|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
858-1938 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1485.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 858 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 937
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 938 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1017
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1018 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1097
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1098 KEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1177
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1178 LRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1257
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1258 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE 1337
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1338 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQR 1417
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1418 LEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALS 1497
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1498 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1577
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1578 NMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1657
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1658 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAL 1737
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1738 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1817
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1818 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1897
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1039738675 1898 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-781 |
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: 1444.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14920 231 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14920 311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14920 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKG 658
Cdd:cd14920 471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14920 631 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-781 |
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: 1332.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespkpvKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG---------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQ 337
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd01377 312 VTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQKP 576
Cdd:cd01377 391 NHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 577 RQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtETAFGSAYKTK 656
Cdd:cd01377 469 KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 657 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 736
Cdd:cd01377 538 GGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQ 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1039738675 737 RYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01377 618 RYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1236.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14932 235 TMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14932 315 QKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14932 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGsAYKTKKG 658
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14932 554 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14932 634 EILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-781 |
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: 1208.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14919 228 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14919 308 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14919 388 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKG 658
Cdd:cd14919 468 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14919 548 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14919 628 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-781 |
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: 1197.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14921 231 TLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14921 311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14921 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKG 658
Cdd:cd14921 471 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14921 551 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14921 631 EILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-781 |
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: 1187.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd15896 155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd15896 235 TMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd15896 315 QKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd15896 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTEtaFGSAYKTKKG 658
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd15896 633 EILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-781 |
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: 1177.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKpRQ 578
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTgMTETAFGSayKTKKG 658
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-781 |
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: 1143.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPqespkpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQE 338
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayKTKKG 658
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14930 548 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14930 628 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-781 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1112.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKN 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------VGRLEEQILQSNPILEAFGNAKTVRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 247 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYI 325
Cdd:pfam00063 147 NNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 326 PIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:pfam00063 227 TIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:pfam00063 307 LCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:pfam00063 387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 566 EQGSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMT 645
Cdd:pfam00063 464 TFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 646 ETafgsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGF 725
Cdd:pfam00063 543 ST----PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGF 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 726 PNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:pfam00063 619 PNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-793 |
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: 1018.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpQGELERQLLQANPILESFG 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------------VGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 240 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRF 319
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 320 LSNG-YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGM 397
Cdd:smart00242 225 LNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 398 NVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFE 477
Cdd:smart00242 305 DPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 478 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDK 557
Cdd:smart00242 384 VNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 558 TFVEKLVQEQGSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivg 637
Cdd:smart00242 461 TFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 638 ldqvtgmtetafGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 717
Cdd:smart00242 534 ------------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLEN 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 718 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 793
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1471 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 919.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 36 VWIPSERHGFEAASIKEERGDEVMVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 191 VIQYLAHVASSHKGRKdhnipqespkpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGAN 270
Cdd:COG5022 172 IMQYLASVTSSSTVEI---------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 271 IETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFS 349
Cdd:COG5022 237 IETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 350 HEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 429
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 430 AVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 509
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 510 QREGIEWNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQKPRQLKDKadFCI 587
Cdd:COG5022 475 VKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 588 IHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVgldqvtgmtetafgsayktKKGMFRTVGQLY 667
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRF 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 668 KESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA-- 745
Cdd:COG5022 612 KESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKsw 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 746 --IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQL 823
Cdd:COG5022 692 tgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRI 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 824 SALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEEL--LKVKEKQTKVEGELEEMERKHQqlleekni 901
Cdd:COG5022 772 KKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIikLQKTIKREKKLRETEEVEFSLK-------- 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 902 lAEQLQAETELFAEAEEMRARLaaKKQELEEilhdlesrveeeeernQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQL 981
Cdd:COG5022 844 -AEVLIQKFGRSLKAKKRFSLL--KKETIYL----------------QSAQRVELAERQLQELKIDVKSISSLKLVNLEL 904
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 982 EKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSS--QLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKT 1059
Cdd:COG5022 905 ESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTIL 983
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1060 RQELEKAKRKLDG---ETTDLQDQIAELQAQVDELKV---------QLTKKEEELQGALARGDDETLHKNNALKVARELQ 1127
Cdd:COG5022 984 VREGNKANSELKNfkkELAELSKQYGALQESTKQLKElpvevaelqSASKIISSESTELSILKPLQKLKGLLLLENNQLQ 1063
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1128 AQIAELQEDFESEKASRNKAEKQK--RDLSEELEALKTELEDT-------LDTTAAQQELRTKREQEVAELKKALEDETK 1198
Cdd:COG5022 1064 ARYKALKLRRENSLLDDKQLYQLEstENLLKTINVKDLEVTNRnlvkpanVLQFIVAQMIKLNLLQEISKFLSQLVNTLE 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1199 NHEAQIQ------DMRQRHATALEELS-----EQLEQAKRFKANLEKNKQGLETDNKELACEVK-VLQQVKAESEHKRKK 1266
Cdd:COG5022 1144 PVFQKLSvlqlelDGLFWEANLEALPSpppfaALSEKRLYQSALYDEKSKLSSSEVNDLKNELIaLFSKIFSGWPRGDKL 1223
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1267 LDAQVQELHAKVSEGDRLRVELAEKANKLQNELDN--VSTLLEEAEKKGIKFAKDA----AGLESQLQDTQELLQEETRQ 1340
Cdd:COG5022 1224 KKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNekLLSLLNSIDNLLSSYKLEEevlpATINSLLQYINVGLFNALRT 1303
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1341 KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQsQLADTKKKVDDDLGTIesleeakKKLLKDVEALSQRLEE 1420
Cdd:COG5022 1304 KASSLRWKSATEVNYNSEELDDWCREFEISDVDEELEELI-QAVKVLQLLKDDLNKL-------DELLDACYSLNPAEIQ 1375
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1421 KVLA-YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK--QKKFDQLLAEEK 1471
Cdd:COG5022 1376 NLKSrYDPADKENNLPKEILKKIEALLIKQELQLSLEGKDetEVHLSEIFSEEK 1429
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-781 |
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: 867.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-----------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQD 332
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 333 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGS 569
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 570 HSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdvdrivgldqvtgmtetaf 649
Cdd:cd00124 467 HPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 650 gsayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 729
Cdd:cd00124 519 -----------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRL 581
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 730 VFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd00124 582 PFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-781 |
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: 787.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKdhniPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPG----KKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14927 236 MATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14927 316 YVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQK 575
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 576 PR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDQVtgmTETAFGSA 652
Cdd:cd14927 472 PRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---EDPKSGVK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 653 YKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 731
Cdd:cd14927 546 EKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILY 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 732 QEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14927 626 ADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-781 |
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: 773.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKK--------KDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14913 233 ATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKP 576
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYK 654
Cdd:cd14913 469 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA--------TADADSGKKKVAK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 655 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14913 541 KKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 735 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14913 621 KQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-781 |
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: 752.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipqeSPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK----------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14909 311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKP 576
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 577 RQLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgLDQVTGMTETAFGSAY 653
Cdd:cd14909 467 KPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD------HAGQSGGGEQAKGGRG 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 654 KtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14909 541 K-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 734 FRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14909 620 FKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-781 |
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: 743.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG------------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKP 576
Cdd:cd14934 388 NHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 577 RQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtETAFGSAY 653
Cdd:cd14934 465 KGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 654 KTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14934 531 KQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYP 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039738675 733 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14934 611 EFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-781 |
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: 723.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqESpkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01380 226 ETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd01380 306 IVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 497 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK--FQ 574
Cdd:cd01380 386 FNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 575 KPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRfvaelwkdvdrivgldqvtgmtetafgsayk 654
Cdd:cd01380 462 KPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR------------------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 655 tKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd01380 509 -KK----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEF 583
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1039738675 735 RQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01380 584 FSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-781 |
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: 718.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASShkgrkdhnipqesPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM-------------IESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQK 575
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivglDQVTGmTETAFGSAY 653
Cdd:cd14929 462 PKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 654 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14929 534 RKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYAD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039738675 734 FRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14929 614 FKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-781 |
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: 709.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnipqESPKpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPG----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14917 153 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14917 232 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQK 575
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDqvtGMTETAFGsay 653
Cdd:cd14917 468 PRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGAD---APIEKGKG--- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 654 KTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14917 539 KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 733 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14917 619 DFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-781 |
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: 695.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 181 GAGKTENTKKVIQYLAHVASSHKGRKDHNipqespkpVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEES--------GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 261 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQET 339
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 340 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 500 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQ 578
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 LKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgldqVTGMTETAFGSAYKTK 656
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 657 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 736
Cdd:cd14918 543 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039738675 737 RYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14918 623 RYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-781 |
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: 693.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnipqESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPR 577
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 578 QLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYK- 654
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQ--------TAEGASAGGGAKKg 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 655 -TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14912 544 gKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 733 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14912 624 DFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-781 |
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: 693.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14923 234 ATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKP 576
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDQVTGMTETAFGsayK 654
Cdd:cd14923 470 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---K 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 655 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14923 544 KKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 735 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14923 624 KQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-781 |
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: 691.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnipqespkPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN--------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDN 335
Cdd:cd14916 154 HFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14916 232 LLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14916 312 EYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 496 LFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQ 574
Cdd:cd14916 391 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 575 KPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDqvTGmtETAFGSA 652
Cdd:cd14916 468 KPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASAD--TG--DSGKGKG 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 653 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14916 541 GKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 733 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14916 621 DFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnipqESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR 577
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 578 QLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgldqVTGMTETAFGSAYKT 655
Cdd:cd14910 472 PAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 656 KKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14910 544 KKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 735 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14910 624 KQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-781 |
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: 679.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnipqESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQ 337
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKP 576
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYK 654
Cdd:cd14915 471 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------TAEAEGGGGKKGG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 655 TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14915 543 KKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039738675 734 FRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14915 623 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-781 |
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: 648.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14883 223 DHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14883 303 NVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 575
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 576 PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTGMTETAfGSAYKT 655
Cdd:cd14883 459 PDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 656 KKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 735
Cdd:cd14883 537 SKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFV 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039738675 736 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14883 616 DRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-781 |
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: 648.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipqespkpVKpqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQE 338
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---R 415
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd01378 306 SVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 496 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQ 574
Cdd:cd01378 386 IFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 575 KPRQLKD--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtetafgsa 652
Cdd:cd01378 463 CPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 653 yKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd01378 525 -LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYE 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039738675 733 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01378 604 KFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-781 |
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: 647.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQE 338
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd01383 221 LKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd01383 301 VKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 499 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRq 578
Cdd:cd01383 381 RHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 579 lkDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayktkkg 658
Cdd:cd01383 457 --GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd01383 526 QKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRY 605
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 739 EILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01383 606 GFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-781 |
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: 611.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01381 142 HFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01381 222 DIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd01381 302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSK 572
Cdd:cd01381 382 QQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 573 FQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkDVDRIVGLDqvtgmtetafgSA 652
Cdd:cd01381 458 YLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TR 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 653 YKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd01381 525 KKSP-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFE 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039738675 733 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01381 600 EFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-781 |
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: 606.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIpqespKPVkpqgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEG-----RSV------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDN 335
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIK 412
Cdd:cd01384 225 YRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 413 VGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01384 304 VTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHS 571
Cdd:cd01384 383 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 572 KFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmteTAFGS 651
Cdd:cd01384 460 RFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------EGTSS 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 652 AYKtkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 731
Cdd:cd01384 526 SSK-----FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPF 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 732 QEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd01384 601 EEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-781 |
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: 576.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQ 337
Cdd:cd01382 143 IHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRA 405
Cdd:cd01382 208 RMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd01382 285 MQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:cd01382 363 INYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 566 EQGSHSKFQKPRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivg 637
Cdd:cd01382 440 KHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF-------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 638 ldqvTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 717
Cdd:cd01382 512 ----ESSTNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 718 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01382 588 LDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-781 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 572.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV- 413
Cdd:cd14872 220 EVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIk 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14872 300 GCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 573
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 574 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgLDQVTGMTetafgsay 653
Cdd:cd14872 457 VYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQKTSKV-------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 654 ktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14872 525 --------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039738675 734 FRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-781 |
3.04e-179 |
|
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: 559.39 E-value: 3.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 254 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 334 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 412 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQ--- 565
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAsfg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 566 ----------EQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELwkdvdri 635
Cdd:cd14890 477 rksgsggtrrGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELI-KQSRRSIREV------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 636 vgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 715
Cdd:cd14890 548 --------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 716 EGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-781 |
1.73e-175 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 548.97 E-value: 1.73e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnipqesPKPVKPQGElerQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRFGKYLEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01387 143 FFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd01387 302 RERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQ 574
Cdd:cd01387 381 YYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 575 KPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYK 654
Cdd:cd01387 458 KPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 655 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd01387 531 TMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVF 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 735 RQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 781
Cdd:cd01387 611 IDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-781 |
1.30e-169 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 533.20 E-value: 1.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIpqespkpvkpqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLsgAGEHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNF 336
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGSHSKFQ 574
Cdd:cd14903 380 QKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 575 K----PRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDQVTGMTETAFG 650
Cdd:cd14903 453 DviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 651 SAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 730
Cdd:cd14903 528 RRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLL 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 731 FQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 781
Cdd:cd14903 608 HEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-781 |
3.16e-168 |
|
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: 530.80 E-value: 3.16e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLahVASSHKGrkdHNipqespkpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG------------SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01385 224 RLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01385 304 ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHS 571
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 572 KFQKPrQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdriVGLDQV---------- 641
Cdd:cd01385 460 YYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlra 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 642 ----------TGM----------------TETAFGSAYKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 695
Cdd:cd01385 531 fframaafreAGRrraqrtaghsltlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEK 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 696 RAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQ 775
Cdd:cd01385 609 KPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGK 684
|
....*.
gi 1039738675 776 SKIFFR 781
Cdd:cd01385 685 TKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-779 |
4.87e-168 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 528.98 E-value: 4.87e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 171 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPQESpkpvkpqgeLERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------VRDRVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIP 326
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 327 IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14901 231 RDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQL 484
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 485 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFV 560
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 561 EKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldq 640
Cdd:cd14901 464 NKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 641 vtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 720
Cdd:cd14901 531 ---------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 721 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 779
Cdd:cd14901 590 SRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-743 |
1.26e-164 |
|
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: 520.02 E-value: 1.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVT---------GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-- 326
Cdd:cd14888 145 LQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPis 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 327 ----------------------IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE 384
Cdd:cd14888 225 idmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 385 NTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG 461
Cdd:cd14888 305 ASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 462 ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGV 541
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 542 LALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSS 621
Cdd:cd14888 462 FCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 622 DRFVAELWKD-VDRIVGLdqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKL 700
Cdd:cd14888 540 NPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLF 604
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 701 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 743
Cdd:cd14888 605 DRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-781 |
8.21e-164 |
|
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: 517.04 E-value: 8.21e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespkpVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSL----------KEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR- 415
Cdd:cd14873 231 REVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14873 307 EEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQ 574
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 575 KPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVtgmtetafGSAYK 654
Cdd:cd14873 460 KPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTL--------KCGSK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 655 TKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14873 530 HRR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDF 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1039738675 735 RQRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14873 607 YKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-781 |
2.32e-163 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 515.29 E-value: 2.32e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASShkgrkdhnipqespkpvkPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA------------------NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD 332
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 333 --KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAi 406
Cdd:cd01379 220 gnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd01379 299 LTSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd01379 379 LCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 563 LvqEQGSHSKFQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvt 642
Cdd:cd01379 455 F--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 643 gmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 722
Cdd:cd01379 517 -------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRR 577
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 723 QGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd01379 578 QGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-781 |
4.82e-159 |
|
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: 503.45 E-value: 4.82e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD------------------DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD----- 332
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseele 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 333 --KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14897 223 yyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 567 QGSHSKFQKPrqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivgldqvtgmte 646
Cdd:cd14897 460 CGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 647 tafgsayktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 726
Cdd:cd14897 522 ------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYP 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 727 NRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd14897 584 IRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-781 |
1.40e-157 |
|
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: 500.44 E-value: 1.40e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQ 330
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 331 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAI 406
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 407 LTPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIF 476
Cdd:cd14892 313 VTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 477 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KAT 555
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 556 DKTFVEKLVQEQ-GSHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdvdr 634
Cdd:cd14892 470 DKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 635 ivgldqvtgmtetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 714
Cdd:cd14892 536 -------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGV 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 715 LEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 781
Cdd:cd14892 584 LEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-741 |
2.28e-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: 476.72 E-value: 2.28e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkDHNIPQESPKPVKPQGeLERQLLQANPILESFGNAKT 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------DNNLAASVSMGKSTSG-IAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 244 VKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlksdlllegfnnyrflsng 323
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 324 yipipGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLG 396
Cdd:cd14900 214 -----AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAG 472
Cdd:cd14900 289 VDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 473 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP 552
Cdd:cd14900 369 FEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 553 KATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSSdrfvaelwkdV 632
Cdd:cd14900 446 KGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------V 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 633 DrivgldqvtgmtetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 712
Cdd:cd14900 508 D-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561
|
650 660
....*....|....*....|....*....
