAESMNRE--------VTTLRSRLSKLERQQRKR 1945
Cdd:COG4913 864 ERIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEEEESDRR 942
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1096-1311 |
6.64e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1096 EEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtldstAAQQEL 1175
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------ERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1176 --RAKREQEVTDLKKTIE--------EDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIK 1245
Cdd:COG3883 89 geRARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1246 EVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSI 1311
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1687-1930 |
7.62e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1687 KKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELsngvsgksalldekRALEMRISQLEEELDEEQSNTELINDRY 1766
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--------------AALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1767 RKLTLQVETITTELSAERSFSQKAENARQQMERQNKeLKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQESKERII 1846
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1847 ANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKAnirMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNR 1926
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 1785379713 1927 EVTT 1930
Cdd:COG4942 242 RTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1642-1860 |
8.18e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1642 SANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLA 1721
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1722 DELSNGVSGKSALLDE----KRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQM 1797
Cdd:COG4942 97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 1798 ERQNKELKVKLNEMDSTMRSKyKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKE 1860
Cdd:COG4942 177 EALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
834-1476 |
9.71e-08 |
|
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: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 834 LKLRHWQWWRLFTKVKPLLQVTRQDEVMQAKVVELQkvkdTQVKTESELKEMANKYQQlfeeKSILAEQLQAETELFAEA 913
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELR----AQEAVLEETQERINRARK----AAPLAAHIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 914 EEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQleKVTTESRLKKMEED 993
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 994 ILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEE------KVKSLNKLRNKYEAVIADLEDRLKKEEKGRQ-EMEKMKRK 1066
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDlqgqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQS 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1067 LDGETTDLQDQLLELQQQIEELKQQLARKEE-----------ELQAALARVD-DEVGQKNNLLKQLRDLQSQLAELHEDL 1134
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVLARLLElqeepcplcgsCIHPNPARQDiDNPGPLTRRMQRGEQTYAQLETSEEDV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1135 ESEKAARakaEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEE 1214
Cdd:TIGR00618 548 YHQLTSE---RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1215 ISEQLEQA--RRFKGNLEKVKQTLESENTDLIKE--VKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQ 1290
Cdd:TIGR00618 625 QDLQDVRLhlQQCSQELALKLTALHALQLTLTQErvREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1291 KLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQklnfssRVRQLEEEKNNLMENLEEEESAKAQLS 1370
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVTAALQTGA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1371 RQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYkelEFLQQRFDEKHQINDKLEKTRNRLqQELDDLMVDLDHQRQiv 1450
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP---SDEDILNLQCETLVQEEEQFLSRL-EEKSATLGEITHQLL-- 852
|
650 660
....*....|....*....|....*.
gi 1785379713 1451 sNLEKKQKKFDQMLAEEKNISARYGE 1476
Cdd:TIGR00618 853 -KYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1090-1299 |
1.17e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1090 QQLARKEEELQAALARVDdevgqknnLLKQLRDLQSQLAELHEDLESEKAARAK-----AEKQRRDLGEELEALKTELED 1164
Cdd:COG4913 235 DDLERAHEALEDAREQIE--------LLEPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1165 TLDSTAAQQELRAKREQEVTDLKKTIEEDVkvrDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLI 1244
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNG---GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1785379713 1245 KEVKNLQAAKQDSEQRRKKLEQQVSEfqirtneSEKVKFELAEKLQKLQAELDGV 1299
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAE-------AEAALRDLRRELRELEAEIASL 431
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
853-1267 |
1.94e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 853 QVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAEtELFAEAEEMRARLASKKQELEEI-- 930
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLEELee 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 931 ----LHDLEARVEEEEERTLQLQNEKKK--------MHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLE 998
Cdd:COG4717 154 rleeLRELEEELEELEAELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 999 DQNAKLAKERKLLDDR--------IGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGE 1070
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1071 TTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLR------DLQSQLAELHEDLESEKAARAKA 1144
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1145 EKQRRDLGEELEALKTELEDTLDstAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEIsEQLEQARR 1224
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLG--ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-EQLEEDGE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379713 1225 FkGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQ 1267
Cdd:COG4717 471 L-AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
867-1251 |
1.95e-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: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 867 ELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLqaeTELFAEAEEMRARLASKKQELEEILHDLEARVEEEEertl 946
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL---TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 947 QLQNEKKKMHQHIQDLEEQLEEEegarqklqlekvttESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEE 1026
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQK--------------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1027 EKVKSLNKLRNKYEAVIADLEDRLKKEEkgrQEMEKMKRKLDGETTDLQDQLLELQQQIEELKqQLARKEEELQAALARV 1106
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKELEEKVK-DLTKKISSLKEKIEKL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1107 DDEVGQKNNllkQLRDLQSQLAELHEDLESEkaaraKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1186
Cdd:TIGR04523 530 ESEKKEKES---KISDLEDELNKDDFELKKE-----NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379713 1187 KKTIEEdvkvrdaqvtemrqrHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1251
Cdd:TIGR04523 602 IKEIEE---------------KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1097-1519 |
2.77e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1097 EELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLES--EKAARAKAEKQRRDLGEELEALKTELEDT---LDSTAA 1171
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1172 QQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1251
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1252 AAKQDsEQRRKKLEQQVSEFQIRTnesekVKFELAEKLQKLQAELDGVSGALGSTEG----KSIKLTKDLSTVQSQLQDT 1327
Cdd:COG4717 234 NELEA-AALEERLKEARLLLLIAA-----ALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1328 QELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESaKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKE 1407
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1408 LEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQrqivsNLEKKQKKFDQMLAEEKNISARYgeERDRAEAEARE 1487
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELEEELEELEEEL--EELREELAELE 459
|
410 420 430
....*....|....*....|....*....|..
gi 1785379713 1488 KETKALSLSRALEEAIDLKDELDRQNKQLRAE 1519
Cdd:COG4717 460 AELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1184-1890 |
2.85e-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: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1184 TDLKKTIEEDVKVRDAQVTEMRQRHNQVVEE---ISEQLEQARRFKGNLEKVKQTLE---SENTDLIKEVKNLQAAKQDS 1257
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQENrkiIEAQRKAIQELQFENEKVSLKLEeeiQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1258 EQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVS-GALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETR 1336
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1337 QklnFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEfLQQRFD 1416
Cdd:pfam05483 241 Q---VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS-TQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1417 EKHQIndkLEKTRNRLQQELDDLMVDLDHQRQ----IVSNLEKKQKKFDQMLAEEKNisaRYGEERDRAEAEAREKETKa 1492
Cdd:pfam05483 317 EDLQI---ATKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQ---RLEKNEDQLKIITMELQKK- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1493 lslSRALEEAIDLKDELDRQNKQLR---AEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGK 1569
Cdd:pfam05483 390 ---SSELEEMTKFKNNKEVELEELKkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1570 LRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEVELEEE---RKQKSQILAAKKKLEMDLQDMESQMDSANKG 1646
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlelKKHQEDIINCKKQEERMLKQIENLEEKEMNL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1647 RDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADElsn 1726
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK--- 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1727 gvsgKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKlTLQVETITTELSAERSFSQK--AENARQQMERQNKEL 1804
Cdd:pfam05483 624 ----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKLLEEVEKAKaiADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1805 KVKLNEMDSTM---RSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEK 1881
Cdd:pfam05483 699 QHKIAEMVALMekhKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
....*....
gi 1785379713 1882 ANIRMKQLK 1890
Cdd:pfam05483 779 NTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1481-1709 |
4.75e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1481 AEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELED 1560
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1561 ELQAIEDGKLRLEVNMQAMKAQ-FERDLQNRDDSNDEKKKL-LFKQVREMEVELEEERKQKSQILAAKKklemdlQDMES 1638
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQpPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRADLAELAALR------AELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379713 1639 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERA 1709
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
880-1470 |
5.48e-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: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 880 SELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHI 959
Cdd:TIGR04523 89 DKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 960 QDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEdqnaKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKY 1039
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1040 EAVIADLEDRLKKEekgRQEMEKMKRKLDGETtdlqdqllelqQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLkq 1119
Cdd:TIGR04523 245 TTEISNTQTQLNQL---KDEQNKIKKQLSEKQ-----------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1120 LRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELED-TLDSTAAQQELRAKrEQEVTDLKKTIEEDVKvrd 1198
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsESENSEKQRELEEK-QNEIEKLKKENQSYKQ--- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1199 aQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKvkqtLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNES 1278
Cdd:TIGR04523 385 -EIKNLESQINDLESKIQNQEKLNQQKDEQIKK----LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1279 EKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKnnlmen 1358
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK------ 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1359 leeeesakaqlsrQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDD 1438
Cdd:TIGR04523 534 -------------KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
570 580 590
....*....|....*....|....*....|....*.
gi 1785379713 1439 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNI 1470
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1018-1239 |
6.17e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1018 FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEE 1097
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1098 ELQAALARVDDevgQKNNLLKQLRDLQ--SQLAELHEDLESEKAARA--------KAEKQRRDLGEELEALKTELEDTLD 1167
Cdd:COG4942 91 EIAELRAELEA---QKEELAELLRALYrlGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1168 STAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESE 1239
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
986-1194 |
6.25e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 986 RLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKgrqemekmkr 1065
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1066 kldgettdlqdqllelqqqieelKQQLARKEEELQAALARVDdevgqknNLLKQLRDLQSQLAELHEDLESEKAARAKAE 1145
Cdd:COG1579 81 -----------------------QLGNVRNNKEYEALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1146 KQRRDLGEELEALKTELEDTLDSTAAQ-QELRAKREQevtdLKKTIEEDV 1194
Cdd:COG1579 131 AELAELEAELEEKKAELDEELAELEAElEELEAEREE----LAAKIPPEL 176
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1652-1984 |
6.45e-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: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1652 KQLKKLQLQfkevwreveeTRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGK 1731
Cdd:TIGR02168 200 RQLKSLERQ----------AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1732 SALLDEKRALEMRIsqleeeldeeqsntELINDRYRKLTLQVETITTELsaersfsQKAENARQQMERQNKELKVKLNEM 1811
Cdd:TIGR02168 270 EELRLEVSELEEEI--------------EELQKELYALANEISRLEQQK-------QILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1812 DStMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVllqveeerrnadqfKEQLEKANIRMKQLKR 1891
Cdd:TIGR02168 329 ES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--------------EEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1892 QLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKRAPIQFTTRTIRQVYQLEAVSDEEPES 1971
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330
....*....|...