gi 1039738675 713 GVLEGIRICRQGFPNRIVFQEFRQRYEIL 741
Cdd:cd14900 562 GVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-744 |
2.44e-146 |
|
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: 469.90 E-value: 2.44e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPV-KPQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 249 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE----GFNNYRFLSNG 323
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 324 YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 401
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 402 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 474
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 552
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 553 KATDKTFVEKLVQEQGSHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdv 632
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 633 driVGLDQVTGMTETAFGSAYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 712
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 1039738675 713 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 744
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-781 |
3.52e-145 |
|
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: 466.31 E-value: 3.52e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 177 TGESGAGKTENTKKVIQYLAHVAsshkgrkdhnipqespkpvKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-------------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 257 RINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-- 332
Cdd:cd14889 144 QLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRev 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 333 ---KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAi 406
Cdd:cd14889 217 qywKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd14889 294 LTCTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKL 563
Cdd:cd14889 374 ACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 564 VQEQGSHSKFQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQS-----SDRFVAELWKdVDRIVGL 638
Cdd:cd14889 451 NIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSatpllSVLFTATRSR-TGTLMPR 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 639 DQVTGMTETAFGSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 718
Cdd:cd14889 528 AKLPQAGSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETI 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 719 RICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd14889 602 RIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-781 |
1.71e-142 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 458.35 E-value: 1.71e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 252 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 329
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 330 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 404
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 405 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 482
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 483 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 563 LVQEQGSHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHqSSDRFvaelwkdvdrivgLDQV 641
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 642 TGMTEtafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 721
Cdd:cd14891 535 QELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 722 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-781 |
1.15e-136 |
|
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: 442.07 E-value: 1.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPQespkpvkpqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIAK---------------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDN 335
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14904 223 FASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14904 302 ESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSK 572
Cdd:cd14904 382 KFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNES 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 573 FQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtGMTETAFGSA 652
Cdd:cd14904 458 IDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 653 YKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14904 527 GKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPK 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 733 EFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 781
Cdd:cd14904 606 ELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-781 |
2.98e-136 |
|
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: 440.76 E-value: 2.98e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIpqespkpvkpqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------RQPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQ 337
Cdd:cd14896 143 HLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-G 414
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14896 301 YGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 494 QQLFNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 573
Cdd:cd14896 381 QLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 574 QKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtgmtetafgSAY 653
Cdd:cd14896 458 AKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAE-----------------PQY 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 654 KTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14896 519 GLGQGK-PTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 734 FRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14896 598 FLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-781 |
9.81e-135 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 437.80 E-value: 9.81e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQEspkpvkpQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-------KLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--------HLKSDLLLEGFNNYRFL 320
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 321 SNGYIPIPGQ-QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLG 396
Cdd:cd14908 234 GQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFE 474
Cdd:cd14908 314 VDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-K 553
Cdd:cd14908 393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 554 ATDKTFVEKLV--------QEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqssdrf 624
Cdd:cd14908 470 GSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 625 vaelwkdvdrivgldqvtgmtetafgsayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 704
Cdd:cd14908 536 -----------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKR 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 705 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMIRALELD 767
Cdd:cd14908 586 VTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSM 664
|
730
....*....|....*...
gi 1039738675 768 PNL----YRIGQSKIFFR 781
Cdd:cd14908 665 KNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-743 |
1.60e-133 |
|
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: 435.86 E-value: 1.60e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhniPQES-PKPVKPQGELERQLLQANPILESFGNAKTVKND 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR----------DQSStEQEGSDAVEIGKRILQTNPILESFGNAQTIRND 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 248 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsNGYIP- 326
Cdd:cd14902 151 NSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPs 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 327 ---IPGQQDKDN--FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMN 398
Cdd:cd14902 230 farKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 399 VMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDI 470
Cdd:cd14902 310 VDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 471 AGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECW 550
Cdd:cd14902 390 FGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 551 FPKATDKTFVEKLVQEQGSHSKfqkprqlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwk 630
Cdd:cd14902 467 MPKGSNQALSTKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN-------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 631 DVDRIVGLDQVTGMTETAFGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQ 708
Cdd:cd14902 527 EVVVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQ 606
|
650 660 670
....*....|....*....|....*....|....*
gi 1039738675 709 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 743
Cdd:cd14902 607 MRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-834 |
1.85e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 433.30 E-value: 1.85e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIPQespkpvkpqgelerQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKIQN--------------AIMAANPVLEAFGNAKTIRNNNSSRFGRF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 256 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:PTZ00014 251 MQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:PTZ00014 331 FEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTN 490
Cdd:PTZ00014 411 TYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITN 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 491 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSH 570
Cdd:PTZ00014 490 EMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNN 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 571 SKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafg 650
Cdd:PTZ00014 567 PKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG------------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 651 sayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 730
Cdd:PTZ00014 633 ---KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 731 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIIFFQAVC 807
Cdd:PTZ00014 708 FAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALI 787
|
730 740
....*....|....*....|....*..
gi 1039738675 808 RGYLARKAFAKKqqqlsaLKVLQRNCA 834
Cdd:PTZ00014 788 LKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-742 |
3.37e-131 |
|
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: 428.60 E-value: 3.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPQEspkpvkpqgelerQLLQANPILESFGNA 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS-------------ELLSANPILESFGNA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 242 KTVKNDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN- 315
Cdd:cd14895 142 RTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 316 -NYRFLSNG--YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD-------------- 378
Cdd:cd14895 222 qEFQYISGGqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrl 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 379 -QASMPENTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 454
Cdd:cd14895 302 aSASPSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 455 DRTK----------RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLD 524
Cdd:cd14895 382 PQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 525 lQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWL 602
Cdd:cd14895 462 -SVCLEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFC 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 603 MKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGmfrtVGQLYKESLTKLMATLRNTN 682
Cdd:cd14895 537 EKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQ 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 683 PNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 742
Cdd:cd14895 613 THYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-779 |
2.06e-127 |
|
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: 415.93 E-value: 2.06e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpQESpkpvkpqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI-QTA-------------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIK 412
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 413 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14876 304 AGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHS 571
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 572 KFqKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafgs 651
Cdd:cd14876 459 KF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG-------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 652 ayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 731
Cdd:cd14876 524 --KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPF 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 732 QEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 779
Cdd:cd14876 600 EEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-781 |
2.02e-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: 2.02e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnipqespkpvkpqgeLERQLLQA-NPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV------------------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:cd01386 143 LDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI--------- 406
Cdd:cd01386 223 FSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 407 ---LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN---- 479
Cdd:cd01386 303 qqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 480 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALL 545
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 546 DEECWFPKATDKTFVEKLVQEQG--SHSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQ 619
Cdd:cd01386 462 DEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 620 SSDRFVAelwkdvdrivgldqvtgmtetafgsayKTKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRCIIPNH--EKRA 697
Cdd:cd01386 542 SQKETAA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDE 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 698 GK----------LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACERMIR 762
Cdd:cd01386 591 RStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLE 670
|
730
....*....|....*....
gi 1039738675 763 ALELDPNLYRIGQSKIFFR 781
Cdd:cd01386 671 ELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-743 |
6.15e-119 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 392.29 E-value: 6.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQEspkpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER----------IEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 255 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKD 334
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 335 NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14880 227 CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 412 KVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd14880 307 RAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGS 569
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 570 HSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAf 649
Cdd:cd14880 464 GNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAP- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 650 gsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 729
Cdd:cd14880 543 ----------VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRV 612
|
650
....*....|....
gi 1039738675 730 VFQEFRQRYEILTP 743
Cdd:cd14880 613 SHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-744 |
7.02e-118 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 391.26 E-value: 7.02e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 177 TGESGAGKTENTKKVIQYLAHVASShKGRKDHNIPQESPKpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSS-NQQQNNNNNNNNNS-------IEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 257 RINFDVTGYIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLSGAGehlKSDLLLEGFNN----YRFL---------- 320
Cdd:cd14906 153 KIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 321 ----SNGYIPIPGQQDKD-NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---C 392
Cdd:cd14906 230 ksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 393 HLLGMNVMEFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQ 460
Cdd:cd14906 310 KLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 461 GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppG 540
Cdd:cd14906 390 NNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--G 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 541 VLALLDEECWFPKATDKTFVEKLVQEQgsHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQS 620
Cdd:cd14906 467 ILSLLDDECIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLAS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 621 SDRFVAELWKdvdrivglDQVTGMTETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKL 700
Cdd:cd14906 545 SNFLKKSLFQ--------QQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNF 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039738675 701 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 744
Cdd:cd14906 611 NNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-781 |
1.98e-113 |
|
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: 376.15 E-value: 1.98e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 253 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQ 331
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 332 DKDNFQETMEAMHIMgFSHEEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILT 408
Cdd:cd14886 223 DQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIIT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 409 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd14886 302 KVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECwfpkatdktfvekLVQ 565
Cdd:cd14886 378 INYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQC-------------LIQ 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 566 eQGSHSKFQKPRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDR 634
Cdd:cd14886 442 -TGSSEKFTSSCKSKIKNNsfipgkgsqcnFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPN 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 635 IVGLdqvtgmtetafgsayktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 714
Cdd:cd14886 521 EDGN-----------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSI 581
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 715 LEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14886 582 FESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-781 |
9.60e-112 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 371.84 E-value: 9.60e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPQESPKpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSS----NTSQRSIA-----DKIDENLKWSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 256 IRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPG 329
Cdd:cd14875 152 IKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 330 Q--QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAIL 407
Cdd:cd14875 232 KtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 408 tprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 567 QGSHSK-FQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdrivgldqvtgmt 645
Cdd:cd14875 465 WANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL----------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 646 etafgsaYKTKKGMFR---TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 722
Cdd:cd14875 527 -------LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKR 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 723 QGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 781
Cdd:cd14875 600 QGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-738 |
1.17e-109 |
|
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: 367.50 E-value: 1.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 168 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKND 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 248 NSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-----AGEHLKSDLLLEGFNNYRFLS 321
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 322 NGYIPI--PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ-------- 389
Cdd:cd14899 240 QSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 390 --KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT---------- 457
Cdd:cd14899 320 ftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 458 ----KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE 533
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 534 RpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLN 610
Cdd:cd14899 479 H--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 611 DNVATLLHQSSDRFVAEL-----WKDVDRIVGLDQVTGMTETAFGSAYKTKkgmfrTVGQLYKESLTKLMATLRNTNPNF 685
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAV-----SVGTQFKIQLNELLSTVRATTPRY 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 686 VRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14899 632 VRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-781 |
1.34e-97 |
|
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: 332.77 E-value: 1.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpVKPQGeLERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHG-------------ADSQG-LEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 251 RFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFlsngyipipgq 330
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 331 qDKDNFQETMEAMHIMGFSHEEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL------- 395
Cdd:cd14887 216 -DLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclss 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 396 GMNVMEFTRAILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD 455
Cdd:cd14887 292 GLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 456 RTKR-------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 519
Cdd:cd14887 372 RSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 520 --DFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGSH 570
Cdd:cd14887 452 csAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 571 SKFQK--PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVaelwkdvdRIVGLDQVTGMteta 648
Cdd:cd14887 532 AKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV---- 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 649 fgSAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 728
Cdd:cd14887 599 --RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCR 673
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 729 IVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14887 674 LPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-780 |
7.21e-97 |
|
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: 327.97 E-value: 7.21e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnipqeSPKPVKpqgeLERQLLQANPILESFGNAKTVK 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTK----LSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 246 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNG 323
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 324 Y--IPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMN 398
Cdd:cd14879 223 HplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 399 VMEFtRAILTPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGF 473
Cdd:cd14879 302 PEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 474 EIF---ELNSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALL 545
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGIL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 546 DEEC-WFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSS 621
Cdd:cd14879 449 DDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SP 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 622 DrFVAelwkdvdrivgldqvtgmtetafgsayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLD 701
Cdd:cd14879 519 D-FVN--------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFD 564
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 702 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSKIFF 780
Cdd:cd14879 565 KRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-745 |
7.98e-96 |
|
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: 322.62 E-value: 7.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDvtGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQET 339
Cdd:cd14898 139 FD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 340 MEAMHIMGFSHeeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14898 210 CSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 500 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgshSKFQKPRqL 579
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 580 KDKADFCII--HYAGKVDYKADEWLMKNMDplndnvatllhqssdrfvaelwkdvdrivgldqvtGMTETAFGSAYKTKK 657
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDE 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 658 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 737
Cdd:cd14898 475 GSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEER 554
|
....*...
gi 1039738675 738 YEILTPNA 745
Cdd:cd14898 555 YRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-781 |
4.46e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 314.45 E-value: 4.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT------------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 256 IRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQ 330
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 331 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14878 223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCIN 487
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 488 YTNEKLQQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATD 556
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 557 KTFVEKL--VQEQGSHSKFQKPRQ-------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVA 626
Cdd:cd14878 450 PNLPKKLqsLLESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 627 ELwkdvdrivgldqvtgmtetafgsaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVL 706
Cdd:cd14878 530 HL------------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVS 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 707 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKIFFR 781
Cdd:cd14878 583 AQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-781 |
5.22e-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: 307.71 E-value: 5.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAhvasshkgrkdhnipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL-------------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 339 TMEAMHIMGFsHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14937 218 LMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 494 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 573
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 574 QKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTetafgsaY 653
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLIT-------F 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 654 KtkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQE 733
Cdd:cd14937 524 K------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDV 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 734 FRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 781
Cdd:cd14937 591 FLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-733 |
4.25e-81 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 282.95 E-value: 4.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT-------------ERIDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 251 RFGKFIRINFD---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-AGEHLKSDLLLEGFNNYRFL 320
Cdd:cd14884 144 RCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 321 --------------------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKkerntdqa 380
Cdd:cd14884 224 npdeshqkrsvkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 381 smpentvaqKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ 460
Cdd:cd14884 296 ---------AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 461 GA-----------SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCI 529
Cdd:cd14884 367 DEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 530 DLIERpanppgVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGSHSK-FQKPR--------QLKDKADFCIIHY 590
Cdd:cd14884 446 IFIAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 591 AGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvtgmtetafgSAYKTKKGMFRTVGQLYKES 670
Cdd:cd14884 520 AGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKE 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 671 LTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14884 577 LDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-768 |
7.73e-78 |
|
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: 271.99 E-value: 7.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 173 SILCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipqespkpvKPQGELERQLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGG-----------------GPETDAFKHLAAAFTVLRSLGSAKTATNSESSRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 253 GKFIRINFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQ 330
Cdd:cd14881 133 GHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 331 QDKDNFQETMEAMHIMGFsheEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiL 407
Cdd:cd14881 212 EDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-L 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 408 TPRIK-VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFEL 478
Cdd:cd14881 284 TTRTHnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 479 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDK 557
Cdd:cd14881 360 SQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 558 TFVEKLVQEQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdvdrivg 637
Cdd:cd14881 436 SYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 638 ldqvtgmteTAFGsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 717
Cdd:cd14881 499 ---------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLET 560
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 718 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 768
Cdd:cd14881 561 VNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-746 |
2.55e-71 |
|
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: 252.87 E-value: 2.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQEspkpvkpqgelerqllqanpILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES--------------------VFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDvTGYIVGANIE-TYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14874 131 LLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14874 210 KHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 414 GrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 494 QQLFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK 572
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 573 FQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdrivgldqvtgmtetaFGSA 652
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESY 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 653 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14874 500 SSNTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKT 579
|
650
....*....|....
gi 1039738675 733 EFRQRYEILTPNAI 746
Cdd:cd14874 580 TFARQYRCLLPGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-781 |
1.60e-69 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 248.85 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnipqespkpvkpqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNF 336
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 417 YVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 497 FNHTMFILEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF-Q 574
Cdd:cd14905 367 YLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 575 KPRQlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRF-------------VAELWKDVD-------- 633
Cdd:cd14905 440 KPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakks 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 634 --RIVGL---------DQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKL 700
Cdd:cd14905 514 plSIVKVllscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTF 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 701 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIF 779
Cdd:cd14905 594 DVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIF 671
|
..
gi 1039738675 780 FR 781
Cdd:cd14905 672 LR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-780 |
1.29e-67 |
|
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: 244.50 E-value: 1.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKpqgeleRQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIG------QQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgEH---LKSDLLL-EGFNNYRFLSNGyIPI 327
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 328 PGQ--QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------L 395
Cdd:cd14893 236 ATNfaLDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 396 GMNVMEFTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG- 461
Cdd:cd14893 316 AAKLLEVEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNi 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 462 ---ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCI 529
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 530 DLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD------------FCIIHYAGKVDYK 597
Cdd:cd14893 476 QLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 598 ADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkDVDRIVGLDQVT--------------GMTETAFG----SAYKTKKGM 659
Cdd:cd14893 554 GKGLSSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAaassekaakqteerGSTSSKFRksasSARESKNIT 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 660 FRTVGQLYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYe 739
Cdd:cd14893 626 DSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY- 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1039738675 740 iltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 780
Cdd:cd14893 704 --------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-741 |
2.02e-64 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 232.71 E-value: 2.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 180 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPQespkpvkpqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATG--------------RVESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG------ 329
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 330 ----QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14882 219 rddpEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNS 480
Cdd:cd14882 297 LTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 481 FEQLCINYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDK 557
Cdd:cd14882 374 LEQLMVNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 558 TFVEKLVQEQgsHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivg 637
Cdd:cd14882 446 NYIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN------ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 638 lDQVTGMtetafgsayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 714
Cdd:cd14882 515 -SQVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAV 578
|
650 660
....*....|....*....|....*..
gi 1039738675 715 LEGIRICRQGFPNRIVFQEFRQRYEIL 741
Cdd:cd14882 579 LDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-779 |
1.63e-60 |
|
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: 222.79 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 179 ESGAGKTENTKKVIQYLAH-VASSHKGRKDHNIPQESPKPV----KPQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYqVKGSRRLPTNLNDQEEDNIHNeentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 254 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 334 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 387
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 388 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 464
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 465 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 544
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 545 LDEECWFPKATDKTFVEKLVQEQGSHSKF--QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 622
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 623 RFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHEKRA- 697
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 698 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRIGQSK 777
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1039738675 778 IF 779
Cdd:cd14938 710 IF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-265 |
6.53e-60 |
|
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: 203.35 E-value: 6.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 200 SSHKGRKDHNIpqeSPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 265
Cdd:cd01363 81 FNGINKGETEG---WVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1015-1871 |
2.36e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 147.90 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1015 EDRIAECSSQL------AEEEEKAKNL-AKIRNKQ-EVMISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQA 1086
Cdd:TIGR02168 192 EDILNELERQLkslerqAEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1087 QVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1166
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1167 DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATaLEELSEQLEQAKRFKANLEKNKQGLETDNkel 1246
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI--- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1247 acevkvlqqvkaeSEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDaaglESQ 1326
Cdd:TIGR02168 424 -------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1327 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVdddlgTIESLEEAKKk 1406
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-----VVENLNAAKK- 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1407 llkDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAeekGISARYAEERDRAEA 1486
Cdd:TIGR02168 561 ---AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1487 EAREKETKAL---------------SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1551
Cdd:TIGR02168 635 LELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1552 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQnEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1631
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL-EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1632 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1711
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1712 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSA-- 1789
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtl 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1790 ------AQKSDNARQQLERQNKELKAKLQELeGAVKSKFKATISALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEK 1859
Cdd:TIGR02168 954 eeaealENKIEDDEEEARRRLKRLENKIKEL-GPVNLAAIEEYEELKERYDFLTAQKEdlTEAKEtlEEAIEEIDREARE 1032
|
890
....*....|..
gi 1039738675 1860 KLKEIFMQVEDE 1871
Cdd:TIGR02168 1033 RFKDTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1141-1896 |
8.23e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 145.97 E-value: 8.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1141 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ----QELRTKREQE--------VAELKKALE--DETKNHEAQ 1203
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEdilNELERQLKSLERQaekaERYKELKAELrelelallVLRLEELREelEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1204 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDR 1283
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1284 LRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ-------EETRQKLNLSSRIRQLEEEKN 1356
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1357 SLQE-----QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKkkllkdvEALSQRLEEKVLAYDKLEKT 1431
Cdd:TIGR02168 411 RLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL-------EELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1432 KNRLQQELDDLTVDLDHQRQI---VSNLEKKQKKF--------DQLLAEEKGISARYAEERDRAEAEAREKETKAL---- 1496
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaia 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1497 SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL--- 1573
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrp 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1574 ---------------------RLEVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1631
Cdd:TIGR02168 644 gyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1632 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1711
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1712 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNdrfrkttLQVDTLNTELAAERSAAQ 1791
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1792 KSDNARQQLERQNKELKAKLQELEGAVKSKFKAtISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1871
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESK-RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
810 820
....*....|....*....|....*.
gi 1039738675 1872 -RRHADQYKEQMEKANARMKQLKRQL 1896
Cdd:TIGR02168 956 aEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1015-1868 |
1.68e-30 |
|
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: 132.11 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1015 EDRIAECSSQLAEEEEKAKNLAKIRNKQEvMISDLEERLKKEE-----KTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1089
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1090 ELKVQLTKKEEELQGALARGDDETLHKNNALKVA-RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDT 1168
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1169 LDTTAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELS---EQLEQAKRFKANLEKNKQGLETDNKE 1245
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1246 LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1325
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1326 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearknlEKQVLALQSQLADTKKK--VDDDLGTIESLEEA 1403
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG----------ERYATAIEVAAGNRLNNvvVEDDAVAKEAIELL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1404 KKKLL-----------KDVEALSQRLEEKV---LAYDKLE---KTKNRLQQELDDLTV--DLDHQRQIVSN--------- 1455
Cdd:TIGR02169 568 KRRKAgratflplnkmRDERRDLSILSEDGvigFAVDLVEfdpKYEPAFKYVFGDTLVveDIEAARRLMGKyrmvtlege 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1456 -LEKKQKKFDQLLAEEKGISaRYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG 1534
Cdd:TIGR02169 648 lFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1535 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQTRDEQNEEKKRLLLKQVRELEAE 1614
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1615 LEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKS 1694
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1695 LEAEILQLQEELAsserarrHAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttl 1774
Cdd:TIGR02169 873 LEAALRDLESRLG-------DLKKERDELEAQL-------RELERKIEELEAQIEKKRKRLSELKAKLEALEEE------ 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1775 qvdtlNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE--GAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1852
Cdd:TIGR02169 933 -----LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
890
....*....|....*.
gi 1039738675 1853 LVRRTEKKLKEIFMQV 1868
Cdd:TIGR02169 1008 RIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1195-1944 |
5.68e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 130.18 E-value: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1195 DETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA--NLEKNKQG--LETDNKELACEVKVLQQVKAESEHKRKKLDAQ 1270
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1271 VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQ 1350
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1351 LEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK 1430
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1431 TKNRLQQELDDLTVDLDHQR--QIVSNLEKKQKKFDQLLAEEKGISARYAE---ERDRAEAEAREKETKALSLARALEEA 1505
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1506 LEAKEEFERQNKQ----------------------------LRADMEDL-MSSKDDVGKNVHELEKS---KRALEQQVEE 1553
Cdd:TIGR02168 502 EGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvVENLNAAKKAIAFLKQNelgRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1554 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTR----------DEQNEEKKRLLLkqvRELEAELEDER---- 1619
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRP---GYRIVTLDGDLvrpg 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1620 ----KQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1695
Cdd:TIGR02168 659 gvitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1696 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeleeEQSNMELLNDRFRKTTLQ 1775
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1776 VDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSkFKATISALEAKIGQLEEQLEQEAKERAAANKLVR 1855
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1856 RTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA-------TEANEGL 1927
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAealenkiEDDEEEA 970
|
810
....*....|....*..
gi 1039738675 1928 SREVSTLKNRLRRGGPI 1944
Cdd:TIGR02168 971 RRRLKRLENKIKELGPV 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1064-1708 |
1.65e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.52 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1064 EKAKRKLDGETTDL---QDQIAELQAQVDELKVQ---------LTKKEEELQGALargddetlhknnALKVARELQAQIA 1131
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPLERQaekaeryreLKEELKELEAEL------------LLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1132 ELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknheaqiQDMRQRH 1211
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------EERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1212 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1291
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1292 ANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKN 1371
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1372 LEKQVLALQSQLADtkkkvdddlgtieslEEAKKKLLKDVEALSQRLEEKVLAYDKLEKtKNRLQQELDDLTVDldhqrq 1451
Cdd:COG1196 475 LEAALAELLEELAE---------------AAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGV------ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1452 ivsnlekkQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD 1531
Cdd:COG1196 533 --------EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1532 DVgKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRLLLKQVREL 1611
Cdd:COG1196 605 AS-DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT-LEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1612 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEiFAQSKESEKK 1691
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEPPD 761
|
650
....*....|....*..
gi 1039738675 1692 LKSLEAEILQLQEELAS 1708
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1681 |
1.17e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.94 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 859 RQEEELQakdeeLLKVKEKQTKVEGELEEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKK-QELEEILHDL 937
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALLVLRlEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 938 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1017
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1018 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1097
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1098 KEEELQGALARgdDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQE 1177
Cdd:TIGR02168 405 LEARLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1178 LRTKREQEvaelkkaleDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNK-ELACE------- 1249
Cdd:TIGR02168 477 LDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrl 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1250 ----VKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLqnelDNVSTLLEEAEKKGIKFAKDAAGLES 1325
Cdd:TIGR02168 548 qavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI----EGFLGVAKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1326 Q------LQDTQELLQEETRQ---------------------------KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL 1372
Cdd:TIGR02168 624 GvlvvddLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1373 EKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQi 1452
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1453 vsNLEKKQKKFDQLLAEEKGISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1529
Cdd:TIGR02168 783 --EIEELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1530 KDDVGKNVHELE-------KSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKR 1602
Cdd:TIGR02168 861 IEELEELIEELEseleallNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1603 LLLKQVREL-EAELEDERKQRALAVASKKKMEIDLKDLEAQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASR 1678
Cdd:TIGR02168 940 NLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
...
gi 1039738675 1679 DEI 1681
Cdd:TIGR02168 1020 EEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1177-1868 |
1.61e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1177 ELRTKREQevAELKkaLEdETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA------NLEKNKQGLETDNKELacEV 1250
Cdd:COG1196 169 KYKERKEE--AERK--LE-ATEENLERLEDILGELERQLEPLERQAEKAERYRElkeelkELEAELLLLKLRELEA--EL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1251 KVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDT 1330
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1331 QELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKD 1410
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1411 VEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEARE 1490
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1491 KETKALSLARaleealeakeefERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRaLEQQVEEMRTQLEELEDELQATED 1570
Cdd:COG1196 479 LAELLEELAE------------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1571 AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR 1650
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1651 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANS 1730
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1731 ASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKsdnARQQLERQNKEL--- 1807
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELERLEREIEALgpv 782
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 1808 --KAkLQELEgavkskfkatisALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEKKLKEIFMQV 1868
Cdd:COG1196 783 nlLA-IEEYE------------ELEERYDFLSEQREdlEEAREtlEEAIEEIDRETRERFLETFDAV 836
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1702 |
3.44e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.40 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 859 RQEEELQAKDEELLKVKEKQtkVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 938
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 939 SRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRI 1018
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1019 AECssqlaeeeekaknlakirnkqevmisdleerlkkeektRQELEKAKRKLDgettDLQDQIAELQAQVDELKVQLtkk 1098
Cdd:TIGR02168 375 EEL--------------------------------------EEQLETLRSKVA----QLELQIASLNNEIERLEARL--- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1099 eEELQGALARGDDETLHKNNALKvarelQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQEL 1178
Cdd:TIGR02168 410 -ERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1179 RTKREQevaelkkalEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNK-ELACE-------- 1249
Cdd:TIGR02168 478 DAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrlq 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1250 ---VKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAnklqNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1326
Cdd:TIGR02168 549 avvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL----KNIEGFLGVAKDLVKFDPKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1327 LQDTQELLQE-ETRQKLNLSSRIRQLEEEK-----------NSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDL 1394
Cdd:TIGR02168 625 VLVVDDLDNAlELAKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1395 GTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL-DHQRQIVSNLEKKQKKFDQLLAEEKGI 1473
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1474 sARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEE 1553
Cdd:TIGR02168 785 -EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1554 MRTQLEELEDELQATEDAKLRLEVNMQAmkAQFERDLQTRDEQNEEKKRlllkqvRELEAELEDERKQralavaskkkme 1633
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALAL--LRSELEELSEELRELESKR------SELRRELEELREK------------ 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1634 idLKDLEAQIEAANKARDEVIKQLRklqaqmKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1702
Cdd:TIGR02168 924 --LAQLELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1046-1927 |
5.20e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 117.48 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1046 ISDLEERLKKEEKTRQELEKAKRKLDgettdlqdqiaELQAQVDELKVQLTKKEEElqgalargddetlhKNNALKvare 1125
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEELEEVEENIE-----------RLDLIIDEKRQQLERLRRE--------------REKAER---- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1126 LQAQIAELQEDFESEKASR-NKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQI 1204
Cdd:TIGR02169 213 YQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKL-------TEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1205 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETdnkelacevkvlQQVKAESEhkRKKLDAQVQELHAKVSEGDRL 1284
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE------------RLAKLEAE--IDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1285 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1364
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKE-------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1365 EEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDdltv 1444
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA---- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1445 DLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEarEKETKALSLAraleealeakeeferqnkqLRADME 1524
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA-------------------AGNRLN 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1525 DLMSSKDDVGKNVHELEKSK---RALEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMKAQFE-------RDlqTRD 1594
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafkyvfGD--TLV 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1595 EQNEEKKRLLLKQVR--ELEAELEDE--------RKQRALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1664
Cdd:TIGR02169 626 VEDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1665 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1744
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1745 EARIAQLEEELEEEQsnMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV------ 1818
Cdd:TIGR02169 785 EARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngk 862
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1819 KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRqLEE 1898
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKG 941
|
890 900
....*....|....*....|....*....
gi 1039738675 1899 AEEEATRANASRRKLQRELDDATEANEGL 1927
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-722 |
1.08e-25 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 116.00 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 105 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYSENIIEMYRGKKRHE--MPPHIYAISE---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 160 ----SAYRCMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKPQGEL----------- 224
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSEETCKVSGSTRQPKIKLftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 225 ----------------------------------------------------------------ERQL------------ 228
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 229 ----LQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHI 293
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 294 FYQLLSGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHEEILSMLK 358
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 359 VVSSVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVE 432
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 433 ALAKATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQl 496
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 497 fnhtmfileqEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVEKLVQE 566
Cdd:cd14894 565 ----------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 567 QGSHSKfQKPRQLKDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRiv 636
Cdd:cd14894 635 NSSRLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ-- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 637 gLDQVTGMTETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 716
Cdd:cd14894 712 -LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIR 789
|
....*.
gi 1039738675 717 GIRICR 722
Cdd:cd14894 790 QMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1331-1896 |
1.82e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.42 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1331 QELLQEETRQKLNLSS-RIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1409
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1410 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1489
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1490 EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATE 1569
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------RLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1570 DAKLRLEvnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKA 1649
Cdd:COG1196 449 EEEAELE--------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1650 RdeVIKQLRKLQAQMKDYQRELEEARASR--------DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERD 1721
Cdd:COG1196 521 G--LAGAVAVLIGVEAAYEAALEAALAAAlqnivvedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1722 ELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLE 1801
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1802 RQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQ 1881
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 1039738675 1882 M---EKANARMKQLKRQL 1896
Cdd:COG1196 759 PpdlEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
854-1716 |
1.62e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.47 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 854 LLQVTRQEEELQAKDEEllkVKEKQTKVEGELEEMERkHQQLLEEKNILA--EQLQAETELFAEAEEMRARLAAKKQELE 931
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 932 EILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGarqKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEK 1011
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG---ELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1012 KLMEDRIAECSSQLAEEE-EKAKNLAKIRNKQEVM---ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQ 1087
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERkRRDKLTEEYAELKEELedlRAELEEVDKEFAETRDELKDYREKLE----KLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1088 VD---ELKVQLTKKEEELQGALARGDDetlhKNNALKVARE-LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1163
Cdd:TIGR02169 408 LDrlqEELQRLSEELADLNAAIAGIEA----KINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1164 ELE------DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELS----------------EQ 1221
Cdd:TIGR02169 484 ELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAgnrlnnvvveddavakEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1222 LEQAKRFKAN----LEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQN 1297
Cdd:TIGR02169 564 IELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF------GDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1298 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklNLSSRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVL 1377
Cdd:TIGR02169 638 KYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQSE-------LRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1378 ALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1457
Cdd:TIGR02169 706 ELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1458 KKQKKFDQLLAEEKGISARyaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNV 1537
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1538 HELEKSKRALEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqferDLQTRDEQNEEKKRLLLKQVRELEAELED 1617
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1618 ERKQRALAVASKKKMEIDLKDLEAQIeAANKARDEVIKQLRKLQAQMKDYQRELEE-------ARASRDEIFAQSKESEK 1690
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKE 993
|
890 900
....*....|....*....|....*.
gi 1039738675 1691 KLKSLEAEILQLQEELASSERARRHA 1716
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
817-1459 |
1.87e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 817 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRvftkvkplLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQL 895
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELE--------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 896 LEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdlesrveeeeeRNQILQNEKKKMQAHIQDLEEQLDEEEGA 975
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------------RLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 976 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK 1055
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1056 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQE 1135
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1136 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAL 1215
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1216 EELSEQLEQAKRFKANLeknkqGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKL 1295
Cdd:COG1196 586 AALAAALARGAIGAAVD-----LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1296 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQ 1375
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1376 VLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALsqrleEKV--LA---YDKLEKTKNRLQQELDDLTVDLDHQR 1450
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-----GPVnlLAieeYEELEERYDFLSEQREDLEEARETLE 815
|
....*....