gi 1785379713 1972 HSGEPSANHQQQQ 1984
Cdd:TIGR02168 474 EQALDAAERELAQ 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1492-1725 |
6.45e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1492 ALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLR 1571
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1572 LEVNMQAMKAQferdLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAV 1651
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1652 KQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELS 1725
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1224 |
6.62e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 999 DQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQL 1078
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1079 LELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEAL 1158
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1159 KTELEDTLdstAAQQELRAKREQEVTDLKKTIEEDvKVRDAQVTEMRQRHNQVVEEISEQLEQARR 1224
Cdd:COG4942 180 LAELEEER---AALEALKAERQKLLARLEKELAEL-AAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1396-1600 |
1.02e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1396 AMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA----EEKNIS 1471
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAelekEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1472 ARYGEERDR-------AEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRAL 1544
Cdd:COG4942 97 AELEAQKEElaellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1545 EQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKL 1600
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1507-1962 |
1.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1507 DELDRQNKQLRAEMDDLvsskddvgknvHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEVnmqamkAQFERD 1586
Cdd:COG4717 74 KELEEELKEAEEKEEEY-----------AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1587 LQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQD----MESQMDSANKGRDEAVKQLKKLQLQFK 1662
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1663 EVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDD-----LADELSNGVSGKSALLDE 1737
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvLFLVLGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1738 KRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVK--LNEMDSTM 1815
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1816 RSKYKITIASLEAKISQLEEQMEQESKeriianklVRRAEKRLKEVLLQVEEERRNADqfKEQLEKaniRMKQLKRQLEE 1895
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEE--------LEELEEQLEELLGELEELLEALD--EEELEE---ELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1896 AEEEASRANSNRRRLQRELEDVTESAE--SMNREVTTLRSRLSKLERQQRKRAPIQFTTRTIRQVYQLE 1962
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1476-1703 |
2.28e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1476 EERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQI 1555
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1556 EELEDELQAIEDGKLRLEvNMQAMKAQFERDLQNRDDSNDEKKKLL--FKQVREMEVELEEERKQKSQILAAKKKLEmdl 1633
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEEEKELVekIKELEKELEKAKKALEKNEKLKELRAELK--- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1634 qDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDL 1703
Cdd:COG1340 171 -ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1533-1948 |
3.00e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1533 NVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLEvnmqAMKAQFERDLQNRDDSNDEKKKL---------LFK 1603
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK----EKEKELEEVLREINEISSELPELreeleklekEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1604 QVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQlQFKEVWREVEETRAARDEIFVQSR 1683
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1684 DNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLadelsngvsgkSALLDEKRALEMRISQLEEELDEEqsnTELIN 1763
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----------KELEKRLEELEERHELYEEAKAKK---EELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1764 DRYRKLTLQVETITTELsaersfsQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKIS------QLEEQM 1837
Cdd:PRK03918 377 LKKRLTGLTPEKLEKEL-------EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrELTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1838 EQESKERIIANklVRRAEKRLKEVLLQVEEERRNADQFKEQLEKAN--IRMKQLKRQLEEAEEEASRANSNR-RRLQREL 1914
Cdd:PRK03918 450 RKELLEEYTAE--LKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEElEKKAEEY 527
|
410 420 430
....*....|....*....|....*....|....
gi 1785379713 1915 EDVTESAESMNREVTTLRSRLSKLERQQRKRAPI 1948
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
954-1715 |
3.80e-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: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 954 KMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLN 1033
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1034 KlRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgeTTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQK 1113
Cdd:TIGR00618 254 E-QLKKQQLLKQLRARIEELRAQEAVLEETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1114 NNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEAlkTELEDTLDSTAAQQELRAKREQEVTDLKKTIEED 1193
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ--HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1194 VKVRDAQVTEMR-QRHNQVVEEISEQLEQARrfkgnLEKVKQTLESENTDLIKEVKNLQAAKQdSEQRRKKLEQQVSEFQ 1272
Cdd:TIGR00618 409 QATIDTRTSAFRdLQGQLAHAKKQQELQQRY-----AELCAAAITCTAQCEKLEKIHLQESAQ-SLKEREQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1273 IRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEK 1352
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1353 NNLMENLEEEEsakaqlsrqlqalqqqlleskkrmedqggmveAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRL 1432
Cdd:TIGR00618 563 EQMQEIQQSFS--------------------------------ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1433 QQELDDLMVDLDHQrQIVSNLEKKQKKFDQMLAEEKNISARYGEERdraeaeAREKETKALSLSRALEEaidlkdeldRQ 1512
Cdd:TIGR00618 611 ACEQHALLRKLQPE-QDLQDVRLHLQQCSQELALKLTALHALQLTL------TQERVREHALSIRVLPK---------EL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1513 NKQLRAEMDDLVSSKDDVGKNVHELERSKRALeqqvQEMKTQIEELEDELQAIEdgklrlevnmQAMKAQfERDLQNRDD 1592
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIE----------NASSSL-GSDLAARED 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1593 SNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETR 1672
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1785379713 1673 AARDEIFVQSRDNEK-KLKSLEAELLQLQEDLAAAERAKRQAQQ 1715
Cdd:TIGR00618 820 NLQCETLVQEEEQFLsRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1637-1856 |
4.39e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1637 ESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIfvqsrdnEKKLKSLEAELLQLQEDLAAAERAKRQAQQE 1716
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL-------QAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1717 RDDLADEL---SNGVSGKSALLDEKRALEMrisqleeelDEEQSNTELINDRYRKLTLQVETITTELSAERSfsqKAENA 1793
Cdd:COG3883 88 LGERARALyrsGGSVSYLDVLLGSESFSDF---------LDRLSALSKIADADADLLEELKADKAELEAKKA---ELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 1794 RQQMERQNKELKVKLNEMDSTmRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEK 1856
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQ-QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1089-1293 |
4.94e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 KQQLARKEEELQAALAR--VDDEVGQKNNLLKQLRDLQSQLAELhedleseKAARAKAEKQRRDLGEELEALKTELEDTL 1166
Cdd:COG3206 188 RKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEA-------RAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1167 DSTAAQQELRAKREQEvtdlkktieedvkvrdAQVTEMRQR----HNQVVeEISEQLEQARR-FKGNLEKVKQTLESENT 1241
Cdd:COG3206 261 QSPVIQQLRAQLAELE----------------AELAELSARytpnHPDVI-ALRAQIAALRAqLQQEAQRILASLEAELE 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1242 DLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQ 1293
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1117-1297 |
7.06e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1117 LKQLRDLQ---SQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTldstaaqQELRAKREQEVTDLKKTIEED 1193
Cdd:COG1579 6 LRALLDLQeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1194 vKVRDAQVTEMRQrhnqvVEEISEQLEQarrfkgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQV----S 1269
Cdd:COG1579 79 -EEQLGNVRNNKE-----YEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeekkA 145
|
170 180
....*....|....*....|....*...
gi 1785379713 1270 EFQIRTNESEKVKFELAEKLQKLQAELD 1297
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIP 173
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1098-1270 |
7.46e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1098 ELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKT---ELEDTLDSTAAQQE 1174
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1175 LRAkREQEVTDLKKTIEEdvkvrdaqvteMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAK 1254
Cdd:COG1579 91 YEA-LQKEIESLKRRISD-----------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|....*.
gi 1785379713 1255 QDSEQRRKKLEQQVSE 1270
Cdd:COG1579 159 EELEAEREELAAKIPP 174
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1397-1940 |
1.09e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1397 MEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNL---EKKQKKFDQMLAE-EKNISA 1472
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELsslEDMKNRYESEIKTaESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1473 RYGEERDRAEAEAREKETKALSLSRALEEAID-LKDELDRQN-KQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQE 1550
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDyFKYKNDIENkKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1551 MKtQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREmeveleeerkqKSQILAAKKKLE 1630
Cdd:PRK01156 348 YD-DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEID-----------PDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1631 MDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWRE----VEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAA 1706
Cdd:PRK01156 416 VKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1707 ERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTL----QVETITTELSA 1782
Cdd:PRK01156 496 DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLedldSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1783 ERSfSQKAENARQQMERQNKELK---VKLNEMDSTM---RSKYKITIASLEAKISQLEEQMeQESKERIIANKLVRRAEK 1856
Cdd:PRK01156 576 VIS-LIDIETNRSRSNEIKKQLNdleSRLQEIEIGFpddKSYIDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKID 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1857 RLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLeeaeeeaSRANSNRRRLQRELEDVTESAESMNREVTTLRSRLS 1936
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKAL-------DDAKANRARLESTIEILRTRINELSDRINDINETLE 726
|
....