gi 1039738675 1451 QIVSNLEKK 1459
Cdd:COG1196 816 EAIEEIDRE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
869-1750 |
2.37e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.08 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 869 EELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlAAKKQELEEILHDLEsrVEEEEERN 948
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 949 QILQNEKKKMQAHIqdleeqldeeegARQKLQLEKVTAE--AKIKKMEEEVLLLEDQNSKFikeKKLMEDRIAECSSQLA 1026
Cdd:TIGR02169 233 EALERQKEAIERQL------------ASLEEELEKLTEEisELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1027 EEEEKAKNLAKIrnkqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1106
Cdd:TIGR02169 298 ELEAEIASLERS-------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1107 ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEV 1186
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE---AKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1187 AELKKAlEDETKNHEAQIQDMRQRH---ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLqqvkaesEHK 1263
Cdd:TIGR02169 448 LEIKKQ-EWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1264 RKKLDAQVQELhAKVSEGDRLRVELAekankLQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLN 1343
Cdd:TIGR02169 520 IQGVHGTVAQL-GSVGERYATAIEVA-----AGNRLNNVVVEDDAVAKEAIELLK-----RRKAGRATFLPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1344 LSSRIRqleeeknslqeqqeeeeearknlEKQVLALQSQLADTKKK-------VDDDLGTIESLEEAKKKL--------- 1407
Cdd:TIGR02169 589 DLSILS-----------------------EDGVIGFAVDLVEFDPKyepafkyVFGDTLVVEDIEAARRLMgkyrmvtle 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1408 ----------------LKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK----QKKF 1463
Cdd:TIGR02169 646 gelfeksgamtggsraPRGGILFSRSEPAELQRLrerlEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1464 DQLLAEEKGISARYAEERDRAEAEAREKETKALSLARaleeALEAKEEFERQNKQLRADMEDLMSSKDDVGknVHELEKS 1543
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE----LEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1544 KRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRA 1623
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1624 LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE------SEKKLKSLEA 1697
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQA 958
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1698 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:TIGR02169 959 ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1116-1891 |
5.65e-24 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 110.59 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1116 KNNALKVARELQAQIAELQEDFESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALED 1195
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1196 ETKNHEAQiqdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD--NKELACEVKVLQQVKAESEHKR--------- 1264
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvDFEEASGKKIYEHDSMSTMHFRslgsaiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1265 -KKLDAQVQELHAKV-SEGDRLRVELAEKANK----LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ---LQDTQELLQ 1335
Cdd:pfam15921 226 lRELDTEISYLKGRIfPVEDQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1336 EETRQKLnlSSRIRQLEEeknslqeqqeeeeearknLEKQVLALQSQLADTKKKVDDdlgTIESLEeaKKKLLKDVEALS 1415
Cdd:pfam15921 306 EQARNQN--SMYMRQLSD------------------LESTVSQLRSELREAKRMYED---KIEELE--KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1416 QRLEEkvlayDKLEKTKNRLQQELDDLTVDLdHQRQIVSNLEKKQKKfdQLLAEEKGISARYAEERdraeaeaREKETKA 1495
Cdd:pfam15921 361 ARTER-----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNK--RLWDRDTGNSITIDHLR-------RELDDRN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1496 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1575
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1576 EVNMQAMKAqferdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKD-----LEAQIE-----A 1645
Cdd:pfam15921 506 QEKERAIEA-------TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDkvieiLRQQIEnmtqlV 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1646 ANKARDEVIKQLRK--LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1723
Cdd:pfam15921 579 GQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1724 ADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELLNDRFRKTTLQVDT----LNTELAAERSAAQKSDNARQQ 1799
Cdd:pfam15921 659 LNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKS 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1800 LERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERaaanKLVRRTEKKLKEIFMQVEDERRHADQYK 1879
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
810
....*....|..
gi 1039738675 1880 EQMEKANARMKQ 1891
Cdd:pfam15921 793 EVLRSQERRLKE 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
856-1554 |
4.05e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.83 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 935
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 936 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ-----LEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1010
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieeLLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1011 KKLMEDRIAECSSQLAEEEEK----AKNLAKIRNKQEvMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI---AE 1083
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQAldaaERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1084 LQAQVDelkvqlTKKEEELQGALARGDD------ETLHKNNALKVA---------RELQAQIAELQEDFESEKASRNKAE 1148
Cdd:TIGR02168 535 YEAAIE------AALGGRLQAVVVENLNaakkaiAFLKQNELGRVTflpldsikgTEIQGNDREILKNIEGFLGVAKDLV 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1149 KQKRDLSEELEAL--KTELEDTLDTTAAQQEL-------------------------------RTKREQEVAELKKALEd 1195
Cdd:TIGR02168 609 KFDPKLRKALSYLlgGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIE- 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1196 ETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELH 1275
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1276 AKVSEGDRLRVELAEKANKLQNELDNVSTLLEEaekkgikfakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1355
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKA--------------LREALDELRAELTLLNEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1356 NSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL 1435
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1436 QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFER 1514
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1039738675 1515 QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1554
Cdd:TIGR02168 987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1141-1750 |
1.54e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1141 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ-------QELRTKREQEVAELKKALEDETKNHEAQIQDMRQR 1210
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEdilGELERQLEPLERQaekaeryRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1211 HATALEELSEQLEQAkrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1290
Cdd:COG1196 251 LEAELEELEAELAEL---EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1291 KANKLQNELDNVSTL----------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQE 1360
Cdd:COG1196 328 LEEELEELEEELEELeeeleeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1361 QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1440
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1441 DLTVDLDHQRQIVSNLEKKQK--KFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA----RALEEALEAKEEFER 1514
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnivVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1515 QNKQLRA------DMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER 1588
Cdd:COG1196 568 AAKAGRAtflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1589 DLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1668
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1669 RELEEARASRDEIFAQSK----ESEKKLKSLEAEILQLQEELASSERARRH-------AEQERDELADEIANSASGKSAL 1737
Cdd:COG1196 728 EQLEAEREELLEELLEEEelleEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDL 807
|
650
....*....|...
gi 1039738675 1738 LDEKRRLEARIAQ 1750
Cdd:COG1196 808 EEARETLEEAIEE 820
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1324-1940 |
4.95e-21 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 101.02 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1324 ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEeeeeARKNLEKQVLALQSQLADTKKKVDDDLGTIES---- 1399
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETELCAEAEEMRARLAARKQELEEILHELESrlee 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1400 -------LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEekg 1472
Cdd:pfam01576 87 eeersqqLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1473 isaryaeerdrAEAEAREKETKALSLARALEealeakeeferQNKQLRADMEDLMSSKDdvgKNVHELEKSKRALEQQVE 1552
Cdd:pfam01576 164 -----------FTSNLAEEEEKAKSLSKLKN-----------KHEAMISDLEERLKKEE---KGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1553 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKM 1632
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1633 EIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELE-EARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1711
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1712 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQ 1791
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1792 KSDNARQQLERQNKELKAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1871
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1872 RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1730 |
1.17e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 859 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEleEILHDLE 938
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE--EVRKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 939 SRVEeeeernqilQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRI 1018
Cdd:PTZ00121 1193 LRKA---------EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1019 AECSSQLAEEEEKAKNLAKIRNKQEVMISDleERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKK 1098
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK----KK 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1099 EEELQGALARGDDETLHKNNALKVARElQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQEL 1178
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1179 RTKREqevaELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelACEVKVLQQVKA 1258
Cdd:PTZ00121 1417 KKKAD----EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADEAKK 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1259 ESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNEldnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET 1338
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1339 RQKlnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK----KKVDDDLGTIESLEEAKKKlLKDVEAL 1414
Cdd:PTZ00121 1563 KKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKAEEE-KKKVEQL 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1415 SQRLEEKVLAYDKLEKTknrlqqelddltvdlDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETK 1494
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---------------EEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAE 1699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1495 AlslARALEEALEAKEEFERQNKQLRADMEDLMSskddvgkNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLR 1574
Cdd:PTZ00121 1700 E---AKKAEELKKKEAEEKKKAEELKKAEEENKI-------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1575 LEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEidlkdleaqieaankarDEVI 1654
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-----------------DSAI 1832
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1655 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSleaEILQLQEELASSERARRHAEQERDELADEIANS 1730
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNK---EKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1606-1896 |
2.01e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.86 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1606 KQVRELEAELEdeRKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQS 1685
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1686 KESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1765
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1766 NDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAK 1845
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1846 ERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1896
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
857-1726 |
2.02e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 95.81 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 857 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlAAKKQELEEILHD 936
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 937 LESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1016
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1017 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKrkldgettDLQDQIAELQAQVDELKVQLT 1096
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE--------EELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1097 KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDF-ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaq 1175
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLlKEEKKEELEILEEEEESIELKQGKLTEEKEELEK---- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1176 QELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ 1255
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1256 VKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ 1335
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1336 EETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALS 1415
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1416 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerdrAEAEAREKETKA 1495
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE------------EEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1496 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1575
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1576 EVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVI 1654
Cdd:pfam02463 844 EEQKLEKLAEEElERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1655 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKsleaEILQLQEELASSERARRHAEQERDELADE 1726
Cdd:pfam02463 924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN----KRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1466 |
2.32e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.52 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 846 RVFTKVKPLLQVTRQEEELqaKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQL-QAETELFAEAEEM----- 919
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLaKLEAEIDKLLAEIeeler 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 920 --------RARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIK 991
Cdd:TIGR02169 344 eieeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 992 KMEEEVLLLEDQNSKFIKEKKLMEDRIaecssqlAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLD 1071
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEI-------KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1072 GETTDLQDQIAELQAQVDELK----------VQLTKKEEELQGALargddETLHKNNALKVARELQAQIAELQEDFESEK 1141
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKasiqgvhgtvAQLGSVGERYATAI-----EVAAGNRLNNVVVEDDAVAKEAIELLKRRK 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1142 ASR------NKAEKQKRDLSEELE-------------------ALKTELEDTL---DTTAAQQELRTKR----EQEVAE- 1188
Cdd:TIGR02169 572 AGRatflplNKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYVFGDTLvveDIEAARRLMGKYRmvtlEGELFEk 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1189 ----------------LKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKV 1252
Cdd:TIGR02169 652 sgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1253 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEkkgikfakdAAGLESQLQDTQE 1332
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLE---------ARLSHSRIPEIQA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1333 LLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVE 1412
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1413 ALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL-EKKQKKFDQL 1466
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1304-1940 |
2.23e-18 |
|
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: 92.43 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1304 TLLEEAekKGI-KFAKDAAGLESQLQDTQELLQeetRQKLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEKQVLALQ 1380
Cdd:TIGR02168 159 AIFEEA--AGIsKYKERRKETERKLERTRENLD---RLEDILNELERQLKslERQAEKAERYKELKAELRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1381 sqLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTvdldhqrQIVSNLEKKQ 1460
Cdd:TIGR02168 234 --LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-------NEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1461 KKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL 1540
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1541 EKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDERK 1620
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERL-----------------QQEIEELLKKLEEAELKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1621 QRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK--LKSLEAE 1698
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1699 ILQLQE--ELASSERARRHAEQ---ERDELADEI----ANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRF 1769
Cdd:TIGR02168 528 LISVDEgyEAAIEAALGGRLQAvvvENLNAAKKAiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1770 RKTTLQ--------------VDTLNTELAAERS-----------------------AAQKSDNARQQLERQNKELKAKLQ 1812
Cdd:TIGR02168 608 VKFDPKlrkalsyllggvlvVDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1813 ELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQL 1892
Cdd:TIGR02168 688 ELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039738675 1893 KRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1430 |
2.86e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 91.66 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 860 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEqLQAETElfaEAEEMRARLAAKKQELEEILHDLES 939
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 940 RVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEVLLLEDQNSkfikEKKLMEDRIA 1019
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1020 ECSSQLAEEEEKAKNLAKIRNKQEVMisdleERLKKEEKTR---------QELEKAKRKLDGETTDLQDQIAELQAQVDE 1090
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEEL-----ERLKKRLTGLtpeklekelEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1091 LKvqltKKEEELQGAlargddetlhKNNALKVARELQAQiaELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1170
Cdd:PRK03918 424 LK----KAIEELKKA----------KGKCPVCGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1171 TTAAQQELRtkREQEVAELKKALEDETKNHEAQiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETD---NKELA 1247
Cdd:PRK03918 488 VLKKESELI--KLKELAEQLKELEEKLKKYNLE----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1248 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKfakdaagLESQL 1327
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-------LEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1328 QDTQELLQEETRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1402
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
570 580 590
....*....|....*....|....*....|
gi 1039738675 1403 AKKKLLKDVEALS--QRLEEKVLAYDKLEK 1430
Cdd:PRK03918 709 AKKELEKLEKALErvEELREKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
855-1494 |
9.45e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 9.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 855 LQVTRQEEELQaKDEELLKVKEKQTKVEGELEEMERKHQQLLE-EKNILAEQLQAETELFAEAEEmrARLAAKKQELEEI 933
Cdd:PTZ00121 1178 AEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 934 LHDLESRVEEEEERNQILQNEKKKM-----QAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----IKKMEEEVLLLEDQN 1004
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKadelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1005 SKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK--EEKTRQELEKAKRKLDGETTDLQDQIA 1082
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1083 ELQAQVDEL--KVQLTKKEEEL--QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS--RNKAEKQKRDlSE 1156
Cdd:PTZ00121 1415 AAKKKADEAkkKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1157 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataleelSEQLEQAKRFKANLEKNK 1236
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--------ADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1237 qgleTDNKELACEVKVLQQVKAESEHKRKKldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTllEEAEKKGIKF 1316
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQ 1637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1317 AKDAAglESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlalQSQLADTKKKVdddlgt 1396
Cdd:PTZ00121 1638 LKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-----LKKEAEEAKKA------ 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1397 iESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISAR 1476
Cdd:PTZ00121 1705 -EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 1039738675 1477 YAEERDRAEAEAREKETK 1494
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1213-1932 |
1.50e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 89.59 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1213 TALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKAESEhKRKKLDAQVQELHAkvsEGDRLRVELAE-K 1291
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELAE-RYAAARERLAELEY---LRAALRLWFAQrR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1292 ANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLS-SRIRQLEEEKNSLQEQQEEEEEARK 1370
Cdd:COG4913 290 LELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1371 NLEKQVLALQSQLADTKkkvdddlgtiESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1450
Cdd:COG4913 363 RLEALLAALGLPLPASA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1451 QIVSNLEKKQKKFDQLLAEEKGISA---RYA------EERDRAEAEAREKE--TKALSLARALEEALEAKEEFERQNKQL 1519
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEaelPFVgelievRPEEERWRGAIERVlgGFALTLLVPPEHYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1520 RADMEdlmsskdDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedaklRLEVNMQAMKAQFERDLQTrdeqneE 1599
Cdd:COG4913 513 RLVYE-------RVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDYVCVDSPEELRR------H 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1600 KKRL----LLKQVRELeAELEDERKQRALAV----ASKKkmeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1671
Cdd:COG4913 574 PRAItragQVKGNGTR-HEKDDRRRIRSRYVlgfdNRAK-----LAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1672 EEARAsrdeiFAQSKESEKKLKSLEAEILQLQEELASSERAR---RHAEQERDELADEIANSASGKSALLDEKRRLEARI 1748
Cdd:COG4913 648 EALQR-----LAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1749 AQLEEELEEEQSNMELLNDRFRK-TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV---KSKFKA 1824
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMrafNREWPA 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1825 TISALEAKIGQLEE------QLEQE---AKERAAANKLVRRTEKKLKEIFMQVEDERRHAdqyKEQMEKANARMKQLK-- 1893
Cdd:COG4913 803 ETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPfg 879
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1039738675 1894 --RQLeeAEEEATRANASRRKLQRELDDATEANEGLSREVS 1932
Cdd:COG4913 880 pgRYL--RLEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
987-1586 |
1.80e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.92 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 987 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKA 1066
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1067 KRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEEL---QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS 1143
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1144 RNKAEKQKRDLSEELEALKTELEDT----LDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRqrhaTALEELS 1219
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTqtqlNQLKDEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQLK----SEISDLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1220 EQLEQ--AKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKkldaqvqELHAKVSEGDRLRVELAEKANKLQN 1297
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1298 ELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1377
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQIND----LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1378 ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1457
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1458 KKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKALSLaraleeaLEAKEEFERQNKQLRADMEDLMSSKDDVGK 1535
Cdd:TIGR04523 531 SEKKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1536 NVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF 1586
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1406 |
2.10e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 838 KLRHWQWWRVFTKVKPLLQVTRQ---EEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQAETELFA 914
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 915 EAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----- 989
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaee 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 990 IKKMEEEVLLLEDQNSKFIKEKKLMED-RIAECSSQLAEEEEKAKNLAKirnKQEVMISDLEERLKKEEKTRQELEKAKR 1068
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1069 KLDGETTDLQDQIAELQAQVDELK--VQLTKKEEELQGALARGDDETLHKNNALKVARELQaQIAELQEDFESEKASRNK 1146
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1147 AEKQKRdlseELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAlEELSEQLEQAK 1226
Cdd:PTZ00121 1559 KAEEKK----KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1227 RF----KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQElhakvsEGDRLRVELAEKANKLQNELDNV 1302
Cdd:PTZ00121 1634 KVeqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAEEL 1707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1303 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1382
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
570 580 590
....*....|....*....|....*....|...
gi 1039738675 1383 LADTK---------KKVDDDLGTIESLEEAKKK 1406
Cdd:PTZ00121 1784 ELDEEdekrrmevdKKIKDIFDNFANIIEGGKE 1816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
865-1565 |
4.24e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 865 QAKDEELLKVKEKQTKVEGE---LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH---DLE 938
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQilgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 939 SRVEEEEERNQILQNEKKKMQAHiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEVllledqnskfikekKLMEDRI 1018
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEEL-----------KEEIEELEKELESLEGSKRKLEEKI--------------RELEERI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1019 AECSSQLAEEEEKAKNLAKIRNKQEVMISdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvQLTKK 1098
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1099 EEELQGALARgdDETLHKnnALKVARELQAQIAELqedfeSEKASRNKAEKQKRDLsEELEALKTELEDTLDTTAAQqel 1178
Cdd:PRK03918 347 LKELEKRLEE--LEERHE--LYEEAKAKKEELERL-----KKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITAR--- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1179 RTKREQEVAELKKALEdetknheaQIQDMRQRHATALEELSEqlEQAKRFKAnleknkqgletdnkELACEVKVLQQVKA 1258
Cdd:PRK03918 414 IGELKKEIKELKKAIE--------ELKKAKGKCPVCGRELTE--EHRKELLE--------------EYTAELKRIEKELK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1259 ESEHKRKKLDAQVQELHAKVSEGDRLRV--ELAEKANKLQNELDNVStlLEEAEKKGIKFakdaaglesqlqdtqellqE 1336
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYN--LEELEKKAEEY-------------------E 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1337 ETRQKLN-LSSRIRQLEEEKNSLQEQQEEeeeaRKNLEKQVLALQSQLADTKKKvdddlgtiesLEEAKKKLLKDVEALS 1415
Cdd:PRK03918 529 KLKEKLIkLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKE----------LEELGFESVEELEERL 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1416 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEErdraeaEAREKETKA 1495
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEY 668
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1496 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEqQVEEMRTQLEELEDEL 1565
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1397-1940 |
6.37e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1397 IESLEEAKKKLLKDVEALSQRLEEKVLaYDKLektkNRLQQELDDLTVDLDHqrqivsnLEKKQKKFDQLLAEEKGISAR 1476
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDL-HERL----NGLESELAELDEEIER-------YEEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1477 YAEERDRAE------AEAREK----ETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA 1546
Cdd:PRK02224 246 HEERREELEtleaeiEDLRETiaetEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1547 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK---AQFERDLQTRDEQNEEKKrlllKQVRELEAELEDERKQRA 1623
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRR----EEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1624 LAvaskkkmEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDE--------------IFAQSKESE 1689
Cdd:PRK02224 402 DA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1690 KKLKSLEAEILQLQEELASSErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRf 1769
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1770 rkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfkATISALEAKIGQLEEQLEqeakeraa 1849
Cdd:PRK02224 546 ------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-------- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1850 anklvRRTEKKlkEIFMQVEDERRhadqykEQMEKANARMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEAN 1924
Cdd:PRK02224 610 -----RLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570
....*....|....*.
gi 1039738675 1925 EGLSREVSTLKNRLRR 1940
Cdd:PRK02224 677 DDLQAEIGAVENELEE 692
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
952-1883 |
7.17e-17 |
|
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: 87.33 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 952 QNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKME-------EEVLLLEDQNSKFIKEKKLmedriaecSSQ 1024
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLkekleleEEYLLYLDYLKLNEERIDL--------LQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1025 LAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLdgettdLQDQIAELQAQVDELKVQLTKKEEELQG 1104
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1105 ALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ 1184
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1185 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEqakrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR 1264
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-----SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1265 KKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNL 1344
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1345 SSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLA 1424
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1425 YDKLEKTKNRLQQELDDlTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEE 1504
Cdd:pfam02463 634 LTKLKESAKAKESGLRK-GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1505 ALEAKEEFERQNKQLRADMEDLmsskddvgknvhelekSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1584
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKI----------------NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1585 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQaqm 1664
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE--- 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1665 kdyqrelEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIansasgkSALLDEKRRL 1744
Cdd:pfam02463 854 -------EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL-------NLLEEKENEI 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1745 EARIAQLEEELeeeqsnmellndrfrkttLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1824
Cdd:pfam02463 920 EERIKEEAEIL------------------LKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1825 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQME 1883
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
990-1805 |
1.08e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 990 IKKMEEevLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1069
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1070 LDGETTDLQDQIAELQAQV---DELKVQLTKKEEELQGAL-ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1145
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKkaeDARKAEEARKAEDARKAEeARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1146 KAEKQKRDlseelEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1225
Cdd:PTZ00121 1184 AEEVRKAE-----ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1226 KRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLQNELDNVSTL 1305
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1306 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssrirqlEEEKNSLQEQQEEEEEARKNLEkqvlaLQSQLAD 1385
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----------EEAKKKADAAKKKAEEKKKADE-----AKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1386 TKKKVDDdlgtIESLEEAKKKllkdVEALSQRLEEKVLAyDKLEKtKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQ 1465
Cdd:PTZ00121 1403 DKKKADE----LKKAAAAKKK----ADEAKKKAEEKKKA-DEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1466 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKE-EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1544
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1545 RALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLK--QVRELEAELEDERKQR 1622
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEK 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1623 ALAVASKKKMEIDLKDLEA--QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK---LKSLEA 1697
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeeLKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1698 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRrleaRIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1777
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
810 820
....*....|....*....|....*...
gi 1039738675 1778 TLNTELAAERSAAQKSDNARQQLERQNK 1805
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1124-1731 |
4.08e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.97 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1124 RELQAQIAELQEDFESEKASRNKAEK--QKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknHE 1201
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA---EL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1202 AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE-LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSE 1280
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1281 GDRlrvELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQE 1360
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEE-------ALAEAEAALRDLRR--------------ELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1361 QqeeeeeaRKNLEKQVLALQSQLADTKKKVDDDL-----------------GTIESL-----------EEAKKKLLKDVE 1412
Cdd:COG4913 434 R-------KSNIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1413 ALSQRLE---EKVLAYDKLEKT-----------------------KNRLQQELDDLTVD----LDHQR-------QIVSN 1455
Cdd:COG4913 507 RLHLRGRlvyERVRTGLPDPERprldpdslagkldfkphpfrawlEAELGRRFDYVCVDspeeLRRHPraitragQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1456 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKEtKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG- 1534
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1535 --KNVHELEKSKRALEQ---QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVR 1609
Cdd:COG4913 666 aeREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1610 ELEAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEVIKQLRKLqaqMKDYQRELEEARASRDEIFAQSKESE 1689
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYL 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039738675 1690 KKLKSLEAEIL-QLQEELAssERARRHAEQERDELADEIANSA 1731
Cdd:COG4913 819 ALLDRLEEDGLpEYEERFK--ELLNENSIEFVADLLSKLRRAI 859
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
976-1603 |
7.82e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.20 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 976 RQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKF-----IKEKKLMEDRIAECSSQLAEEEEKaknlakirnkqevmISDL 1049
Cdd:COG4913 249 EQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAE--------------LERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1050 EERLKKEEKTRQELEKAKRKLDGettdlqDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQ 1129
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1130 IAELQEDFESEKAS----RNKAEKQKRDLSEELEALKTELEdtldttaaqqELRTKR---EQEVAELKKALEDETKNHEA 1202
Cdd:COG4913 389 AAALLEALEEELEAleeaLAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1203 QIQ------DMRQRHA---TALEEL-----------SEQLEQAKRFkanLEKNKQGLETdnkelacevkVLQQVKAESEH 1262
Cdd:COG4913 459 ELPfvgeliEVRPEEErwrGAIERVlggfaltllvpPEHYAAALRW---VNRLHLRGRL----------VYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1263 -KRKKLDAQ--VQELHAKVSE-GDRLRVELAEKANKLQneLDNVSTLleEAEKKGI-----------KFAKDAagleSQL 1327
Cdd:COG4913 526 pERPRLDPDslAGKLDFKPHPfRAWLEAELGRRFDYVC--VDSPEEL--RRHPRAItragqvkgngtRHEKDD----RRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1328 QDTQELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ--SQLADTKKKVDDDLGTIESLEEAK 1404
Cdd:COG4913 598 IRSRYVLGFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1405 KKLLK---DVEALSQRLEEKVLAYDKLEKTKN-------RLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgis 1474
Cdd:COG4913 678 ERLDAssdDLAALEEQLEELEAELEELEEELDelkgeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER--- 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1475 aRYAEERDRAEAEAREKETKALSLARaleealeakeefeRQNKQLRADMEDLMSS-KDDVGKNVHELEKSKRALEqQVEE 1553
Cdd:COG4913 755 -FAAALGDAVERELRENLEERIDALR-------------ARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLA 819
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1554 MRTQLEelEDEL-QATEDAKLRLEVNMQAMKAQFERDLqtRDEQNEEKKRL 1603
Cdd:COG4913 820 LLDRLE--EDGLpEYEERFKELLNENSIEFVADLLSKL--RRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1214-1939 |
8.46e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1214 ALEELSEQLEQAKRFKANLEKNKQGLET--DNKELACEVKVLQQVKAESE-----HKRKKLDAQVQELHAKVSEGDRLRV 1286
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1287 ELAEKANKLQNELDNVSTLLEEAEKK--------GIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1358
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1359 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1438
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1439 LDDLTVDLDHQRQIVSNLEKKQKKFDqllaeekgisaryaEERDRAEAEAREKETKALSLAraleealEAKEEFERQNKQ 1518
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWKLEQLA-------ADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1519 LRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAT-----------EDAKLRLEV----NMQAMK 1583
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgERYATAIEVaagnRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1584 AQFERDLQTRDEQNEEKKR-----LLLKQVRELEAELEDERKQRALAVAskkkmeIDLKDLEAQIEAANK--ARDEVIKQ 1656
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRKAgratfLPLNKMRDERRDLSILSEDGVIGFA------VDLVEFDPKYEPAFKyvFGDTLVVE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1657 ----LRKL--QAQMKDYQRELEE--------ARASRDEIFAQSKESEKkLKSLEAEILQLQEELASSERARRHAEQERDE 1722
Cdd:TIGR02169 628 dieaARRLmgKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1723 LadeiansasgKSALLDEKRRLEARiaqleeeleeeQSNMELLNDRFRKttlqvdtLNTELAAERSAAQKSDNARQQLER 1802
Cdd:TIGR02169 707 L----------SQELSDASRKIGEI-----------EKEIEQLEQEEEK-------LKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1803 QNKELKAKLQELEgAVKSKFKATISALEAKIG-----QLEEQLEQEAKERAAANKLVRRTEKKLKEIFM---QVEDERRH 1874
Cdd:TIGR02169 759 ELKELEARIEELE-EDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQE 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1875 ADQY----KEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELddateanEGLSREVSTLKNRLR 1939
Cdd:TIGR02169 838 LQEQridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL-------GDLKKERDELEAQLR 899
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
854-1439 |
3.01e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 854 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELE----EMERKHQQLLEEK-NILAEQLQAETELFAEAEEMRARLAAKKQ 928
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERVLSDQRGSLDqlkaQIEEKEEKDLHERlNGLESELAELDEEIERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 929 ELEEILHDLESRveeeEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLL-------LE 1001
Cdd:PRK02224 238 EADEVLEEHEER----REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1002 DQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI 1081
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1082 AELQAQVDELKVQLTKKEEELQGALARGDDetLHKNNA-----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSE 1156
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDE--LREREAeleatLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1157 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRQRHATALEELSEQLEQAkrfkANLEKNK 1236
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERA----EELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1237 QGLEtdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNeLDNVSTLLEEAEKKGikf 1316
Cdd:PRK02224 547 AELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE--- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1317 aKDAAGLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEKNslQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLG 1395
Cdd:PRK02224 606 -DEIERLREKREALAE-LNDERRERLaEKRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1396 TIESLEEAKKKL------LKDVEALSQRLEEKVLAYDKLEKTKNRLQQEL 1439
Cdd:PRK02224 682 EIGAVENELEELeelrerREALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1290-1896 |
3.42e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.65 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1290 EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEAR 1369
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1370 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDVEALSQRLEEKVLAYDKLEK-------TKNRLQQELD 1440
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKLSEfyeeyldELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1441 DLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAlslaraleealeakeeferQNKQLR 1520
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-------------------ELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1521 ADMEDLmsSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQTRDEQNEEK 1600
Cdd:PRK03918 379 KRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1601 KRLLlkqvRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR--DEVIKQLRKLQAQMKDYQRE-LEEARAS 1677
Cdd:PRK03918 451 KELL----EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1678 RDEIFAQSKESEKKLKSLEAEILQLQE---ELASSERARRHAEQERDELADEIANSASGKSALLDEKrrleariaqleee 1754
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEER------------- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1755 leeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1834
Cdd:PRK03918 594 ----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1835 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEdERRHADQYKEQMEKANARMKQLKRQL 1896
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKV 730
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1267-1838 |
5.14e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1267 LDAQVQELHAKvsegdrlrvELAEKANKLQNELDNVSTLLEEAEKKgikfaKDAAglESQLQDTQELLQ--EETRQklnl 1344
Cdd:PRK02224 192 LKAQIEEKEEK---------DLHERLNGLESELAELDEEIERYEEQ-----REQA--RETRDEADEVLEehEERRE---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1345 ssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIEsLEEAkkkllkDVEALSQRLEEkvla 1424
Cdd:PRK02224 252 --ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-LDDA------DAEAVEARREE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1425 ydkLEKTKNRLQQELDDLTVDL-DHQRQIvsnlekkqkkfdqllaeekgisARYAEERDRAEAEAREKETKALSLARALE 1503
Cdd:PRK02224 319 ---LEDRDEELRDRLEECRVAAqAHNEEA----------------------ESLREDADDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1504 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK 1583
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1584 A-------QFERDLQTRDEQNEekkrlllkQVRELEAELEDERKQRAlAVASKKKMEIDLKDLEAQIEAANKARDEVIKQ 1656
Cdd:PRK02224 454 CpecgqpvEGSPHVETIEEDRE--------RVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1657 LRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADeIANSASGKSA 1736
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIAD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1737 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQELEg 1816
Cdd:PRK02224 604 AEDEIERLREKREALAELNDERRERLAEKRER-------KRELEAEFDEARIEEARED--KERAEEYLEQVEEKLDELR- 673
|
570 580
....*....|....*....|..
gi 1039738675 1817 AVKSKFKATISALEAKIGQLEE 1838
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEE 695
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
856-1703 |
5.99e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.25 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleeKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 935
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI---KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 936 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfikekklme 1015
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR------------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1016 driaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQL 1095
Cdd:TIGR00606 377 -------LELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1096 TKKEEELQGALARGDDETLHKNNALKVARELQAQIAELqedfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1175
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1176 QELRTKREQEVAELKKALEDETKNHEaQIQDMRQRHATALEELSEQLEQAKRFKA---NLEKNKQGLETDNKELACEVKV 1252
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQTRDRLAKLNKELAS 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1253 LQQVKAESEHKRKKLDAQVQELHAKVSEgdrlrvelAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQE 1332
Cdd:TIGR00606 603 LEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1333 -------LLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1405
Cdd:TIGR00606 675 enqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1406 KLLKDVEALSQRLEEKvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1485
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1486 AEarEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEleksKRALEQQVEEMRTQLEELEDEL 1565
Cdd:TIGR00606 831 KQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1566 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQN---EEKKRLLLKQVRELEAELED-ERKQRALAVASKKKMEIDLKDLEA 1641
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1642 QIEAANKARDEVIKQLRKLQAQM--KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1703
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1135-1876 |
1.17e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1135 EDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQrhata 1214
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1215 lEELSEQLEQAKRfkanLEKNKQGLETDNkelACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1294
Cdd:PTZ00121 1166 -AEEARKAEDAKK----AEAARKAEEVRK---AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1295 LQNELDNVstlleEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNSlqeqqeeeEEARKNLEK 1374
Cdd:PTZ00121 1238 DAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKA--------DEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1375 QVLALQSQLADTKKKVDDdlgTIESLEEAKKKllkdVEALSQRLEEKvlaYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1454
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADE---AKKKAEEAKKK----ADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1455 NLEKKQKKFDQllAEEKGISARYAEERDRAEAEAREK--ETKALSLARALEEALEAKEEFERQNKQLRADMEDlmSSKDD 1532
Cdd:PTZ00121 1372 KKEEAKKKADA--AKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--AKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1533 VGKNVHELEKSKRALEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFERDLQTRDEQNEEKKRLLLKQVRE 1610
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1611 LEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1690
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1691 KLKSLEA----EILQLQEELASSERARRHAEQERDELADEIANS---------ASGKSALLDEKRRLEARIAQLEEELEE 1757
Cdd:PTZ00121 1606 KMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1758 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQqlERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLE 1837
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
730 740 750
....*....|....*....|....*....|....*....