gi 1785379713 1937 KLER 1940
Cdd:PRK01156 727 SMKK 730
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
852-1224 |
1.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 852 LQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQEL---- 927
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 928 EEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDIL------------ 995
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggslls 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 996 --------------LLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYE-------AVIADLEDRLKKEE 1054
Cdd:COG4717 271 liltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdlspEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1055 KGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQ-----QLARKEEELQAALARVDDEVGQKNNLLKQLRDlQSQLAE 1129
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLE-ALDEEE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1130 LHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAqQELRAKREQEVTDLKKTIEEDVKVRDAQvtemrqrhn 1209
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL-AELLQELEELKAELRELAEEWAALKLAL--------- 499
|
410
....*....|....*
gi 1785379713 1210 QVVEEISEQLEQARR 1224
Cdd:COG4717 500 ELLEEAREEYREERL 514
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1434-1956 |
1.40e-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: 50.61 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1434 QELDDLMVDLDHQRQIVSN---LEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELd 1510
Cdd:pfam12128 221 QQVEHWIRDIQAIAGIMKIrpeFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1511 rqnKQLRAEMD-DLVSSKDDVGKNVHELER-------------SKRALEQ-QVQEMKTQIEELEDELQAIEDGKLRLEVN 1575
Cdd:pfam12128 300 ---KEKRDELNgELSAADAAVAKDRSELEAledqhgafldadiETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1576 MQAMKAQfeRDLQNRDDSNDEKKKLlfkqvremEVELEEERKQKSQILAAKKKLEMDLQD-MESQMDSANKGRDEAVKQL 1654
Cdd:pfam12128 377 YNRRRSK--IKEQNNRDIAGIKDKL--------AKIREARDRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1655 KKLQLQ-------------------------------FKEVWR---EVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQ 1700
Cdd:pfam12128 447 GELKLRlnqatatpelllqlenfderierareeqeaaNAEVERlqsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1701 EDLAAA-----ERAKRQAQQERDDLADELS-------------NGVSGKSAL------LDEKR-----------ALEMRI 1745
Cdd:pfam12128 527 LQLFPQagtllHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpewaaseeELRERL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1746 SQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIAS 1825
Cdd:pfam12128 607 DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1826 LEAKISQLEEQMeQESKERIIANKLVRRAEKrlKEVLLQVEEERRNA-DQFKEQLEKANI----RMKQLKRQLEEAEEEA 1900
Cdd:pfam12128 687 LEAQLKQLDKKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALDAQlALLKAAIAARRSgakaELKALETWYKRDLASL 763
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1901 SRANSNRRRLQRELEDVTESAESMNREvttlRSRLSKLERQQRKRAPIQFTTRTIR 1956
Cdd:pfam12128 764 GVDPDVIAKLKREIRTLERKIERIAVR----RQEVLRYFDWYQETWLQRRPRLATQ 815
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1107-1967 |
1.41e-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: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1107 DDEVGQKNNLLKqlRDLQSQLAELHEDLESEKAARAKAEKQRRDLgEELEALKTELEDTLDSTAAQQELRAKREQEVTDL 1186
Cdd:pfam12128 208 DDGVVPPKSRLN--RQQVEHWIRDIQAIAGIMKIRPEFTKLQQEF-NTLESAELRLSHLHFGYKSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1187 KKTIEEDVKVRDAQVTEMRQRHNQvveEISEQLEQARRFKGNLEKVkqtlesentdlikEVKNLQAAKQDSEQRRKKLEQ 1266
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDELNG---ELSAADAAVAKDRSELEAL-------------EDQHGAFLDADIETAAADQEQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1267 QVSeFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRvR 1346
Cdd:pfam12128 349 LPS-WQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR-E 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1347 QLEEEKNNLMENLEEEESAkAQLSRQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQ-------RFDEKH 1419
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSR-LGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSelrqarkRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1420 QINDKLEKTRNRLQQELDDLMVDLDHQR-QIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRA 1498
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1499 LEEAIDLKDELDrQNKQLRAEMDDLVSSKDDvgknvhELERSKRALEQQVQ---EMKTQIEELEDELQAIEDGKL---RL 1572
Cdd:pfam12128 586 DLKRIDVPEWAA-SEEELRERLDKAEEALQS------AREKQAAAEEQLVQangELEKASREETFARTALKNARLdlrRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1573 EVNMQAMKAQFERDLQNRDDS--------NDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSAN 1644
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDSanerlnslEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1645 KGRDEAVK-QLKKLQlqfkeVWREVEETRAARDEIFVQSRdnEKKLKSLEAELLQLQEDLAAAERAKRQAQ----QERDD 1719
Cdd:pfam12128 739 AARRSGAKaELKALE-----TWYKRDLASLGVDPDVIAKL--KREIRTLERKIERIAVRRQEVLRYFDWYQetwlQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1720 LADELSNgvsgksallDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVEtITTELSAERSFSQKAenARQQMER 1799
Cdd:pfam12128 812 LATQLSN---------IERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVR-LSENLRGLRCEMSKL--ATLKEDA 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1800 QNKELKVKLNEMD---STMRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFK 1876
Cdd:pfam12128 880 NSEQAQGSIGERLaqlEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1877 EQLekANIRMKQLKRQLEEAEEEASRANSNrrrLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKRAPIQFTTRTIR 1956
Cdd:pfam12128 960 EQW--FDVRVPQSIMVLREQVSILGVDLTE---FYDVLADFDRRIASFSRELQREVGEEAFFEGVSESAVRIRSKVSELE 1034
|
890
....*....|.
gi 1785379713 1957 QVYQLEAVSDE 1967
Cdd:pfam12128 1035 YWPELRVFVKA 1045
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1026-1274 |
1.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1026 EEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLdgettdlqdQLLELQQQIEELKQQLARKEEELQAALAR 1105
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL---------QRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1106 VDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTD 1185
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1186 LKKTIEEDVKVRDAQVTEMRQRHNQVVEEISEQLEQA-RRFKGNLEKVKQTLESeNTDLIKEVKNLQAakQDSEQRRKKL 1264
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLES-LPEYLALLDRLEE--DGLPEYEERF 836
|
250
....*....|
gi 1785379713 1265 EQQVSEFQIR 1274
Cdd:COG4913 837 KELLNENSIE 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1284-1496 |
1.61e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1284 ELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEE 1363
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1364 SAKAQLSRQLQALQQQL-----------LESKKRMEDQGGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRL 1432
Cdd:COG4942 104 EELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1433 QQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLS 1496
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1407-1582 |
1.68e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1407 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE-EKNISARYGEERDRAEAEA 1485
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1486 REKET------------------KALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQ 1547
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1785379713 1548 VQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQ 1582
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
664-688 |
1.84e-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: 1.84e-05
10 20
....*....|....*....|....*
gi 1785379713 664 YKESLSKLMSTLRNTNPNFVRCIIP 688
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
947-1172 |
2.34e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 947 QLQNEKKKMHQHIQDLEEqleeeegARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTstmAEEE 1026
Cdd:COG4942 24 EAEAELEQLQQEIAELEK-------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE---KEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1027 EKVKSLNKLRNKYEAVIADLEDRLKKEE-------KGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEEL 1099
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 1100 QAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQ 1172
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
986-1574 |
2.65e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 986 RLKKMEEDILLLEDQNAKL-----AKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLkkEEKGRQEM 1060
Cdd:COG4913 263 RYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1061 EKMKRKLDGETtdlqdqllelqQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLEsekAA 1140
Cdd:COG4913 341 EQLEREIERLE-----------RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1141 RAKAEKQRRDLGEELEALKTELEdtldstaaqqELRAKR---EQEVTDLKKTIEEDVKVRDAQVtemrqrhnQVVEEISE 1217
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEAEL--------PFVGELIE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1218 QLEQARRFKGNLEKVkqtLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFE---LAEKLQ---- 1290
Cdd:COG4913 469 VRPEEERWRGAIERV---LGGFALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdsLAGKLDfkph 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1291 KLQAELDGVSGALG-----------STEGKSIK---LTKDLSTVQsQLQDTQELLQE-----ETRQKLN-FSSRVRQLEE 1350
Cdd:COG4913 546 PFRAWLEAELGRRFdyvcvdspeelRRHPRAITragQVKGNGTRH-EKDDRRRIRSRyvlgfDNRAKLAaLEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1351 EKNNLMENLEEEESAKAQLSRQLQALQQQLLES---------KKRMEDQGGMVEAMEEAK---KKSYKELEFLQQRFDEK 1418
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSddlAALEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1419 HQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKK-----FDQMLAE------EKNISARYGEERDRAEAEARE 1487
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAalgdavERELRENLEERIDALRARLNR 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1488 KETK---------------ALSLSRALEEAIDLKDELDRQNK----QLRAEMDDLVSSkddvgKNVHELERSKRALEQQV 1548
Cdd:COG4913 785 AEEEleramrafnrewpaeTADLDADLESLPEYLALLDRLEEdglpEYEERFKELLNE-----NSIEFVADLLSKLRRAI 859
|
650 660
....*....|....*....|....*....
gi 1785379713 1549 QEMKTQIEELEDELQAIE---DGKLRLEV 1574
Cdd:COG4913 860 REIKERIDPLNDSLKRIPfgpGRYLRLEA 888
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1423-1603 |
3.01e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1423 DKLEKTRNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAR 1486
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1487 EKETKALSLSRALEEAIDLKDELDRQNK---------------QLRAEMDDLVSSKDDVGKNV-HELERSKRALEQ---- 1546
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctQQISEGPDRITKIKDKLKELqHSLEKLDTAIDEleei 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785379713 1547 ---------QVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFK 1603
Cdd:PHA02562 329 mdefneqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1088-1308 |
4.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1088 LKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLesekAARAKAEKQRRDLGEELEALK--TELEDT 1165
Cdd:COG3883 42 LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GERARALYRSGGSVSYLDVLLgsESFSDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1166 LDSTAAQQELRAKREQEVTDLKKTIEEdvkVRDAQvtemrqrhnqvvEEISEQLEQARRFKGNLEKVKQTLESENTDLIK 1245
Cdd:COG3883 118 LDRLSALSKIADADADLLEELKADKAE---LEAKK------------AELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 1246 EVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEG 1308
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
853-1289 |
4.49e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 853 QVTRQDEVMQAKVVELQKVKDTQVKTESElKEMANKYQQLFEEKSI---------------LAEQLQAETELFAEAEEMR 917
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLEST-KEMLRKVVEELTAKKMtlessertvsdltasLQEKERAIEATNAEITKLR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 918 ARLASKKQELEEILHDLE-ARVEEEEERTLQLQNEKKK-----MHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKME 991
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDhLRNVQTECEALKLQMAEKDkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 992 edillLEDQNAKLAKERKllDDRIGEFTSTMAE-EEEKVKSLNKLRNKYEAViadledrlkkeekgrQEMEKMKRKLDGE 1070
Cdd:pfam15921 604 -----LELQEFKILKDKK--DAKIRELEARVSDlELEKVKLVNAGSERLRAV---------------KDIKQERDQLLNE 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1071 TTDLQDQLLELQQQIEELKQQLARKEEELQAAlarvddevgqKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQrrd 1150
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETT----------TNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV--- 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1151 lgeelealkteledtldSTAAQQELRAKREQeVTDLKKTI---EEDVKVRDAQVTEMRQRHNQVVEEISEQLEQARRFKG 1227
Cdd:pfam15921 729 -----------------AMGMQKQITAKRGQ-IDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1228 NLEkvkqTLESENTDLIKEVKNLQAAKQdseqrrkKLEQQVSEFQ--IRTNESEKVKFELAEKL 1289
Cdd:pfam15921 791 ELE----VLRSQERRLKEKVANMEVALD-------KASLQFAECQdiIQRQEQESVRLKLQHTL 843
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
771-1132 |
4.57e-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: 48.90 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 771 GQSKIFFRAGVLAHLEEERDLKITDIIVFFQAAARgylARRAFYKKQQQMSALKVVQRNCAAYLKLRHWQWWRLFTKVKP 850
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 851 LLQ-VTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEE 929
Cdd:TIGR02168 745 LEErIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 930 ILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERK 1009
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1010 LLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKkeEKGRQEMEKMKRKldgettdlqdqLLELQQQIEELK 1089
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEYSLTLEEAEAL-----------ENKIEDDEEEAR 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1090 QQLARKEEELQ-------AALARVDDEVGQKNNLLKQLRDLQSQLAELHE 1132
Cdd:TIGR02168 972 RRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1043-1229 |
4.68e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1043 IADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQlRD 1122
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1123 LQSQLAELhedlESEKAARAKAEKQRRDLGEELEALKTELEDTldstaaqQELRAKREQEVTDLKKTIEEDVKVRDAQVT 1202
Cdd:COG1579 91 YEALQKEI----ESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180 190
....*....|....*....|....*....|.