gi 1039738675 1838 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHAD 1876
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
850-1442 |
3.04e-14 |
|
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: 78.86 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 850 KVKPLLQVTRQEEELQAKDEELL-KVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFA-EAEEMRARLAA 925
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHtELQSKMRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRdAHEVATSIREI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 926 KKQELEEI--LHDLESRVEEEEERNQILQNEKKKMQAhiqdLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQ 1003
Cdd:TIGR00618 371 SCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQR----EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1004 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIrnkqevmisdleerLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1083
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI--------------HLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1084 LQAqvdelKVQLTKKEEELQGALARGDDETLHKNNALKVAR----ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1159
Cdd:TIGR00618 513 PNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1160 ALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN-----HEAQIQDMRQRHATALEELSEQL------EQAKRF 1228
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLqdvrlHLQQCSQELALKLTALHALQLTLtqervrEHALSI 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1229 KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLdaqvQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEE 1308
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1309 AEKKGIKFAKDA--AGLESQLQDTQELL------QEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1380
Cdd:TIGR00618 744 SLKELMHQARTVlkARTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1381 SQLADTKKKVDDDLgtiesleEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDL 1442
Cdd:TIGR00618 824 ETLVQEEEQFLSRL-------EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1258-1938 |
3.31e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.57 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1258 AESEHKRKKLDAQVQELHAKVsegDRLRVEL--AEKANKLQNELDNVSTLLEEAEKKgiKFAKDAAGLESQLQDTQELLQ 1335
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQL---ERLRRERekAERYQALLKEKREYEGYELLKEKE--ALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1336 EETRQKLNLSSRIRQLEEEKNSLQEQQeeeeeaRKNLEKQVLALQSQLADTKkkvdddlGTIESLEEAKKKLLKDVEALS 1415
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI------KDLGEEEQLRVKEKIGELE-------AEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1416 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKE--- 1492
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRD---KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklk 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1493 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1572
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1573 LRLEVNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELEAELE------------DERKQRALAVASKKKME------- 1633
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1634 ---------------------------------------------IDLKDLEAQIEAANK--ARDEVIKQ----LRKL-- 1660
Cdd:TIGR02169 558 avakeaiellkrrkagratflplnkmrderrdlsilsedgvigfaVDLVEFDPKYEPAFKyvFGDTLVVEdieaARRLmg 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1661 QAQMKDYQRELEE--------ARASRDEIFAQSKESEkKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSAS 1732
Cdd:TIGR02169 638 KYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1733 GKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLER-----QNKEL 1807
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1808 KAKLQELEgAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANA 1887
Cdd:TIGR02169 797 QAELSKLE-EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1888 RMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
989-1815 |
4.50e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 78.16 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 989 KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE----EEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELE 1064
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRT---VREKERELVDCQRELEKLN 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1065 KAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQG--------ALARGDDETLHKNNALKVARELQAQIAELQED 1136
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1137 FESEKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELKKALEDETKNHEAQIQDMRQRH 1211
Cdd:TIGR00606 413 LCADLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAEK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1212 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESehkRKKLDAQVQELHAKVSEGDRLRVELAEK 1291
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1292 ANK--LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL---EEEKNSLQEQQEEEE 1366
Cdd:TIGR00606 570 PNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1367 EARKNLekQVLALQSQLADTK-KKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDD 1441
Cdd:TIGR00606 650 KSSKQR--AMLAGATAVYSQFiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLApdklKSTESELKKKEKRRDE 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1442 LTVDLDHQRQIvsnLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKET--KALSLARALEEALEAKEEFERQNKQL 1519
Cdd:TIGR00606 728 MLGLAPGRQSI---IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDV 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1520 RADMEDLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA---QFERDLQTRd 1594
Cdd:TIGR00606 805 ERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRR- 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1595 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKardevikqlrKLQAQMKDYQRELEEA 1674
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1675 RASRDEIFAQSKES-EKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEE 1753
Cdd:TIGR00606 954 HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1754 ELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE 1815
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1146-1862 |
4.64e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1146 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKK---ALEDETKNHEAQIQDMRQRHATaLEELSEQL 1222
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1223 EQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLQNELDNV 1302
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIREL--------------EERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1303 STLLEEAEKKGIKFAKDAAGLESQLQDTQELlqeetrqklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqVLALQSQ 1382
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1383 LADTKKKVdddlgTIESLEEAKKKLlkdvEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldhqRQIVSNLEKKQKK 1462
Cdd:PRK03918 374 LERLKKRL-----TGLTPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIKEL-------KKAIEELKKAKGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1463 F---DQLLAEE--KGISARYAEERDRAEAEAREKETKaLSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK-N 1536
Cdd:PRK03918 438 CpvcGRELTEEhrKELLEEYTAELKRIEKELKEIEEK-ERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKyN 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1537 VHELEKSKRALEQQVEEMRT---QLEELEDELQatedaklrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEA 1613
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKlkgEIKSLKKELE--------------------------KLEELKKKLAELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1614 ELED-ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDeVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1692
Cdd:PRK03918 571 ELAElLKELEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1693 KSLEAEIlqlqeelasSERARRHAEQERDELADEIAnsasgksalldekrRLEARIAQLEEELEEEQSNMELLNDRFrkt 1772
Cdd:PRK03918 650 EELEKKY---------SEEEYEELREEYLELSRELA--------------GLRAELEELEKRREEIKKTLEKLKEEL--- 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1773 tlqvdtlntelaaersaaQKSDNARQQLERQNKELkAKLQELEGAVKS-KFKATISALeAKIGQLEEQLEQEAKERAAAN 1851
Cdd:PRK03918 704 ------------------EEREKAKKELEKLEKAL-ERVEELREKVKKyKALLKERAL-SKVGEIASEIFEELTEGKYSG 763
|
730
....*....|.
gi 1039738675 1852 KLVRRTEKKLK 1862
Cdd:PRK03918 764 VRVKAEENKVK 774
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
980-1577 |
4.81e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 78.24 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 980 QLEKVTAEAKiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKI-----RNKQEVMISDLEERLK 1054
Cdd:pfam15921 246 QLEALKSESQ-NKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiqeqaRNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1055 KEEKTRQELEKAKRKLDGettdlqdqiaelqaQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1134
Cdd:pfam15921 325 TVSQLRSELREAKRMYED--------------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1135 EDFESEKASRNKAEKQKRDLSEELEALKTELEDtldttaaqqelrtkREQEVAELKKALedetKNHEAQIQDMRQRHATA 1214
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDD--------------RNMEVQRLEALL----KAMKSECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1215 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ---------------------VKAESEHKRKKLDAQVQE 1273
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdltaslqekeraieaTNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1274 LHAKVSEGDRLR----------VELAEKANK---LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ 1340
Cdd:pfam15921 533 LQHLKNEGDHLRnvqtecealkLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1341 KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVlalqsqlADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE 1420
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV-------KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1421 KVlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL-LAEEKGISARyaeerdRAEAEAREKETKALSLA 1499
Cdd:pfam15921 686 KS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDALQSKIQFLEEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1500 raLEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAK 1572
Cdd:pfam15921 757 --MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQES 834
|
....*
gi 1039738675 1573 LRLEV 1577
Cdd:pfam15921 835 VRLKL 839
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1025-1726 |
8.53e-14 |
|
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: 77.32 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1025 LAEEEEKAKNLAKIRNKQEV-MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI--AELQAQVDELKvQLTKKEEE 1101
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYtQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTyhERKQVLEKELK-HLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1102 LQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEK-----QKRDLSEELEALKTELEDTLDTTAAQQ 1176
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1177 ELRTKREQEVAELKKALEDETkNHEAQIQDMRQRHAtALEELSEQLEQAKRFKANLEKNKQgLETDNKELACEVKVLQQV 1256
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1257 KAESEHKRKKLDAQVQELHAKVSEGDRLRVELA----------EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1326
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAhakkqqelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1327 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL-------------EKQVLALQSQLADTKKKVDDD 1393
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1394 LGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdLDHQRQIV-SNLEKKQKKFDQLLAEEKG 1472
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---SEAEDMLAcEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1473 ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK---RALEQ 1549
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQtllRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1550 QVEEMRTQLEELEDELQATEdaklrlevnmqamkaqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASK 1629
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLG------------------SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1630 KKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK----KLKSLEAEILQLQEE 1705
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLK 853
|
730 740
....*....|....*....|.
gi 1039738675 1706 LASSERARRHAEQERDELADE 1726
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL 874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1182-1895 |
1.25e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1182 REQEVAELKKALEDETK-NHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKnkqgletdnKELACEVKVLQQVKAES 1260
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEA---------FGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1261 EHKRKKldaqvqelhAKVSEGDRLRVELAEKANKLQNeldnvstlLEEAEKkgikfAKDAAGLESQLQDTQELLQEETRQ 1340
Cdd:PTZ00121 1114 ARKAEE---------AKKKAEDARKAEEARKAEDARK--------AEEARK-----AEDAKRVEIARKAEDARKAEEARK 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1341 klnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlALQSQLADTKKKVDDdlgtIESLEEAKK-KLLKDVEALSQRLE 1419
Cdd:PTZ00121 1172 ----AEDAKKAEAARKAEEVRKAEELRKAEDARK---AEAARKAEEERKAEE----ARKAEDAKKaEAVKKAEEAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1420 EkvlAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE--KGISARYAEERDRAEAEAR--EKETKA 1495
Cdd:PTZ00121 1241 E---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkkKADEAKKAEEKKKADEAKKkaEEAKKA 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1496 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELE---DELQATEDAK 1572
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAK 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1573 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKqralAVASKKKMEIDLKDLEAQIEAANKARDE 1652
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1653 VIKQLRKLQAQMKDYQRELEEARASRDEifAQSKESEKKlkslEAEILQLQEELASSERARRHAEQERdelADEIANSAS 1732
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKK----KADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1733 GKSAllDEKRRLE-ARIAQLEEELEEEQSNMELLNDRFRKTTL--QVDTLNTELAAERSAAQKSDNARQQLERQNKELKA 1809
Cdd:PTZ00121 1545 KKKA--DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1810 KLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTE---KKLKEIFMQVEDERRHADQYKEQMEKAN 1886
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
....*....
gi 1039738675 1887 aRMKQLKRQ 1895
Cdd:PTZ00121 1703 -KAEELKKK 1710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
864-1525 |
1.37e-13 |
|
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: 76.30 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 864 LQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEE 943
Cdd:pfam05483 115 IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 944 eeernQILQNEKKKMQAhiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEvllledqnskFIKEKKLMEDRIAECSS 1023
Cdd:pfam05483 195 -----MILAFEELRVQA------------ENARLEMHFKLKEDHEKIQHLEEE----------YKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1024 QLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD----LQDQIAELQAQVDELKVQLTKKE 1099
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1100 EELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ---- 1175
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKevel 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1176 QELRT-----------------------KREQEVAELKKALEDETKNHEAQ---IQDMRQRHATALEELSEQLEQAKRFK 1229
Cdd:pfam05483 408 EELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQltaIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1230 ANLEKNKQGLETDNKEL-------ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNV 1302
Cdd:pfam05483 488 IELTAHCDKLLLENKELtqeasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN---LRDELESVREEFIQKGDEV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1303 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1382
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1383 LADTKKKVDDDLGTIESLEEAKK----KLLKDVEALSQRLEEKVlaydklektknRLQQELDdltVDLDHQ-RQIVSNLE 1457
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAV-----------KLQKEID---KRCQHKiAEMVALME 710
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1458 KKQKKFDQLLAE---EKGISARYAEERDRA----EAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1525
Cdd:pfam05483 711 KHKHQYDKIIEErdsELGLYKNKEQEQSSAkaalEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
927-1703 |
2.52e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.93 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 927 KQELEEILHDLESRVEEEEER----NQILQNEKKKMQAHIQDLEEQLdeeegarQKLQLEKvTAEAKIKKME---EEVLL 999
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRlnesNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRREsqsQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1000 LEDQNS--KFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQEL------------EK 1065
Cdd:pfam15921 145 NQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1066 AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAlargddetlHKNNALKVARELQAQIAELqedfeSEKASrn 1145
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ---------HQDRIEQLISEHEVEITGL-----TEKAS-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1146 KAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1225
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1226 KRF---KANLEKNKQGLETD----NKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1298
Cdd:pfam15921 366 DQFsqeSGNLDDQLQKLLADlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1299 LDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQqeeeeearknlEKQVLA 1378
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1379 LQSQLADTKKKVDDDLGTIESL---EEAKKKLLKDVEALSQRLEEKvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1455
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLkneGDHLRNVQTECEALKLQMAEK-------DKVIEILRQQIENMTQLVGQHGRTAGA 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1456 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM----SSKD 1531
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRN 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1532 DVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAKLRLE-VNMQAMKAQFerDLQTRDEQNEEKKRL 1603
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMETttnklkmQLKSAQSELEQTRNTLKSMEgSDGHAMKVAM--GMQKQITAKRGQIDA 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1604 LLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQieaankaRDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1683
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-------KNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818
|
810 820
....*....|....*....|
gi 1039738675 1684 QSKESEKKLKSLEAEILQLQ 1703
Cdd:pfam15921 819 QFAECQDIIQRQEQESVRLK 838
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1602 |
2.54e-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: 75.78 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 854 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQE 929
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 930 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEG-ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFI 1008
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1009 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGettdlqdqiaeLQAQV 1088
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-----------LLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1089 DELKVQLTKKEEELQGALARGDDETLHKN-NALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED 1167
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAIsTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1168 TLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1247
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1248 CEVKVLQQVKAES--EHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1325
Cdd:pfam02463 677 EIQELQEKAESELakEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1326 QLQDTQEllQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1405
Cdd:pfam02463 757 LKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1406 KLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1485
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1486 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsskddvgknvhELEKSKRALEQQVEEMRTQLEELEDEL 1565
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-----------EEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750
....*....|....*....|....*....|....*..
gi 1039738675 1566 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKR 1602
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1145-1813 |
4.03e-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: 74.67 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1145 NKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREqevaELKKALEDETKNHEAQIQDMRQrhataleelseqleq 1224
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDE----EKINNSNNKIKILEQQIKDLND--------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1225 akrfKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVS 1303
Cdd:TIGR04523 90 ----KLKKNKDKiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1304 TLLEEAEKKGIKFAKDAAGLESQLQDTQellQEETRQKLNLSSrIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQL 1383
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIK---NKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1384 ADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLT--VDLDHQRQIVSNLEKKQK 1461
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqKEQDWNKELKSELKNQEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1462 KFDQL---LAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVH 1538
Cdd:TIGR04523 322 KLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL-------RLEVNMQAMKAQFERDLQTRDEQNEEKKrLLLKQVREL 1611
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1612 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARasrDEIfaQSKESEKK 1691
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE---DEL--NKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1692 LKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1771
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1039738675 1772 TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQE 1813
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
977-1742 |
4.54e-13 |
|
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: 74.76 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 977 QKLQLEKVTAEAKIK----KMEEEVLLLEDQNsKFIKEKKLMEDRIaecSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1052
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1053 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHknnalkVARELQAQIAE 1132
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH------LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1133 LQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDetknheaqIQDMRQRHA 1212
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1213 TALEELSEQLEQAKRFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1291
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1292 anklqneldnvSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklnlssriRQLEEEKNSLQEQQEEEEEARKN 1371
Cdd:pfam05483 390 -----------SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1372 LEKQVLALQSQLADTKKKVDDDLGTIESLE-EAKKKLLKDVEALSQRleekvlayDKLEKTKNRLQQELDDLTVDLDHQR 1450
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1451 QIVSNLEKKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKAL--SLARALEEALEAKEEFERQNKQLRADMEDL 1526
Cdd:pfam05483 520 EDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEFIQKGDEVKCKldKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1527 MSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQatedaklRLEVNMQAMKAQFERDLQTRDEQNEEKKrlllk 1606
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-------KLELELASAKQKFEEIIDNYQKEIEDKK----- 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1607 qVRELEAELEDERKQRALAVASKKKMEIDLkdleaqieaanKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1686
Cdd:pfam05483 668 -ISEEKLLEEVEKAKAIADEAVKLQKEIDK-----------RCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1687 ESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEiansASGKSALLDEKR 1742
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME----AKENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1267 |
7.19e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 852 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEknilAEQLQAETELFAEAEEMRARLAAK-KQEL 930
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER----HELYEEAKAKKEELERLKKRLTGLtPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 931 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ--------------LEKVTAEakIKKMEEE 996
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPvcgrelteehrkelLEEYTAE--LKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 997 VLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNK-QEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1075
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1076 DLQdQIAELQAQVDELKVQLTKKEEELqgalarGDDETLHKNNALKVARELQAQIAELqEDFESEKASRNKAEKQKRDLS 1155
Cdd:PRK03918 547 ELE-KLEELKKKLAELEKKLDELEEEL------AELLKELEELGFESVEELEERLKEL-EPFYNEYLELKDAEKELEREE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1156 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAL-EDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEK 1234
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
410 420 430
....*....|....*....|....*....|...
gi 1039738675 1235 NKQGLETdNKELACEVKVLQQVKAESEHKRKKL 1267
Cdd:PRK03918 699 LKEELEE-REKAKKELEKLEKALERVEELREKV 730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1287-1936 |
7.69e-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: 73.90 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1287 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEE 1366
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1367 EARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL 1446
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1447 DHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLradmedl 1526
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1527 msskDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLK 1606
Cdd:TIGR04523 270 ----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1607 QVRELEAELEDERKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSK 1686
Cdd:TIGR04523 343 QISQLKKELTNSESE-------NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-------LNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1687 ESEKKLKSLEAEILQLqeelasserarrhaEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1766
Cdd:TIGR04523 409 QKDEQIKKLQQEKELL--------------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1767 DRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQ--EA 1844
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKddFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1845 KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATranasrrKLQRELDDATEAN 1924
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-------SLEKELEKAKKEN 626
|
650
....*....|..
gi 1039738675 1925 EGLSREVSTLKN 1936
Cdd:TIGR04523 627 EKLSSIIKNIKS 638
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
813-1459 |
8.89e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 813 RKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEgeleemERKH 892
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 893 QQLLEEKnilAEQLQAETELFAEAEEMRARLAAKKQELEeilhdlesrveeeeernqilqnekkkmqahiqdleeqldee 972
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKKAEE----------------------------------------- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 973 egARQKLQLEKVTAEAkiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1052
Cdd:PTZ00121 1482 --AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1053 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQVDELKVQ----LTKKEEELQGALARGDDETLHKNNALKVARELQA 1128
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1129 QIAELQEDFESEKasrNKAEKQKRdlSEELEALKTELEdtldttaAQQELRTKREQEvaELKKALEDETKNHEAQIQDmr 1208
Cdd:PTZ00121 1634 KVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE-- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1209 qrhatalEELSEQLEQAKRFKAnlEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE------LHAKVSEGD 1282
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEK 1768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1283 RLRVELAEKANKLQNELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET----RQKLNLSSRIRQLEEEKNSL 1358
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELD------EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEDSAIKEVADSKNMQ 1842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1359 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1438
Cdd:PTZ00121 1843 LEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
650 660
....*....|....*....|.
gi 1039738675 1439 lDDLTVDLDHQRQIVSNLEKK 1459
Cdd:PTZ00121 1923 -EYIKRDAEETREEIIKISKK 1942
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1263-1720 |
3.09e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1263 KRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEKKGIKFAKDAAGLEsQLQDTQELLQEETRQKL 1342
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1343 NLSSRIRQLEEEKNSLQeqqeeeeeARKNLEKQVLALQSQLADTKKKVDDDL-GTIESLEEAKKKLLKDVEALSQRLEEK 1421
Cdd:COG4717 140 ELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1422 VLAYDKLEKTKNRLQQELDDLTVDLDHQrqivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA-- 1499
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1500 --------RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATE 1569
Cdd:COG4717 287 allflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1570 DAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERK--QRALAVASKKKMEIDLKDLEAQIEAAN 1647
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1648 KARDEVIKQLRKLQAQMKDY--QRELEEARASRDEIFAQskesekkLKSLEAEILQLQEELASSERARRHAEQER 1720
Cdd:COG4717 446 EELEELREELAELEAELEQLeeDGELAELLQELEELKAE-------LRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
850-1311 |
3.42e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 850 KVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQE 929
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 930 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIK 1009
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1010 EKKLMEDRIAECSSQLAEEEEKaknlaKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT---------DLQDQ 1080
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1081 IAELQAQVDELKVQ-LTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASRNKA---EKQKRDLSE 1156
Cdd:PRK03918 505 LKELEEKLKKYNLEeLEKKAEEYEKLKEK--------------LIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1157 ELEALKTELEdtldttaaqqELRTKREQEVAELKKALEdETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNK 1236
Cdd:PRK03918 571 ELAELLKELE----------ELGFESVEELEERLKELE-PFYNEYLELKDAEKE----LEREEKELKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1237 QGLETDNKELACEVKVLQQVKAESEHKRK-----KLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1311
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1623-1863 |
4.31e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.18 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1623 ALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1702
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1703 QEELasserarrhaEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1782
Cdd:COG4942 96 RAEL----------EAQKEELAELLR-------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1783 LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLK 1862
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
.
gi 1039738675 1863 E 1863
Cdd:COG4942 238 A 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
909-1637 |
4.81e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.79 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 909 ETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEA 988
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 989 KIKKMEEEVLLLEDQNSKFIKEK----KLMEDRIAECSSQLAEEEEKAK----NLAKIRNKQEVMISDLEERLKK----- 1055
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKaltgKHQDVTAKYNRRRSKIKEQNNRdiagi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1056 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddETLHKNNALKVARELQAQIAELQE 1135
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG----ELKLRLNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1136 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDttAAQQElrtkrEQEVAELKKALEdetknhEAQIQDMRQRHaTAL 1215
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASE--ALRQA-----SRRLEERQSALD------ELELQLFPQAG-TLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1216 EELSEQLEQAKRFKANLEKNKQGLETDnkeLACEVkVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvelaEKANKL 1295
Cdd:pfam12128 538 HFLRKEAPDWEQSIGKVISPELLHRTD---LDPEV-WDGSVGGELNLYGVKLDLKRIDVPEWAASEEELR----ERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1296 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNSLQeqqeeeeearknlekq 1375
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK-------NARLDLRRLFDEKQSEK---------------- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1376 vLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1455
Cdd:pfam12128 667 -DKKNKALAERKDSANER---LNSLEAQLKQLDKKHQAWLEEQKE--------QKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1456 LEKKQKKFDQLLAEEKGISARYAEE-------RDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1528
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDlaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1529 SKDDVGKNVHELEKSkraLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQV 1608
Cdd:pfam12128 815 QLSNIERAISELQQQ---LARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQG---SI 888
|
730 740
....*....|....*....|....*....
gi 1039738675 1609 RELEAELEDERKQRALAVASKKKMEIDLK 1637
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
857-1459 |
5.78e-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: 71.36 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 857 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNilaEQLQAETELFAEAEEMRARLaakKQELEEILHD 936
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNRL---QQELDDLLVD 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 937 LESrveeeeeRNQILQNEKKKMQ-----------AHIQDLEEQLDEEEGARQK----LQLEKVTAEAKIKKME------- 994
Cdd:pfam01576 589 LDH-------QRQLVSNLEKKQKkfdqmlaeekaISARYAEERDRAEAEAREKetraLSLARALEEALEAKEElertnkq 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 995 -----EEVLLLEDQNSKFIKE----KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEK 1065
Cdd:pfam01576 662 lraemEDLVSSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1066 AKRKLdgettdLQDQIAELQAQVDELKVQLT-------KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFE 1138
Cdd:pfam01576 742 EKRRQ------LVKQVRELEAELEDERKQRAqavaakkKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1139 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAEL----------KKALEDETKNHEAQIQDMR 1208
Cdd:pfam01576 816 EARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELadeiasgasgKSALQDEKRRLEARIAQLE 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1209 qrhatalEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkaeSEHKRKKLDAQVQELHAKVSEgdrlrvel 1288
Cdd:pfam01576 896 -------EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKLQE-------- 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1289 aekanklqneldnvstlLEEAEKKgiKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknslqeqqeeeeea 1368
Cdd:pfam01576 957 -----------------MEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK--------------- 1002
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1369 rknlekqvlalqsQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDH 1448
Cdd:pfam01576 1003 -------------KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNES 1069
|
650
....*....|.
gi 1039738675 1449 QRQIVSNLEKK 1459
Cdd:pfam01576 1070 MNREVSTLKSK 1080
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1009-1231 |
7.56e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1009 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQV 1088
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1089 DEL--KVQLTKKEEELQGALARGDDETLHKNNAL--KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTE 1164
Cdd:COG4942 107 AELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 1165 LedtldttAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRhATALEELSEQLEQAKRFKAN 1231
Cdd:COG4942 187 R-------AALEALKAERQKLLARLEK----ELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
1.21e-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: 60.91 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1039738675 31 TAKKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
884-1485 |
2.43e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 884 ELEEMERKHQQLLEEKnilaEQLQAETELFAEAEEmRARLAAKKQELEEILHDLesRVEEEEERNQILQNEKKKMQAhiq 963
Cdd:COG4913 233 HFDDLERAHEALEDAR----EQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRA--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 964 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfIKEKKLmeDRIAECSSQLAEEEEKAKNLAKIRNKQE 1043
Cdd:COG4913 303 -----------ELARLEAELERLEARLDALREELDELEAQ----IRGNGG--DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1044 VMISDLEERLKKEEK----TRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD--DETLHK- 1116
Cdd:COG4913 366 ALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLAl 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1117 ----NNALKVARELQAQIAELQEDFESEKASRNKAEK----QKRDL--SEELEALKTELEDTLDTTAAQQELRTKREQEV 1186
Cdd:COG4913 446 rdalAEALGLDEAELPFVGELIEVRPEEERWRGAIERvlggFALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1187 AELKKALED------ETKNHEAQ--IQD-MRQRHATALEELSEQLEQAKR-------FKANL---EKNKQGLET------ 1241
Cdd:COG4913 526 PERPRLDPDslagklDFKPHPFRawLEAeLGRRFDYVCVDSPEELRRHPRaitragqVKGNGtrhEKDDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1242 -DNKE----LACEVKVLQQVKAESEHKRKKLDAQVQEL------HAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAE 1310
Cdd:COG4913 606 fDNRAklaaLEAELAELEEELAEAEERLEALEAELDALqerreaLQRLAEYSWDEIDVAS----AEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1311 KkgikFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKkv 1390
Cdd:COG4913 682 A----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF-- 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1391 dDDLGTIESLEEAKKKLLKDVEALSQRLEEkvlAYDKLEKTKNRLQQELDDLTVDLD------------HQRQIVSNLEK 1458
Cdd:COG4913 756 -AAALGDAVERELRENLEERIDALRARLNR---AEEELERAMRAFNREWPAETADLDadleslpeylalLDRLEEDGLPE 831
|
650 660 670
....*....|....*....|....*....|..
gi 1039738675 1459 KQKKFDQLLAEEKG-----ISARYAEERDRAE 1485
Cdd:COG4913 832 YEERFKELLNENSIefvadLLSKLRRAIREIK 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1545-1940 |
3.10e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1545 RALEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQ 1621
Cdd:COG4913 238 ERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1622 RALAVASKKKME--------IDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQrelEEARASRDEIFAQSKESEKKLK 1693
Cdd:COG4913 318 LDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1694 SLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA----------------------------LLD------ 1739
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparllalrdalaealgldeaelpfvgeLIEvrpeee 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1740 -------------------------------EKRRLEARI-AQLEEELEEEQSNMELLNDR------FRKTTLQvDTLNT 1781
Cdd:COG4913 475 rwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLvYERVRTGLPDPERPRLDPDSlagkldFKPHPFR-AWLEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1782 ELAaERSAAQKSDNArQQLER------------QNKEL-------------------KAKLQELEGAVKsKFKATISALE 1830
Cdd:COG4913 554 ELG-RRFDYVCVDSP-EELRRhpraitragqvkGNGTRhekddrrrirsryvlgfdnRAKLAALEAELA-ELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1831 AKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeiFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASR 1910
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510
....*....|....*....|....*....|
gi 1039738675 1911 RKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1073-1842 |
5.70e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1073 ETTDLQDQIAELQAQVDELkvqltkkeEELQGALargdDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-----A 1147
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1148 EKQKRDLSEELEALKTELEDTldttaaqqelrtkrEQEVAELKKALEDetknHEAQIQDMRQRHATALEELSEQLEQakr 1227
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARLDA----LREELDELEAQIRGNGGDRLEQLER--- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1228 fkanleknkqgletdnkelacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRlrvELAEKANKLQNELDNVSTLLE 1307
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1308 EAEkkgikfaKDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVLALQSQLADTK 1387
Cdd:COG4913 402 ALE-------EALAEAEAALRDLRR--------------ELRELEAEIASLERR-------KSNIPARLLALRDALAEAL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1388 KKVDDDL-----------------GTIESL-----------EEAKKKLLKDVEALSQRLEekvLAYDKLEKT-KNRLQQE 1438
Cdd:COG4913 454 GLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVNRLHLRGR---LVYERVRTGlPDPERPR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1439 LDDltvdldhqRQIVSNLEKKQKKFDQLLAEEkgisarYAEERDRA---EAEAREKETKALSLARaleealeakeeferq 1515
Cdd:COG4913 531 LDP--------DSLAGKLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRHPRAITRAG--------------- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1516 nkqlradmedLMSSkddvGKNVHELEKSKRALEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlqtr 1593
Cdd:COG4913 582 ----------QVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---- 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1594 deqneEKKRLLLKQVRELEAElederkqralavaskkkmEIDLKDLEAQIEAANKARDEVIK---QLRKLQAQMKDYQRE 1670
Cdd:COG4913 644 -----QERREALQRLAEYSWD------------------EIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAE 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1671 LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELassERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1751 LEEELEEEQSNMELLNDRFRKT-TLQVDTLNTELAAERSAAQKsdnaRQQLERQN-KELKAKLQELEGAVKSKFKATI-S 1827
Cdd:COG4913 778 LRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEEDGlPEYEERFKELLNENSIEFVADLlS 853
|
810
....*....|....*
gi 1039738675 1828 ALEAKIGQLEEQLEQ 1842
Cdd:COG4913 854 KLRRAIREIKERIDP 868
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1050-1880 |
1.94e-10 |
|
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: 66.51 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1050 EERLKKEEKT---RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlHKN---NAL--- 1120
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAASD-------HLNlvqTALrqq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1121 -KVAR------ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED---TLDT--TAA---QQELRTKRE-Q 1184
Cdd:COG3096 347 eKIERyqedleELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqALDVqqTRAiqyQQAVQALEKaR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1185 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLEtdnkelacevKVLQQVKAESEHKR 1264
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVC----------KIAGEVERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1265 -KKLDAQVQELHAKVSEGDRLRVELAEkANKLQNELDNVSTLLEEaekkgikFAKDAAGLESQLQDTQELLQEETRQKLN 1343
Cdd:COG3096 497 aRELLRRYRSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEE-------FCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1344 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLkdvealsQRLEE 1420
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLL-------ERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1421 KVLAYDKLEKTKNRLQQElddltvdldhqrqiVSNLEKKQKKFD---QLLAEEKG------------------ISARYAE 1479
Cdd:COG3096 642 ATVERDELAARKQALESQ--------------IERLSQPGGAEDprlLALAERLGgvllseiyddvtledapyFSALYGP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1480 ER------DraeaeareketkaLSLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK----- 1542
Cdd:COG3096 708 ARhaivvpD-------------LSAVK-------------EQLAGLEDCPEDLYliegdpDSFDDSVFDAEELEDavvvk 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1543 -SKRAL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEE 1599
Cdd:COG3096 762 lSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEA 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1600 KKRLLLKQVRELEAELEDERKQralavaskkkmeidLKDLEAQIEAANkardEVIKQLRKLQAQM------------KDY 1667
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQ--------------EQQLRQQLDQLK----EQLQLLNKLLPQAnlladetladrlEEL 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1668 QRELEEARASRDEIFAQSK---ESEKKLKSLEAEILQ---LQEELASSERARRHAEQERDELADEIANSA----SGKSAL 1737
Cdd:COG3096 899 REELDAAQEAQAFIQQHGKalaQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1738 LDEKRRLEARIAQLEEELEEEQSNmelLNDRFRKTTLQVDTLNTELAAERSAAqksDNARQQLerqnKELKAKLQELEGA 1817
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARRE---AREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTL----QELEQELEELGVQ 1048
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1818 V-----------KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqveDERRHADQYKE 1880
Cdd:COG3096 1049 AdaeaeerarirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKA 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1640-1863 |
2.09e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.85 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1640 EAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELasserarrhaEQE 1719
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1720 RDELADEIA------NSASGKSALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKs 1793
Cdd:COG3883 85 REELGERARalyrsgGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1794 dnARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1863
Cdd:COG3883 155 --KLAELEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1617-1939 |
2.96e-10 |
|
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: 65.86 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1617 DERKQRALAvaskkkmeiDLKDLEAQIEAANKARDEVIKQLRKLQAQ------MKDYQRELEEARASrdEIFAQSKESEK 1690
Cdd:TIGR02169 169 DRKKEKALE---------ELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGY--ELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1691 KLKSLEAEILQLQEELASSERarrhaeqERDELADEIAnsasgksALLDEKRRLEARIaqleeeleeeqsnMELLNDRFR 1770
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTE-------EISELEKRLE-------EIEQLLEELNKKI-------------KDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1771 KTTLQVDTLNTELAaersaaqksdnarqQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQEAKERAAA 1850
Cdd:TIGR02169 291 RVKEKIGELEAEIA--------------SLERSIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1851 NKLVRRTEKKLKEIFMQVEDE-------RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA 1923
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330
....*....|....*.
gi 1039738675 1924 NEGLSREVSTLKNRLR 1939
Cdd:TIGR02169 436 INELEEEKEDKALEIK 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1114-1831 |
4.71e-10 |
|
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: 65.24 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1114 LHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAA-QQELRTKREQeVAELKKA 1192
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQ-WKEKRDE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1193 LEDETKNHEAQIQDMRqrhatalEELSEQLEQAKRF-KANLEKNKQGLETdnkelacevkvLQQVKAESEHKRKKLDAQV 1271
Cdd:pfam12128 306 LNGELSAADAAVAKDR-------SELEALEDQHGAFlDADIETAAADQEQ-----------LPSWQSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1272 QELHAKVSEGDRLRV----ELAEKANKLQNELDNVStllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETR-QKLNLSS 1346
Cdd:pfam12128 368 GKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESELREQLEAGKLEFNeEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1347 RIRQL----------EEEKNSLQEQQEEEEEARKNLE---KQVLALQSQLADTKKKVDddlgtiesleEAKKKLlkdvEA 1413
Cdd:pfam12128 445 RLGELklrlnqatatPELLLQLENFDERIERAREEQEaanAEVERLQSELRQARKRRD----------QASEAL----RQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1414 LSQRLEEkvlaydklektknrLQQELDDLTVDLDHQR-QIVSNLEKKQKKFDQLLAeeKGISARYAEERDRAEAEAREKE 1492
Cdd:pfam12128 511 ASRRLEE--------------RQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1493 TKALSLARALEEALEAKEEFERQ-NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDA 1571
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAAsEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1572 KLRLEVNMQAMKAQFERDLQTRDEQNEE--------KKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQI 1643
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANErlnsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1644 EAANKARDEVIKqlRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaEILQLQEELASSERARRHA-EQERDE 1722
Cdd:pfam12128 735 KAAIAARRSGAK--AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE-RIAVRRQEVLRYFDWYQETwLQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1723 LADEIANSASGKSALLDEKRRLEA----RIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTeLAAERSAAQKSDNARQ 1798
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT-LKEDANSEQAQGSIGE 890
|
730 740 750
....*....|....*....|....*....|....*.