gi 1785379713 1203 EMRQRHNQVVEEISEQL----EQARRFKGNL 1229
Cdd:COG1579 160 ELEAEREELAAKIPPELlalyERIRKRKNGL 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1124-1344 |
4.83e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1124 QSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVkvrdaqvte 1203
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1204 mrqrhnqvvEEISEQLEQARRFKGNLEKVKQTLESEN-TDLIKEVKNLQA-AKQDSE------QRRKKLEQQVSEFQIRT 1275
Cdd:COG3883 86 ---------EELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKiADADADlleelkADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1276 NESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSR 1344
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
903-1195 |
5.85e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 903 LQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVT 982
Cdd:PLN02939 102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 983 TESRLKKMEE---DILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLN-KLRNKYEAV------IADLEDRLKK 1052
Cdd:PLN02939 182 TDARIKLAAQekiHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENmLLKDDIQFLkaelieVAETEERVFK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1053 EEKGRQEMEKMKRKLDgetTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHE 1132
Cdd:PLN02939 262 LEKERSLLDASLRELE---SKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEA 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1133 DLESEKAARAKAEKQRRdLGEELEALKTELEDTLDSTAAQQELRAKREQEVTD-LKKTIEEDVK 1195
Cdd:PLN02939 339 SLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDtLSKLKEESKK 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1681-1915 |
8.22e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1681 QSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERD--DLADELSNGVSGKSALLDEKRALEMRISQleeeldeeqsn 1758
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE----------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1759 telINDRYRKLTLQVETITTELSAersfsQKAENARQQMERQNKELKVKLNEMDSTMRSKYkITIASLEAKISQLEEQME 1838
Cdd:COG3206 238 ---AEARLAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEAELAELSARYTPNH-PDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379713 1839 QESKERIIAnklvrrAEKRLKEVLLQVEEERRNADQFKEQLEKANirmkQLKRQLeeaeeeasransnrRRLQRELE 1915
Cdd:COG3206 309 QEAQRILAS------LEAELEALQAREASLQAQLAQLEARLAELP----ELEAEL--------------RRLEREVE 361
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1394-1967 |
9.88e-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: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1394 VEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNlEKKQKKFDQMLAEEKNISAR 1473
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR-EKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1474 YGEERDRAEAEAREKEtkaLSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVG--KNVHELERskralEQQVQEM 1551
Cdd:TIGR00606 336 RLLNQEKTELLVEQGR---LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVI-----ERQEDEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1552 KTqIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNrddsndEKKKLLFKQVREMEVELEEERKQKSqilaAKKKLEM 1631
Cdd:TIGR00606 408 KT-AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL------KKEILEKKQEELKFVIKELQQLEGS----SDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1632 DLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEaelLQLQEDLAAAERAKR 1711
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME---MLTKDKMDKDEQIRK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1712 QAQQERDDLADELSNGVSGK------SALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITT---ELSA 1782
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfDVCG 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1783 ERSFSQKAENARQQMERQNKELKVklnemdstmrskykitIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVL 1862
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAM----------------LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFI 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1863 LQVEEERRNADQFKEQLEKaniRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQ- 1941
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTES---ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLl 774
|
570 580 590
....*....|....*....|....*....|.
gi 1785379713 1942 -----QRKRAPIQFTTRTIRQVYQLEAVSDE 1967
Cdd:TIGR00606 775 gtimpEEESAKVCLTDVTIMERFQMELKDVE 805
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1549-1942 |
1.06e-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: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1549 QEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDD--SNDEKKKLLFKQVREMEVELEEERKQKSQILAAK 1626
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1627 KKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEvwreveetraardeifvqsrdNEKKLKSLEAELLQLQEDLaaa 1706
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ---------------------NNKKIKELEKQLNQLKSEI--- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1707 ERAKRQAQQERD-DLADELSNgvsgksaLLDEKRALEMRISQleeeldeeqsNTELINdryrKLTLQVETITTELSAERS 1785
Cdd:TIGR04523 298 SDLNNQKEQDWNkELKSELKN-------QEKKLEEIQNQISQ----------NNKIIS----QLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1786 FSQKAENarqQMERQNKELKVKLNEMDSTMRSKYKIT--IASLEAKIS---QLEEQMEQESKERIIANKLVRRAEKRLKE 1860
Cdd:TIGR04523 357 ENSEKQR---ELEEKQNEIEKLKKENQSYKQEIKNLEsqINDLESKIQnqeKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1861 VLLQVEEERRNAD----QFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLS 1936
Cdd:TIGR04523 434 TIIKNNSEIKDLTnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
....*.
gi 1785379713 1937 KLERQQ 1942
Cdd:TIGR04523 514 DLTKKI 519
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
974-1316 |
1.07e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.54 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 974 QKLQLEKVTTESRLKKMEEDILLledqnaklaKERKLLDDRIGEFTSTMAEEEEKVKSLnKLRNKYEAVIADLEDRLKK- 1052
Cdd:PLN03229 372 QQIKIAINENMDELGKMDTEELL---------KHRMLKFRKIGGFQEGVPVDPERKVNM-KKREAVKTPVRELEGEVEKl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1053 ---------------EEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEEL-----------------KQQLARKEEELQ 1100
Cdd:PLN03229 442 keqilkakessskpsELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLReefskansqdqlmhpvlMEKIEKLKDEFN 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1101 AALARVDDEVGQKNNLlKQLRDLQ-----SQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAqqEL 1175
Cdd:PLN03229 522 KRLSRAPNYLSLKYKL-DMLNEFSrakalSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEALKAEVASSGASSGD--EL 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1176 RAKREQEVTDLKKTIEEDV----KVRDAQVTEMRQRHNQVVEEISEQleqarRFKGNLEKVKQTLESENTDLIK--EVKN 1249
Cdd:PLN03229 599 DDDLKEKVEKMKKEIELELagvlKSMGLEVIGVTKKNKDTAEQTPPP-----NLQEKIESLNEEINKKIERVIRssDLKS 673
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1250 ------LQAAK------QDSEQRRKKLEQQVSEfQIRTNESEKvkfELAEKLQKLQAELdgvSGALGSTEGKSIKLTKD 1316
Cdd:PLN03229 674 kiellkLEVAKasktpdVTEKEKIEALEQQIKQ-KIAEALNSS---ELKEKFEELEAEL---AAARETAAESNGSLKND 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
873-1070 |
1.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 873 DTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEK 952
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 953 KKMHQHIQDLEEQLEEE---------------EGARQKLQLEKVTTESRLKKMEEdillLEDQNAKLAKERKLLDDRIGE 1017
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 1018 FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGE 1070
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1633-1869 |
1.20e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1633 LQDMESQMdsANKGRDEAVKQLKKLQLQFKEVWREVE----------ETRAARDEIFVQSRDNEKKLKSLEAELLQLQED 1702
Cdd:PRK02224 189 LDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIEryeeqreqarETRDEADEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1703 LAAAERakrqaqqERDDLADElsngVSGKSALLDEkraLEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSA 1782
Cdd:PRK02224 267 IAETER-------EREELAEE----VRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1783 ER----SFSQKAENARQ---QMERQNKELKVKLNEMDSTMRSKyKITIASLEAKISQLEEQMEQESKERIIANKLVRRAE 1855
Cdd:PRK02224 333 CRvaaqAHNEEAESLREdadDLEERAEELREEAAELESELEEA-REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250
....*....|....
gi 1785379713 1856 KRLKEVLLQVEEER 1869
Cdd:PRK02224 412 DFLEELREERDELR 425
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1502-1745 |
1.41e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1502 AIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDgklRLEVNMQAMKA 1581
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1582 QFeRDLQNRDDSNDekkkllfkqvremeveleeerkQKSQILAAKkklemDLQDMESQMDsankgrdeAVKQLKKLQLQf 1661
Cdd:COG3883 91 RA-RALYRSGGSVS----------------------YLDVLLGSE-----SFSDFLDRLS--------ALSKIADADAD- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1662 kevwrEVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRAL 1741
Cdd:COG3883 134 -----LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
....
gi 1785379713 1742 EMRI 1745
Cdd:COG3883 209 EAAA 212
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
891-1267 |
1.88e-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: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 891 QLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEE 970
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 971 GARQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNklrnkyeaviADLEDRL 1050
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ----------AKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1051 KKEEKGRQEMEKMKRKLDGETTDLqdqllelqqqieelkQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAE- 1129
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQV---------------LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAs 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1130 ------LHEDLESEKAARAKAEKQRRDLGEELEALKTELEdtlDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTE 1203
Cdd:pfam07888 250 erkvegLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA---DASLALREGRARWAQERETLQQSAEADKDRIEKLSAE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1204 MRQRHNQVVEEISE----QLEQARRFKGNLEKVKQT------LESENTDLIKEVKNLQAAKQDSEQRRKKLEQQ 1267
Cdd:pfam07888 327 LQRLEERLQEERMEreklEVELGREKDCNRVQLSESrrelqeLKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1480-1844 |
2.18e-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: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1480 RAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELE 1559
Cdd:pfam07888 56 QREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1560 DELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVremeveleeerkqksQILAAKKKLEMDLQDMESQ 1639
Cdd:pfam07888 136 EDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ---------------QTEEELRSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1640 MDSankgRDEAVKQLK----KLQLQFKEVWREVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLA--AAERAKRQA 1713
Cdd:pfam07888 201 LAQ----RDTQVLQLQdtitTLTQKLTTAHRKEAENEALLEEL----RSLQERLNASERKVEGLGEELSsmAAQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1714 QQERDDL-ADELSNGVSGKSALLDEKRAlemrisQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAE- 1791
Cdd:pfam07888 273 ELHQARLqAAQLTLQLADASLALREGRA------RWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEv 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1792 ---NARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAK------ISQLEEQMEQESKER 1844
Cdd:pfam07888 347 elgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKqelleyIRQLEQRLETVADAK 408
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1639-1972 |
2.19e-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: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1639 QMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARD-EIFVQSR---DNEKKLKSLEAELLQLQEDlaaaERAKRQAQ 1714
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1715 QERDDLADELSNGVSGKSALLDEKRALEmRISQLEEELDEEQSNTElinDRYRKLTLQVETITtELSAERSFSQKAENAR 1794
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1795 QQMERQNKELKVKLNEMDstmRSKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRA-EKRLKEVLLQ-VEEERRNA 1872
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1873 DQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESA---ESMNREVTTLRSRLSKLERQQRKRAPIQ 1949
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMMRQIVESEKARAEYEATTP 596
|
330 340
....*....|....*....|....*
gi 1785379713 1950 FTtrTIRQVYQLEAVSDEEP--ESH 1972
Cdd:pfam17380 597 IT--TIKPIYRPRISEYQPPdvESH 619
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
847-1285 |
2.45e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 847 KVKPLLQVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLQAETELFAEAEEMRarlasKKQE 926
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 927 leeilhdlearveeeeertlqlqnEKKKMHQhiqdleeqleeeegaRQKLQLEKVTTESRLKKMEEDILLLEDQNAKLAK 1006
Cdd:PTZ00121 1631 ------------------------EKKKVEQ---------------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1007 ERKLLDDRIGEftstmAEEEEKVKslnklrnkyeaviadlEDRLKKEEKGRQEMEKMKRKlDGETTDLQDQLLELQQQIE 1086
Cdd:PTZ00121 1672 EDKKKAEEAKK-----AEEDEKKA----------------AEALKKEAEEAKKAEELKKK-EAEEKKKAEELKKAEEENK 1729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1087 ELKQQLARKEEELQAALARVDDEVGQKNnllkQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTeLEDTL 1166
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIF 1804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1167 DSTAAQQELRAKREQEVTDLKKTieedvkvRDAQVTEMRQRHNQVVEEiSEQLEQARRFKGNLEKVKQTLES----ENTD 1242
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEM-------EDSAIKEVADSKNMQLEE-ADAFEKHKFNKNNENGEDGNKEAdfnkEKDL 1876
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1785379713 1243 LIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFEL 1285
Cdd:PTZ00121 1877 KEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKL 1919
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1299-1519 |
2.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1299 VSGALGSTEGKSIKLTKDLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQ 1378
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1379 QLLESKKRMEDQ----GGMVEAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLE 1454
Cdd:COG4942 91 EIAELRAELEAQkeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785379713 1455 KKQKKFDQMLAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAE 1519
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1122-1926 |
4.21e-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: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1122 DLQSQLAELHEDLESEKAARAKAEKQRRDLGE---ELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1198
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1199 AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEV--KNLQAAKQDSEQRRKKLEQQVSEFQIRTN 1276
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1277 ESEKVKFELAEKLQKLQAELDGVsgalgstEGKSIKLTKDLSTVQSQLQDTQELLqEETRQKLNFSSRVRQLEEEKNnlm 1356
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQ-------EDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEIL--- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1357 enleeeeSAKAQLSRQLQALQQQLLESKKRMEDqggmveaMEEAKKKSYKELEFLqqrfdEKHQINDKLEKTRNRLQQEL 1436
Cdd:TIGR00606 450 -------EKKQEELKFVIKELQQLEGSSDRILE-------LDQELRKAERELSKA-----EKNSLTETLKKEVKSLQNEK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1437 DDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYGEERDRAEAEAREketkALSLSRALEEAIDLKDELDRQNKQL 1516
Cdd:TIGR00606 511 ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE----LTSLLGYFPNKKQLEDWLHSKSKEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1517 RAEMDDLVsskdDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIeDGKLRLEVNMQAMKAQFERdlQNRDDSNDE 1596
Cdd:TIGR00606 587 NQTRDRLA----KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEK--SSKQRAMLA 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1597 KKKLLFKQVREMEVELEEERKQKSQ-ILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAAR 1675
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1676 DEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQErDDLADELSNGVSGKSALLDEKRALEMRISQleeeldee 1755
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQ-------- 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1756 qsntelindryrkltlqvetittelsaersfsQKAENARQQMERQNKELKVKLNEMDSTMRskykitiasleaKISQLEE 1835
Cdd:TIGR00606 811 --------------------------------QAAKLQGSDLDRTVQQVNQEKQEKQHELD------------TVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1836 QMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELE 1915
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810
....*....|.
gi 1785379713 1916 DVTESAESMNR 1926
Cdd:TIGR00606 927 ELISSKETSNK 937
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1111-1893 |
4.68e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1111 GQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTI 1190
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1191 EEDVKvrdaqvtEMRQRHNQVVEEISEQLEQARRFKgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSE 1270
Cdd:TIGR00618 232 REALQ-------QTQQSHAYLTQKREAQEEQLKKQQ--LLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1271 FQIRtNESEKVKFELAEKLQKLQAELDGVSGALgSTEGKSIKLTKDLSTVQSQ------LQDTQELLQEETRQKLNFSSR 1344
Cdd:TIGR00618 303 TQIE-QQAQRIHTELQSKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQeihirdAHEVATSIREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1345 VRQLEEEKNNLMENLEeeeSAKAQLSRQLQALQQQLLESKKRMEDQGGMVEAmEEAKKKSYKELEFLQQRFDEKHQIndk 1424
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQ---SLCKELDILQREQATIDTRTSAFRDLQGQLAHA-KKQQELQQRYAELCAAAITCTAQC--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1425 lEKTRNRLQQELddlmvdldhqrqivsnlEKKQKKFDQMLAEEKNISARygeerdraeaearEKETKALSLSRALEEAiD 1504
Cdd:TIGR00618 454 -EKLEKIHLQES-----------------AQSLKEREQQLQTKEQIHLQ-------------ETRKKAVVLARLLELQ-E 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1505 LKDELDRQNKQLRAEMDDLvsskDDVGKNVHELERskraLEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFE 1584
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDI----DNPGPLTRRMQR----GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1585 RDLQNRDDSNDEKKKLLfKQVREMEVELEEERKQKSQILAAKKKLEMDLQDmesqmdSANKGRDEAVKQLKKLQLQFKEV 1664
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQP------EQDLQDVRLHLQQCSQELALKLT 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1665 WREVEETRAARDEIfvqsRDNEKKLKSLEAELLQL-QEDLAAAERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEM 1743
Cdd:TIGR00618 647 ALHALQLTLTQERV----REHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1744 RISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMrskykiti 1823
Cdd:TIGR00618 723 IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-------- 794
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1824 ASLEAKISQLEEQMEQESKERiianklvrraekrLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQL 1893
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSD-------------EDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1006-1351 |
4.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1006 KERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDgettdlqdqLLELQQQI 1085
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---------LLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1086 EELKQQLARKEEELQAALARVDdevgQKNNLLKQLRDLQSQLAELHEDLESEKA-ARAKAEKQRRDLGEELEALKTELED 1164
Cdd:COG4717 135 EALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1165 TLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQ-------------------------------------------V 1201
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallallglggsllsliltiagvlflvlgllallF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1202 TEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLE----------SENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEF 1271
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAalglppdlspEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1272 QIR--------TNESE-KVKFELAEKLQKLQAELDGVSGALGSTEGKSIKL--TKDLSTVQSQLQDTQELLQEETRQKLN 1340
Cdd:COG4717 371 EIAallaeagvEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEE 450
|
410
....*....|.
gi 1785379713 1341 FSSRVRQLEEE 1351
Cdd:COG4717 451 LREELAELEAE 461
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1780-1891 |
5.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1780 LSAERSFSQKAENARQQMERQNKELKVKLNEMDSTMRSKYKITIASLEAKISQLEEQMEQesKERIIANKL--VRRAEKR 1857
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQ--KEENLDRKLelLEKREEE 111
|
90 100 110
....*....|....*....|....*....|....
gi 1785379713 1858 LKEVLLQVEEERRNADQFKEQLEKanIRMKQLKR 1891
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEE--LIEEQLQE 143
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1827-1945 |
6.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1827 EAKISQLEEQMEQESKEriiANKlvrRAEKRLKEVLLQVEEERRNA-DQFKEQLEKANIRMKQLKRQLEEAEEEASRANS 1905
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE---AKK---EAEAIKKEALLEAKEEIHKLrNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1785379713 1906 NRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKR 1945
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
886-1272 |
7.18e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 886 ANKYQQLFEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERtLQL------QNEKKKMHQH- 958
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLvqtalrQQEKIERYQEd 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 959 IQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQNA---------------------KLAKERKLLD----- 1012
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqqavqALEKARALCGlpdlt 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1013 -DRIGEFTSTMAEEEEKVKSlnklrnkyeaVIADLEDRLKKEEKGRQEMEK---MKRKLDGETTDLQDQLLElqqqieel 1088
Cdd:COG3096 436 pENAEDYLAAFRAKEQQATE----------EVLELEQKLSVADAARRQFEKayeLVCKIAGEVERSQAWQTA-------- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 kQQLARKEEELQAALARVDdevgqknnllkqlrDLQSQLAELHEDLESEKAARAKAEK----------QRRDLGEELEAL 1158
Cdd:COG3096 498 -RELLRRYRSQQALAQRLQ--------------QLRAQLAELEQRLRQQQNAERLLEEfcqrigqqldAAEELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1159 KTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKV----RDAQvtemrQRHNQVVEEISEQLEQARrfkGNLEKVKQ 1234
Cdd:COG3096 563 EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQ-----DALERLREQSGEALADSQ---EVTAAMQQ 634
|
410 420 430
....*....|....*....|....*....|....*...
gi 1785379713 1235 TLESEntdlikevKNLQAAKQDSEQRRKKLEQQVSEFQ 1272
Cdd:COG3096 635 LLERE--------REATVERDELAARKQALESQIERLS 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
974-1351 |
8.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 974 QKLQLEKVTTESRLKKMEEDILLLEDQNAKLAKERKLLDDrIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKE 1053
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1054 EKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQ--SQLAELH 1131
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1132 EDLESEKAARAKAEKQRRDLGEELEAL--------------------KTELEDTLDSTAAQQELRAKREQEVTDLKKTIE 1191
Cdd:COG4717 250 LLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1192 EDVKVRDAQVTEMRQRHNQVVEEISE--QLEQARRFKGNLEKVKQTLESENTDLIKEVknLQAAKQDSEQRRKKLEQQVS 1269
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAGVEDEEEL--RAALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1270 EFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQD--TQELLQEETRQKLNFSSRVRQ 1347
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRE 487
|
....
gi 1785379713 1348 LEEE 1351
Cdd:COG4717 488 LAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
909-1144 |
8.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 909 LFAEAEEMRARLASKKQELEEILHDLEArveeEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLK 988
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 989 KMEEDIlllEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKV-------KSLNKLRNKYEAVIADLEDRLKKEEKGRQEME 1061
Cdd:COG4942 87 ELEKEI---AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1062 KMKRKLDGETTdlqdQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAAR 1141
Cdd:COG4942 164 ALRAELEAERA----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
...
gi 1785379713 1142 AKA 1144
Cdd:COG4942 240 AER 242
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1494-1591 |
8.95e-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: 463295 [Multi-domain] Cd Length: 151 Bit Score: 41.92 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1494 SLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAIEDGKLRLE 1573
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90
....*....|....*...
gi 1785379713 1574 VNMQAMKAQFERDLQNRD 1591
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRD 139
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1119-1328 |
9.18e-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: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1119 QLRDLQSQLAELHEDLESEKAARAKAEKQRRdlgeELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRD 1198
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYK----ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1199 AQVTEMRQRHNQVVEEISEQLEQARRFKGNLEKVKQTLESENTDLikevknlQAAKQDSEQRRKKLEQQVSEFQIRTNES 1278
Cdd:pfam07888 150 TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF-------QELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1279 EKVKFELAEkLQKLQAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQDTQ 1328
Cdd:pfam07888 223 TTAHRKEAE-NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQ 271
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1802-1949 |
1.08e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1802 KELKVKLNEMDSTMRSKYkitIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERrnadqfkEQLEK 1881
Cdd:COG1196 216 RELKEELKELEAELLLLK---LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-------LELEE 285
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379713 1882 ANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQRKRAPIQ 1949
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1131-1489 |
1.34e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1131 HEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEvtdLKKTIEEDVKVRDAQVTEmrqrhnq 1210
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKRELERIRQ------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1211 vvEEISEQLEQARRfkgnLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFqirtnesEKVKFElaeklq 1290
Cdd:pfam17380 368 --EEIAMEISRMRE----LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM-------EQIRAE------ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1291 klqaeldgvsgalgstegksikltkdlstvqsqlqdtqellQEETRQKlnfssRVRQLEEEKNNLMENLEEEESAKAQLS 1370
Cdd:pfam17380 429 -----------------------------------------QEEARQR-----EVRRLEEERAREMERVRLEEQERQQQV 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1371 RQLQALQQQLLESKKRMEDQGGMVEAMEEAKKKsykeleFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDL--DHQRQ 1448
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK------ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRR 536
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1785379713 1449 IVSNLEKKQKKFDQMLAEEKNISaRYGEERDRAEAEAREKE 1489
Cdd:pfam17380 537 EAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMERERE 576
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1089-1264 |
1.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 KQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDS 1168
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1169 TAAQQELRAKREQEVTDLKKTIEedvkvrdaqvtEMRQRHNQVVEEISE-QLEQARRFKgnLEKVKQTLESENTDLIKEV 1247
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELE-----------ELIEEQLQELERISGlTAEEAKEIL--LEKVEEEARHEAAVLIKEI 178
|
170
....*....|....*..
gi 1785379713 1248 KNLqaAKQDSEQRRKKL 1264
Cdd:PRK12704 179 EEE--AKEEADKKAKEI 193
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1111-1348 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1111 GQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQqelrakreqevtdLKKTI 1190
Cdd:pfam07902 71 GESTGLFKSLEEMLSQLKELNLELTDTKNSNLWSKIKLNNNGMLREYHNDTIKTEIVESAEG-------------IATRI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1191 EEDVKVRDAQVTEMRQRHNQVVEEISEQLeqARRFKGNLEKVKQTLESENTDLIKEVKNLQ---AAKQDSEQRR------ 1261
Cdd:pfam07902 138 SEDTDKKLALINETISGIRREYQDADRQL--SSSYQAGIEGLKATMASDKIGLQAEIQASAqglSQRYDNEIRKlsakit 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1262 -----------KKLEQQVSEFqirTNESEKVKFELAEKLQKL----QAELDGVSGALGSTEGKSIKLTKDLSTVQSQLQD 1326
Cdd:pfam07902 216 ttssgtteayeSKLDDLRAEF---TRSNQGMRTELESKISGLqstqQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQD 292
|
250 260 270
....*....|....*....|....*....|...
gi 1785379713 1327 TQEL----------LQEETR-QKLNFSSRVRQL 1348
Cdd:pfam07902 293 AEKNyssltqtvkgLQSTVSdPNSKLESRITQL 325
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1138-1351 |
1.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1138 KAARAKAEKQRRDLGEELEALKTEledtldstaaqQELRAKreQEVTDLKKTIEEDVKVRDaqvtemrqrhnqvvEEISE 1217
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKE-----------ALLEAK--EEIHKLRNEFEKELRERR--------------NELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1218 QLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEqqvsefqirtnesekvkfelaEKLQKLQAELD 1297
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELE---------------------ELIEEQLQELE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1298 GVSGaLGSTEGKSIKLTKdlstvqsqlqdtqelLQEETRQKLnfSSRVRQLEEE 1351
Cdd:PRK12704 146 RISG-LTAEEAKEILLEK---------------VEEEARHEA--AVLIKEIEEE 181
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
976-1231 |
2.02e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 976 LQLEKVTTESRLKKMEEDillledQNAKLAKERKLlDDRIGEFTstmaEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEK 1055
Cdd:pfam02029 93 IADEKESVAERKENNEEE------ENSSWEKEEKR-DSRLGRYK----EEETEIREKEYQENKWSTEVRQAEEEGEEEED 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1056 GRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQLARK----EEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELH 1131
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKrghpEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1132 EDLESEKaaraKAEKQRRDLGE----ELEALKTEledtldstaaQQElrakREQEVTDLKKTIEEDVKVRDAqvtEMRQR 1207
Cdd:pfam02029 242 VFLEAEQ----KLEELRRRRQEkeseEFEKLRQK----------QQE----AELELEELKKKREERRKLLEE---EEQRR 300
|
250 260
....*....|....*....|....
gi 1785379713 1208 HNQVVEEISEQLEQARRFKGNLEK 1231
Cdd:pfam02029 301 KQEEAERKLREEEEKRRMKEEIER 324
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1395-1944 |
2.06e-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: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1395 EAMEEAKKKSYKELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARY 1474
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1475 GEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAEMDdlVSSKDDVGKNVHELERSKRAL---EQQVQEM 1551
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKIQHLEEEYKKEIndkEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1552 KTQIEELEDELQaieDGKLRLEVNMQAMKaqferDLQNRDDSNDEKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEM 1631
Cdd:pfam05483 246 LIQITEKENKMK---DLTFLLEESRDKAN-----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1632 DLQ-----------DMESQMDSANKGRDE---------------------AVKQLKKLQLQFKEVWREVEETRAARDEIF 1679
Cdd:pfam05483 318 DLQiatkticqlteEKEAQMEELNKAKAAhsfvvtefeattcsleellrtEQQRLEKNEDQLKIITMELQKKSSELEEMT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1680 VQSRDNEKKLKSLEAELLQLQ---------EDLAAAERAKRQA--------QQERDDLADELSNGVSGKSALLDEKRALE 1742
Cdd:pfam05483 398 KFKNNKEVELEELKKILAEDEklldekkqfEKIAEELKGKEQElifllqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1743 MRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERsfsQKAENARQQMERQNK------ELKVKLNEMDSTMR 1816
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ---EDIINCKKQEERMLKqienleEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1817 SKYKITIASLEAKISQLEEQMEQESKERIIANKLVRRAEKRLKEVLLQVEEERRNADQFKE--------------QLEKA 1882
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkalkkkgsaenkQLNAY 634
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1883 NIRMKQLKRQLEEAEEEASRANSNrrrLQRELEDVTESAESMNREVTTLRSRLSKLERQQRK 1944
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDN---YQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1497-1567 |
2.09e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.75 E-value: 2.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785379713 1497 RALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSK---RALEQQVQEMKTQIEELEDELQAIED 1567
Cdd:PRK05431 21 RGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEA 94
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
871-1066 |
2.25e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 42.63 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 871 VKDTQVKTESELKEMANKYQQlfEEKSILAEQLQAETELFAEAEEMRARLASKKQELEEILHDLEARVEEEEERTL-QLQ 949
Cdd:COG4487 24 VKQRRAEFEKELAERLADAAK--REAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKKALAVAEEKEKELaALQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 950 NEKKKMHQHIQDLEeqleeeegaRQKLQLEKVTTEsrlkkmeediLLLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKV 1029
Cdd:COG4487 102 EALAEKDAKLAELQ---------AKELELLKKERE----------LEDAKREAELTVEKERDEELDELKEKLKKEEEEKQ 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1785379713 1030 KSLNKLRN-KYEAVIADLEDrlkkeekgrqEMEKMKRK 1066
Cdd:COG4487 163 LAEKSLKVaEYEKQLKDMQE----------QIEELKRK 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
921-1143 |
2.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 921 ASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDIlllEDQ 1000
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1001 NAKLAKERKLLDDRIGE--------------FTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRK 1066
Cdd:COG4942 96 RAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785379713 1067 LDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAK 1143
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1156-1523 |
2.61e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1156 EALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVRDAQVTEMRQRhnqvVEEISEQLEQARRFKGNLEKVKQT 1235
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR----VAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1236 LESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTK 1315
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1316 DLSTVQSQLQDTQELLQEETRQKLNFSSRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQqlleSKKRMEDQGGMVE 1395
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNA----SERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1396 AMEEAKKKSYKELEflQQRFdEKHQINDKLEKT-------RNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1468
Cdd:pfam07888 262 SMAAQRDRTQAELH--QARL-QAAQLTLQLADAslalregRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1469 NisarygeERDRAEAE-AREKETKALSLSRALEEAIDLKDEL---DRQNKQLRAEMDDL 1523
Cdd:pfam07888 339 M-------EREKLEVElGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEKQEL 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
853-1038 |
2.92e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 853 QVTRQDEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEE----KSILAEQLQA--------ETELFAEAEEMrARL 920
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRAlyrlgrqpPLALLLSPEDF-LDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 921 ASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEGARQKLQLEKVTTESRLKKMEEDILLLEDQ 1000
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
170 180 190
....*....|....*....|....*....|....*...
gi 1785379713 1001 NAKLAKERKLLDDRIGEFTSTMAEEEEKVKSLNKLRNK 1038
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
935-1333 |
3.69e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 935 EARVEEEEERTLQLQNEKKKMhqhiqdleeqleEEEGARQKLQLEKVTTESRLKKMEEdilllEDQNAKLAKERKLLDDR 1014
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQM------------ELEHKRARIELEKKASALKRQLDRE-----SDRNQELQKRIRLLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1015 IGEFTSTMAEEEEkvksLNKLRNKYEAVIADLedrLKKEEKGRQEMEKMKRKLDGETtdlqdqlLELQQQIEELKQQLAR 1094
Cdd:pfam05557 64 EAEAEEALREQAE----LNRLKKKYLEALNKK---LNEKESQLADAREVISCLKNEL-------SELRRQIQRAELELQS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1095 KEEELQAALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDlGEELEALKTELEDTLDSTAAQQE 1174
Cdd:pfam05557 130 TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQD-SEIVKNSKSELARIPELEKELER 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1175 LRAKREQ-------------EVTDLKKTIEEDVKVRDAQVT-EMRQRHNQVVEEISEQLEQ-----------ARRFKGNL 1229
Cdd:pfam05557 209 LREHNKHlnenienklllkeEVEDLKRKLEREEKYREEAATlELEKEKLEQELQSWVKLAQdtglnlrspedLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1230 EKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNESEKVKFELAEKLQKLQAELDGVSGALGS---- 1305
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydke 368
|
410 420 430
....*....|....*....|....*....|
gi 1785379713 1306 --TEGKSIKLTKDLSTVQSQLQDTQELLQE 1333
Cdd:pfam05557 369 ltMSNYSPQLLERIEEAEDMTQKMQAHNEE 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1489-1723 |
3.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1489 ETKALSLSRALEEAIDLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELqaiedg 1568
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1569 klrlevnmqamkAQFERDLQNRDDSNDEKKKLL--------FKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQM 1640
Cdd:COG3883 89 ------------GERARALYRSGGSVSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1641 DSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDL 1720
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
...
gi 1785379713 1721 ADE 1723
Cdd:COG3883 237 AAA 239
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1051-1316 |
3.87e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1051 KKEEKGRQEMEKMKRkLDGETTDLQDQLLELQQQIEELKQQLARKEEELQAALArvddevgQKNNLLKQLRDLQSQLAEL 1130
Cdd:pfam15905 63 KKSQKNLKESKDQKE-LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVR-------EKTSLSASVASLEKQLLEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1131 HE--DLESEKAARAKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREQEV-TDLKKTIEEDVKVRDAQVTEMRQR 1207
Cdd:pfam15905 135 TRvnELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTqKNLEHSKGKVAQLEEKLVSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1208 HNQ---------VVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEqrrKKLEQQVSEFQIRTNES 1278
Cdd:pfam15905 215 IEEkseteklleYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELS---KQIKDLNEKCKLLESEK 291
|
250 260 270
....*....|....*....|....*....|....*...
gi 1785379713 1279 EKVKFELAEKLQKLQAELDGVSGALGSTEGKSIKLTKD 1316
Cdd:pfam15905 292 EELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1544-1944 |
3.98e-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: 42.31 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1544 LEQQVQEMKTQIEELEDELQAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKllfkqvremeveleeerkQKSQIl 1623
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK------------------NKDKI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1624 aakKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWR-------EVEETRAARDEIFVQSRDNEKKLKSLEAEL 1696
Cdd:TIGR04523 99 ---NKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKnidkfltEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1697 LQLQEDLAAAERAKRQAQQERDDLADELSNGVSgksaLLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETI 1776
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK----KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1777 TTELSAERSFSQKA----ENARQQMERQNKELKVKLNEMdstmrSKYKITIASLEAK-----ISQLEEQMEQESKERIIA 1847
Cdd:TIGR04523 252 QTQLNQLKDEQNKIkkqlSEKQKELEQNNKKIKELEKQL-----NQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1848 NKLVRRAEK---RLKEVLLQVEEERRNAD----QFKEQLEKANIRMKQLKRQLEEAEEEASRANSNRRRLQRELEDVTES 1920
Cdd:TIGR04523 327 QNQISQNNKiisQLNEQISQLKKELTNSEsensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420
....*....|....*....|....
gi 1785379713 1921 AESMNREVTTLRSRLSKLERQQRK 1944
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIER 430
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1758-1941 |
3.98e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1758 NTELINDRYRKLTLQVETITTELsaersfsQKAENARQQMERQNK------ELKVKLNEMD--STMRSKYKITIASLEAK 1829
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKEL-------EEAEAALEEFRQKNGlvdlseEAKLLLQQLSelESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1830 ISQLEEQMEQESKE--RIIANKLVRRAEKRLKEVLLQVEEERRN-------ADQFKEQLEKANIRMKQ-LKRQLEEAEEE 1899
Cdd:COG3206 242 LAALRAQLGSGPDAlpELLQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQeAQRILASLEAE 321
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1785379713 1900 ASRANSNRRRLQRELEDVTESAESMNRevttLRSRLSKLERQ 1941
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPE----LEAELRRLERE 359
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1409-1932 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1409 EFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaEEKNISARYGEERDR-----AEA 1483
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML-QSKGLPKKSGEEDWErtrriAEA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1484 EAREKETKALsLSRALEEAIDLKDELDRQNK--QLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQE----------- 1550
Cdd:pfam10174 191 EMQLGHLEVL-LDQKEKENIHLREELHRRNQlqPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhted 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1551 -----------------MKTQIEELEDELQAIE------------------DGKLRLEVNMQAMKAQFERD--LQNRDDS 1593
Cdd:pfam10174 270 reeeikqmevykshskfMKNKIDQLKQELSKKEsellalqtkletltnqnsDCKQHIEVLKESLTAKEQRAaiLQTEVDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1594 ----NDEKKKLLFKQVremeveleeerKQKSQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVE 1669
Cdd:pfam10174 350 lrlrLEEKESFLNKKT-----------KQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1670 ETRAARDEIFVQSRDNEKKLKSLEaELLQLQEDLAAA-----ERAKRQAQQERDDLADELSNGVSGKSALLDEKRALEMR 1744
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLE-EALSEKERIIERlkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEKESS 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1745 ISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQmERQNKELKVKLNEMDSTMrSKYKITIA 1824
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQEV-ARYKEESG 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1825 SLEAKISQL-----EEQMEQESKERIIANkLVRRAEKRLKEV--------LLQVEEERRNADQFKEQL-EKANIRMKQLK 1890
Cdd:pfam10174 576 KAQAEVERLlgilrEVENEKNDKDKKIAE-LESLTLRQMKEQnkkvanikHGQQEMKKKGAQLLEEARrREDNLADNSQQ 654
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1785379713 1891 RQLEEAEEEASRANSNRRRLQRELEDVTESAESMNREVTTLR 1932
Cdd:pfam10174 655 LQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR 696
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
918-1062 |
4.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 918 ARLASKKQELEEILHDLEARVEEEEERTLQLQNEKKKMHQHIQDLEEQLEEEEG--ARQKLQLEKVTTESRLKKMEEDIL 995
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785379713 996 LLEDQNAKLAKERKLLDDRIGEFTSTMAEEEEKVKS----LNKLRNKYEAVIADLEDRLKKEEKGRQEMEK 1062
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAEleaeLEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1407-1568 |
4.09e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1407 ELEFLQQRFDEKHQINDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE----EKNISARYGEERDRAE 1482
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEvearIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1483 AEAREKETKALSLSRAL--EEAIDLKDELDRQNKQLRAEMDDLVSSKDdvgknvhELERSKRALEQQVQEMKTQIEELED 1560
Cdd:COG1579 91 YEALQKEIESLKRRISDleDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 1785379713 1561 ELQAIEDG 1568
Cdd:COG1579 164 EREELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1013-1942 |
4.49e-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: 42.34 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1013 DRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETtdlqDQLLELQQQIEELKQQL 1092
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL----DPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1093 ARKEEELQAALARVDDEVGQKNNL-LKQLRDLQSQLAELHEDLESEKAARAKAEKQRRDLGEELEALKTELEDtLDSTAA 1171
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKDNSELeLKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL-LNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1172 QQELRAKREQEVTDLkktIEEDVKVRDAQVTEMRQRHNqvVEEISEQLEQARRFKGNLEKVKQTLESENTDLIKEVKNLQ 1251
Cdd:TIGR00606 344 ELLVEQGRLQLQADR---HQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1252 AAKQDSEQRRKKLEQQVSEFQiRTNESEKvkfelaEKLQKLQAELDGVSGALGSTEGKS---IKLTKDLSTVQSQLQDTQ 1328
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLG-RTIELKK------EILEKKQEELKFVIKELQQLEGSSdriLELDQELRKAERELSKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1329 ELLQEETRQKlnfssRVRQLEEEKNNLMENLEEEESAKAQLSRQLQALQQQLLESKKRMEDQggmvEAMEEAKKKSYKEL 1408
Cdd:TIGR00606 492 KNSLTETLKK-----EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD----EQIRKIKSRHSDEL 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1409 EFLQQRFDEKHQINDKLEKTRNRLQQ---ELDDLMVDLDHQRQIVSNLEKKQKKFD-QMLAEEKNISARYGEERDRAEAE 1484
Cdd:TIGR00606 563 TSLLGYFPNKKQLEDWLHSKSKEINQtrdRLAKLNKELASLEQNKNHINNELESKEeQLSSYEDKLFDVCGSQDEESDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1485 AREKETKALSLSRALEEAidLKDELDRQNKQLRAEMDDLVSSKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQA 1564
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAG--ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1565 IEdgKLRLEVNMQAMKAQFERDLqnrddsndeKKKLLFKQVREMEVELEEERKQKSQILAAKKKLEMDLQDMESQMDSAN 1644
Cdd:TIGR00606 721 KE--KRRDEMLGLAPGRQSIIDL---------KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1645 KgrdeaVKQLKKLQLQFKEVWREVEETRAArdeifVQSRDNEKKLKSLEAELLQLQEDLAAAERAKRQAQQERDDLADEL 1724
Cdd:TIGR00606 790 D-----VTIMERFQMELKDVERKIAQQAAK-----LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1725 SNGVSGKSALLDEKRALEMRISQLEEELDEEQSNTELINDRYRKLTLQVETITTELSAERSFSQKAENARQQMERQNKEL 1804
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1805 KVKLNEMDSTMRSKYkITIASLEAKIsqleeqmeQESKERIIANKlvrraEKRLKEVLLQVEEERRNADQFKEQLEKANI 1884
Cdd:TIGR00606 940 QDKVNDIKEKVKNIH-GYMKDIENKI--------QDGKDDYLKQK-----ETELNTVNAQLEECEKHQEKINEDMRLMRQ 1005
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785379713 1885 RMKQLKRQleeaeEEASRANSNRRRLQRELEDVTESAESMNREVTTLRSRLSKLERQQ 1942
Cdd:TIGR00606 1006 DIDTQKIQ-----ERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK 1058
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
858-1102 |
4.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 858 DEVMQAKVVELQKVKDTQVKTESELKEMANKYQQLFEEKSILAEQLqaetelfaeaEEMRARLASKKQELEEILHDLEAR 937
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 938 VEEEEERTLQLQNEkkkmhqhiQDLEEQLEEEEGAR------QKLQLEKVTTESRLKKMEEdillLEDQNAKLAKERKLL 1011
Cdd:COG3883 85 REELGERARALYRS--------GGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEE----LKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1012 DDRIGEFTSTMAEEEEKVKSLNKLRNKYEAVIADLEDRLKKEEKGRQEMEKMKRKLDGETTDLQDQLLELQQQIEELKQQ 1091
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250
....*....|.
gi 1785379713 1092 LARKEEELQAA 1102
Cdd:COG3883 233 AAAAAAAAAAA 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1464-1565 |
5.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1464 LAEEKNISARYGEERDRAEAEAREKETKALSLSRALEEAIDLKDELDRQNKQLRAE------------------MDDLVS 1525
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElqklekrllqkeenldrkLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1785379713 1526 SKDDVGKNVHELERSKRALEQQVQEMKTQIEELEDELQAI 1565
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1090-1258 |
5.37e-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: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1090 QQLARKEEELQA-ALARVDDEVGQKNNLLKQLRDLQSQLAELH-------EDLESEKAARAKAEKQRRDLGEELEALKTE 1161
Cdd:pfam09731 297 DQLSKKLAELKKrEEKHIERALEKQKEELDKLAEELSARLEEVraadeaqLRLEFEREREEIRESYEEKLRTELERQAEA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1162 LEDTLDSTAAQQELRAKREQEvTDLKKTIEEDVKVRDAQVTEMRQRHN---QVVEEISEQLEQARRFK---GNLEKVKQT 1235
Cdd:pfam09731 377 HEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRKAQqlwLAVEALRST 455
|
170 180
....*....|....*....|....*...
gi 1785379713 1236 LESENTD-----LIKEVKNLQAAKQDSE 1258
Cdd:pfam09731 456 LEDGSADsrprpLVRELKALKELASDDE 483
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1478-1705 |
5.47e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1478 RDRAEAEAREKETKALSLSRALEEAID-LKDELDRQNKQLRAEMDDLVSSKDDVGKnvhELERSKRALEQQVQEMKTQIE 1556
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEALDkLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1557 ELEDELQAIEDGKLRLEVnmqaMKAqFERDLQNRDDS----------NDEKKKLLFKQVREMEVELEEERKQKSQILAAK 1626
Cdd:PRK05771 111 ELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVVVV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785379713 1627 KKlemdlqdmesqmdsanKGRDEAVKQLKKlqLQFKEVwrEVEETRAARDEIfvqsRDNEKKLKSLEAELLQLQEDLAA 1705
Cdd:PRK05771 186 LK----------------ELSDEVEEELKK--LGFERL--ELEEEGTPSELI----REIKEELEEIEKERESLLEELKE 240
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1486-1739 |
5.53e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.68 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1486 REKETKALSLSRALEEAIDLKDELDRQNKQLRAE---MDDLVSSKDDVGkNVHELERSKRALEQQVQEMKTQIEELEDEL 1562
Cdd:pfam18971 559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKalnFNKAVAEAKSTG-NYDEVKKAQKDLEKSLRKREHLEKEVEKKL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1563 QAIEDGKLRLEVNMQAMKAQFERDLQNRDDSNDEKKKLLFKQVREMEveleeerkqKSQILAAKKKLEMDLQDMESQMDS 1642
Cdd:pfam18971 638 ESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGI---------KRELSDKLEKISKDLKDFSKSFDE 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1643 ANKGRD----EAVKQLKKLQLQFKEV-----W-REVEETRAARDEIFVQSRDNEKKLKSLEAELLQLQEDLAaaerakrq 1712
Cdd:pfam18971 709 FKNGKNkdfsKAEETLKALKGSVKDLginpeWiSKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI-------- 780
|
250 260
....*....|....*....|....*..
gi 1785379713 1713 AQQERDDLADELSNGVSGKSALLDEKR 1739
Cdd:pfam18971 781 INQKVTDKVDNLNQAVSVAKAMGDFSR 807
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1089-1291 |
5.84e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1089 KQQLARKEEELQ-------AALARVDDEVGQKNNLLKQLRDLQSQLAELHEDLESEKAARAKAEK----QRRDLGEELEA 1157
Cdd:PRK11637 53 QQDIAAKEKSVRqqqqqraSLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQqqaaQERLLAAQLDA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1158 L-----KTELEDTLDSTAAQQE---------LRAKREQEVTDLKKTIEEdvkvRDAQVTEMRQRHNQVVEEISEQLEQAR 1223
Cdd:PRK11637 133 AfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREE----LAAQKAELEEKQSQQKTLLYEQQAQQQ 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785379713 1224 RFKGNLEKVKQTLESENTDLIKEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTN----ESEKVKFELAEKLQK 1291
Cdd:PRK11637 209 KLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAErearEAARVRDKQKQAKRK 280
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
999-1188 |
6.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 999 DQNAKLAKERK----LLDDRIGEFTSTMAEEEEkvkSLNKLRNKYEAVIADLEdRLKKEEKgrqemekMKRKlDGETTDL 1074
Cdd:PHA02562 223 DELVEEAKTIKaeieELTDELLNLVMDIEDPSA---ALNKLNTAAAKIKSKIE-QFQKVIK-------MYEK-GGVCPTC 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1075 QDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQKNNLLKQ---LRDLQSQLAELHEDLESE-------KAARAKA 1144
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLvdkakkvKAAIEEL 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1785379713 1145 EKQRRDLGEELEALKTELEDtLDSTAAQQELRAKREQEVTDLKK 1188
Cdd:PHA02562 371 QAEFVDNAEELAKLQDELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1386-1947 |
6.04e-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: 41.88 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1386 RMEDQGGMVEAMEEAKKKSYKELEFLQQRfdekhqinDKLEKTRNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1465
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQK--------REAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1466 EEK--NISARYGE-ERDRAEAEAREKETKALSLSRALEEAIDLKDELD----RQNKQLRAEMDDLVSSKDDVGKNVHELE 1538
Cdd:TIGR00618 292 AAPlaAHIKAVTQiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeqRRLLQTLHSQEIHIRDAHEVATSIREIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1539 RSKRALEQQVQEMKTQIEELEDELQAI--EDGKLRLEVNMQAMKAQFERDLQN-----RDDSNDEKKKLLFKQVREMEVE 1611
Cdd:TIGR00618 372 CQQHTLTQHIHTLQQQKTTLTQKLQSLckELDILQREQATIDTRTSAFRDLQGqlahaKKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1612 LEEERKQK-----SQILAAKKKLEMDLQDMESQMDSANKGRDEAVKQLKKLQLQFKEVWREVEETRAARDEIFVQSR--- 1683
Cdd:TIGR00618 452 QCEKLEKIhlqesAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmq 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1684 ---DNEKKLKSLEAELL-QLQEDLAAAERAKRQAQQERDDLAdELSNGVSGKSALLDEKRALEMRISQLEEELDEEQSNT 1759
Cdd:TIGR00618 532 rgeQTYAQLETSEEDVYhQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1760 ELINDRyRKLTLQVETITTELSA-ERSFSQKAENARQQMERQNKEL-KVKLNEMDSTMRSKYKITIASLEAKISQLEEQM 1837
Cdd:TIGR00618 611 ACEQHA-LLRKLQPEQDLQDVRLhLQQCSQELALKLTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMQSEK 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1838 EQESKERII---ANKLVRRAEKRLKEVLLQVEEERRNADQFKEQLEKANIRMKQLKRQLEEAEEEA--SRANSNRRRLQR 1912
Cdd:TIGR00618 690 EQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEE 769
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1785379713 1913 ---------ELEDVTESAESMNREVTTLRSRLSKLERQQRKRAP 1947
Cdd:TIGR00618 770 vtaalqtgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
959-1166 |
7.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 959 IQDLEEqleeeegarqklqlekvttesRLKKMEEDILLLEDQNAKLAKERKLLDDRIGEFT--STMAEEEEKVKSLnklr 1036
Cdd:COG4913 612 LAALEA---------------------ELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASA---- 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1037 nkyEAVIADLEDRLKKEEKGRQEMEKMKRKLDG---ETTDLQDQLLELQQQIEELKQQLARKEEELQAALARVDDEVGQK 1113
Cdd:COG4913 667 ---EREIAELEAELERLDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1785379713 1114 NNLLKQlrDLQSQLAELHEDlESEKAARAKAEKQRRDLGEELEALKTELEDTL 1166
Cdd:COG4913 744 RLELRA--LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAM 793
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1118-1293 |
8.58e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1118 KQLRDLQSQLAELHEDLESEKAARAkaekqrrDLGEELEALKTELEDTLDSTAAQQELRAKREQEVTDLKKTIEEDVKVR 1197
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQ-------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785379713 1198 DAQVTEMRQRHNQvVEEISEQLEQARRfkgnlekvkqtlesentdlikEVKNLQAAKQDSEQRRKKLEQQVSEFQIRTNE 1277
Cdd:PRK09039 126 DSEKQVSARALAQ-VELLNQQIAALRR---------------------QLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
170
....*....|....*.
gi 1785379713 1278 SekvkfeLAEKLQKLQ 1293
Cdd:PRK09039 184 A------LAQRVQELN 193
|
|
| |