gi 1039738675 1799 QLeRQNKELKAKLQELEGAVKSK---FKATISALEA 1831
Cdd:pfam12128 891 RL-AQLEDLKLKRDYLSESVKKYvehFKNVIADHSG 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1643-1940 |
5.00e-10 |
|
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: 65.09 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1643 IEAANKARDEVIKQLrklqAQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELassERARRHAEqERDE 1722
Cdd:TIGR02169 148 ISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKRQQLERL---RREREKAE-RYQA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1723 LADEIANSASgkSALLDEKRRLEARIAQLEEELEEEQSNMEllndrfrKTTLQVDTLNTELAAersaaqksdnARQQLER 1802
Cdd:TIGR02169 216 LLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELE-------KLTEEISELEKRLEE----------IEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1803 QNKELKAKLQELEGAVKSK---FKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1879
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1880 EQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1308 |
5.43e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.74 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 862 EELQAKDEELLKVKEKQTKVEGE-------LEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQEL 930
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 931 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK- 1009
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1010 ----EKKLMEDR--IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1083
Cdd:pfam05483 491 tahcDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1084 LQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1163
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1164 ELEDTLDTTAAQQELRTKREQEV---AELKKALEDETKNHEAQIqDMRQRHATAleelseqleqakRFKANLEKNKQGLE 1240
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEKLleeVEKAKAIADEAVKLQKEI-DKRCQHKIA------------EMVALMEKHKHQYD 717
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1241 TDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAK-VSEGDRLRVELAEKANKLQNELDNVSTLLEE 1308
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAElLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1077-1863 |
6.22e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1077 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVAREL-QAQIAELQE-DFESEKASRNKAE--KQKR 1152
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEeiQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1153 DLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIqdmrqrhaTALEELSEQLEQAK-RFKAN 1231
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlEMHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1232 LEKNKQGLETDNKELACEVKvlqqvkaESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1311
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEIN-------DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1312 KGIKFAKDAAGLESQLQ---DTQELLQEETRQKlnlSSRIRQLEEEKNSlqeQQEEEEEARKNLEKQVLALQSQLADTKK 1388
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQrsmSTQKALEEDLQIA---TKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1389 KVDDDLGTIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTVDLDHQRQIVSnlekKQKKFDQLLA 1468
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEE-------MTKFKNNKEVELEELKKILAEDEKLLD----EKKQFEKIAE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1469 EEKGisaryAEERDRAEAEAREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1548
Cdd:pfam05483 433 ELKG-----KEQELIFLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1549 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfERDLQTRDEqneekkrllLKQVRELEAELEDERKQRAlavas 1628
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDE---------LESVREEFIQKGDEVKCKL----- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1629 kKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAS 1708
Cdd:pfam05483 569 -DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1709 serARRHAEQERDELADEIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnDRFRKTTLQVDTLNTELAAERS 1788
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA------------------DEAVKLQKEIDKRCQHKIAEMV 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1789 AAQKSDNAR--QQLERQNKEL---KAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1863
Cdd:pfam05483 707 ALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1123-1916 |
6.66e-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: 64.68 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1123 ARELQAQIAELQEDFESEKASRNKAEKQKRDLSE---ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN 1199
Cdd:TIGR00606 219 ACEIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1200 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ-QVKAESEHKRKKlDAQVQELHAkv 1278
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLAT-- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1279 segdRLRVELAEKANKLQNELDNVSTLLEEAEKKGikfAKDAAGLESQLQDTQELLQE---ETRQKLNLSSRIRQLEEEK 1355
Cdd:TIGR00606 376 ----RLELDGFERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTIELKKEI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1356 nslqeqqeeeeearknLEKQvlalQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSqRLEEKVLAYDKLEKTKNRL 1435
Cdd:TIGR00606 449 ----------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1436 QQELDdltvdldhqrqivsnLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKalslaraleealeakeefERQ 1515
Cdd:TIGR00606 508 NEKAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------------------DEQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1516 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFERDLQTRDE 1595
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEE 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1596 QneekkrlllkqvrelEAELEDerkqRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1675
Cdd:TIGR00606 620 Q---------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1676 ASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1755
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1756 EEEQSNMElLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVK----SKFKATISALEA 1831
Cdd:TIGR00606 761 QRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELD 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1832 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRR 1911
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE 919
|
....*
gi 1039738675 1912 KLQRE 1916
Cdd:TIGR00606 920 KDQQE 924
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1467 |
6.72e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 858 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 937
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 938 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIKEKKLMEdr 1017
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLE-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1018 iaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEK----TRQELEKAKRKLDGETTDLQD---QIAELQAQVDE 1090
Cdd:TIGR04523 218 -----SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1091 LKVQLtkkeeelqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1170
Cdd:TIGR04523 293 LKSEI----------------SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1171 TTAAQQELRTKREQEVAELKKALE---DETKNHEAQIQDMRQrhataleelseQLEQAKRFKANLEKNKQGLETDNKELA 1247
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1248 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQL 1327
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1328 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQL--ADTKKKVDDDLGTIESLEEAKK 1405
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQK 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1406 KLLKDVEALSQRLeekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL 1467
Cdd:TIGR04523 579 SLKKKQEEKQELI-------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1639-1891 |
7.58e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.27 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1639 LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIF--AQSKESEKKLKSLEAEILQLQEELASSErARRHA 1716
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAE-ARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1717 EQERDELADEIANSASGKSALldekRRLEARIAQleeeleeeqsnmellndrfrkttlqvdtLNTELAAERSAAQKSDNA 1796
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVI----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1797 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLvrrtEKKLKEIFMQVEDERRHAD 1876
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYE 368
|
250
....*....|....*
gi 1039738675 1877 QYKEQMEKANARMKQ 1891
Cdd:COG3206 369 SLLQRLEEARLAEAL 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1539-1750 |
8.55e-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: 62.86 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDE 1618
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1619 RKQRA--LAVASKKKMEIDLKDLEAQIEAANKARD-EVIKQL-RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS 1694
Cdd:COG4942 103 KEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1695 LEAEILQLQEELASSERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQ 1750
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1158-1629 |
1.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1158 LEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQ 1237
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE--------LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1238 GLET--DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiK 1315
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---D 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1316 FAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK-NLEKQVLALQSQLADTKKKVDDDL 1394
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1395 G----TIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE 1470
Cdd:COG4717 277 GvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1471 KGISARYAEER---------DRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS--SKDDVGKNVHE 1539
Cdd:COG4717 357 EELEEELQLEEleqeiaallAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1540 LEKSKRALEQQVEEMRTQLEELEDELQATEDaklrlEVNMQAMKAQFERDLQTRDEQNEE--KKRLLLKQVRELEAELED 1617
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEwaALKLALELLEEAREEYRE 511
|
490
....*....|..
gi 1039738675 1618 ERKQRALAVASK 1629
Cdd:COG4717 512 ERLPPVLERASE 523
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
856-1312 |
1.49e-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: 63.12 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEmerkHQQLLEEKNILAEQLQAE-TELFAEAEEMrarlaaKKQELEEIL 934
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSE----KQKELEQNNKKIKELEKQlNQLKSEISDL------NNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 935 HDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLM 1014
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1015 EDRIAECSSQLAEEEEKAKNlakirnkqevmisdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ 1094
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQ--------------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1095 LTKKEeelqgalargddetlhknnalKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL---KTELEDTLDT 1171
Cdd:TIGR04523 456 IKNLD---------------------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneeKKELEEKVKD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1172 TAAQQELRTKREQEVAELKKALEDETKNHEAQIQDM-----RQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKEL 1246
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1247 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKK 1312
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1046-1222 |
1.51e-09 |
|
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: 60.32 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1046 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNAlKVARE 1125
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1126 LQAqiaeLQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQIQ 1205
Cdd:COG1579 91 YEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 1039738675 1206 DMRQRHATALEELSEQL 1222
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1341-1937 |
1.57e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1341 KLNLSSRIRQLEEEKNSLQEQQEEEEeaRKNLEKQVLALQSQLADTKKKVDDdlGTIEslEEAKKKLLKDVEALSQRLEE 1420
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAK--EDNRADEATEEAFGKAEEAKKTET--GKAE--EARKAEEAKKKAEDARKAEE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1421 KVLAYDKLEKTKNRLQQelDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETKALSLAR 1500
Cdd:PTZ00121 1133 ARKAEDARKAEEARKAE--DAKRVEIARKAEDARKAEEARKAEDAKKAEA----ARKAEEVRKAEELRKAEDARKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1501 ALEEALEAKEEFERQNKQLRADMEDLMSSKDDVgknvhelEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmQ 1580
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA-------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---E 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1581 AMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL----------AVASKKKMEIDLKDLEAQIEAANKAR 1650
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeakkkADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1651 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEA-----EILQLQEELASSERARRHAEQERDelAD 1725
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkadELKKAAAAKKKADEAKKKAEEKKK--AD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1726 EIANSASGKSALLDEKRRLE-ARIAQLEEELEEEQSNMELLndrfRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQN 1804
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEA----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1805 KELKAKLQELEGAVKSKFKATISALEAKIGQLEEQleQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEK 1884
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1885 ANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1937
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1538-1940 |
1.69e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1538 HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE-RDLQTRDEQNEEKkrllLKQVRELEAELE 1616
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEER----LEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1617 DERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1695
Cdd:COG4717 167 ELEAELAeLQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1696 EAEILQLQEELASSERARRHAEQERDELADEIANSASG-----KSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1770
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1771 KTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKakLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAA 1850
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1851 NKLVRRTEKKLKEIFMQVEDErrhadqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE--GLS 1928
Cdd:COG4717 405 EELEEQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELL 475
|
410
....*....|..
gi 1039738675 1929 REVSTLKNRLRR 1940
Cdd:COG4717 476 QELEELKAELRE 487
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
876-1750 |
1.69e-09 |
|
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: 63.43 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 876 EKQTKVEGELEemerKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeILHDLESRVeeeeeRNQILQNEK 955
Cdd:COG3096 279 ERRELSERALE----LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQ-AASDHLNLV-----QTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 956 -KKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV-----------LLLEDQNSKFIKEKKLMEdRIAECSS 1023
Cdd:COG3096 349 iERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladyqQALDVQQTRAIQYQQAVQ-ALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1024 QLAEEEEKAKN----LAKIRNKQEVMIS---DLEERLKKEEKTRQELEKAK---RKLDGETTdlqdqiaelQAQVDELKV 1093
Cdd:COG3096 428 LCGLPDLTPENaedyLAAFRAKEQQATEevlELEQKLSVADAARRQFEKAYelvCKIAGEVE---------RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1094 QLTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASR------NKAEKQKRDLSEELEALKTELED 1167
Cdd:COG3096 499 ELLRRYRSQQALAQR--------------LQQLRAQLAELEQRLRQQQNAErlleefCQRIGQQLDAAEELEELLAELEA 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1168 TLDTTAAQQElrtkreqEVAELKKALEDETKNHEAQIQDMRQRH------ATALEELSEQLEQAkrfkanLEkNKQGLET 1241
Cdd:COG3096 565 QLEELEEQAA-------EAVEQRSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEA------LA-DSQEVTA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1242 DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAN-KLQNEL-DNVStlLEeaekkgikfakD 1319
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGgVLLSEIyDDVT--LE-----------D 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1320 AAGLESqlqdtqelLQEETRQKL---NLSSRIRQLEEEKNSLQEqqeeeeearknlekqvLALQSQLADTkkkVDDDLGT 1396
Cdd:COG3096 698 APYFSA--------LYGPARHAIvvpDLSAVKEQLAGLEDCPED----------------LYLIEGDPDS---FDDSVFD 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1397 IESLEEAkkkllkDVEALSQRL-------EEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAE 1469
Cdd:COG3096 751 AEELEDA------VVVKLSDRQwrysrfpEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1470 EKGIsaryAEERDrAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA-LE 1548
Cdd:COG3096 825 HLAV----AFAPD-PEAELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADEtLA 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1549 QQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMK---AQFERdLQTRDEQNEEKKRLL------LKQVRELEAELE 1616
Cdd:COG3096 893 DRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLkqqifaLSEVVQRRPHFS 971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1617 DERKQRALAVASkkkmeiDLKD-LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1695
Cdd:COG3096 972 YEDAVGLLGENS------DLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1696 EaeilqLQEELASSERARrhaeQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:COG3096 1046 G-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1077-1830 |
1.94e-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: 62.92 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1077 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD---ETLHKNNALKvaRELQAQIAELQEdfesekasrnkaekQKRD 1153
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTfwsPELKKERALR--KEEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1154 LSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDE------TKNHEAQIQDMRQRHATALEELSEQLEQakr 1227
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKfstpelTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1228 FKANLEKNKQGLETDNKELACEVKVLQ-----QVKAESEHKRKK----LDAQVQE----LHAKVSEGDRLRVELAEKaNK 1294
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHlevlLDQKEKENIHLREELHRR-NQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1295 LQNELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKNSLQEQQEEEEEARK 1370
Cdd:pfam10174 221 LQPDPAKTKALQTVIEMKDTKISS----LERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKIDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1371 NLEK---QVLALQSQLADTKKKVDDDLGTIESLEE---AKKK----LLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1440
Cdd:pfam10174 297 ELSKkesELLALQTKLETLTNQNSDCKQHIEVLKEsltAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1441 DLTVDLDHQRQIVSNLEKK----QKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLaraleealeakeeferqn 1516
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL------------------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1517 kqlrADMEDLMSSKDDVGKNV-HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQTRDE 1595
Cdd:pfam10174 439 ----TTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----ASSLA 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1596 QNEEKKRLLLKQvreLEAELEDERKQRALAVASKKKMEidlkdleaQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1675
Cdd:pfam10174 510 SSGLKKDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQ 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1676 ASRDEIFAQSKESE-------KKLKSLEAEILQLQEELASSERARRHAEQERDEladeiansasgKSALLDEkrrlEARI 1748
Cdd:pfam10174 579 AEVERLLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE----EARR 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1749 AQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSD----NARQQLERQNKE-LKAKLQELEGAVKSKfK 1823
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghltNLRAERRKQLEEiLEMKQEALLAAISEK-D 722
|
....*..
gi 1039738675 1824 ATISALE 1830
Cdd:pfam10174 723 ANIALLE 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1484-1712 |
2.01e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1484 AEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1563
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1564 ELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlkqvrELEAELEDERKQRALAVASKKKMEIDLK-DLEAQ 1642
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRaELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1643 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA 1712
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
904-1272 |
2.78e-09 |
|
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: 62.45 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 904 EQLQAETELFAEAEEMRA-------RLAAKKQELEEILHDLESRVEEEEERNQILQNEK--KKMQAHIQDLEEQLDEEEG 974
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 975 ARQKLQLEKVTAEAKIKKmeEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE--EEEKAKNLAKIRNKQEVMIsdleER 1052
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERirQEEIAMEISRMRELERLQM----ER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1053 LKKEEKTRQELEKAkRKLDGETTDLQDQIAELQAQVDELK--------VQLTKKEEELQGALARGDDETLHKNNALKVAR 1124
Cdd:pfam17380 388 QQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1125 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEElealktELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQI 1204
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1205 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKaESEHKRKKLDAQVQ 1272
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----------EREMMRQIV-ESEKARAEYEATTP 596
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
860-1587 |
3.11e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 62.29 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 860 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIlhdles 939
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 940 rveeeeernqILQNEKKKMQAHIQDLEEQLDEEEGARQKLQlekvTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIA 1019
Cdd:TIGR00618 287 ----------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ----SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1020 ECsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDeLKVQLTKKE 1099
Cdd:TIGR00618 353 QE-IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1100 EELQGALARGDDETLHknnALKVARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR 1179
Cdd:TIGR00618 431 KQQELQQRYAELCAAA---ITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1180 TKREQEV-AELKKALEDE-TKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELAcevKVLQQVK 1257
Cdd:TIGR00618 507 CGSCIHPnPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT---QCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1258 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEkkgikFAKDAAGLESQLQDTQ-ELLQE 1336
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-----CSQELALKLTALHALQlTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1337 ETRQKlnlSSRIRQLEEEKnslqeqqeeeEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1416
Cdd:TIGR00618 659 RVREH---ALSIRVLPKEL----------LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1417 RLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQRQIVSNLEKKQKKFDQLLAEEKgISARYAEERDRAEAEAREKETKAL 1496
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQSLKELMHQ-----ARTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTH 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1497 SLARALEealeakeeferQNKQLRADMEDLMSSKDdvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE 1576
Cdd:TIGR00618 800 LLKTLEA-----------EIGQEIPSDEDILNLQC------ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730
....*....|.
gi 1039738675 1577 vnmQAMKAQFE 1587
Cdd:TIGR00618 863 ---QLTQEQAK 870
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
917-1496 |
3.88e-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: 61.76 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 917 EEMRARLAAKKQELEeilhdlesrveeeeERNQILQNEKKKMQAHIQDLEEQLDEEEGARQklqleKVTAEAKIKKMEee 996
Cdd:pfam10174 140 EEMELRIETQKQTLG--------------ARDESIKKLLEMLQSKGLPKKSGEEDWERTRR-----IAEAEMQLGHLE-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 997 vLLLEDQNSKFIKEKKLMEDRiaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEktrQELEKAKRKLDGETTD 1076
Cdd:pfam10174 199 -VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1077 LQDQIAELQA----------QVDELKVQLTKKEEELQGALARgdDETLHKNNA-----LKVARE-----------LQAQI 1130
Cdd:pfam10174 270 REEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTK--LETLTNQNSdckqhIEVLKEsltakeqraaiLQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1131 AELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELKKALE---DETKNHEAQIQDM 1207
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1208 RQRHA----------TALEELSEQLEQAKRFKANLEKNKqglETDNKELACEVKVLQQvkaesehKRKKLDAQVQELHAK 1277
Cdd:pfam10174 421 KERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK-------ENKDLKEKVSALQPE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1278 VSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQElLQEETRQKLNLSSRIRQLEEEkns 1357
Cdd:pfam10174 491 LTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE--- 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1358 LQEQQEEEEEARKNLEKqVLALQSQLADTKKKVDDDLGTIESL------EEAKKKL-LKDVEALSQRLEEKVLA---YDK 1427
Cdd:pfam10174 567 VARYKEESGKAQAEVER-LLGILREVENEKNDKDKKIAELESLtlrqmkEQNKKVAnIKHGQQEMKKKGAQLLEearRRE 645
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1428 LEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAL 1496
Cdd:pfam10174 646 DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1693-1937 |
3.93e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1693 KSLEAEILQLQEELASSERARRHAEQERDELAdeiansasgksaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1772
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1773 tlQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1852
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1853 LVRRTEkklkeifMQVEDErrhADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateanegLSREVS 1932
Cdd:COG4913 367 LLAALG-------LPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 1039738675 1933 TLKNR 1937
Cdd:COG4913 430 SLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
871-1464 |
5.34e-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: 61.57 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 871 LLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQI 950
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 951 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLE-----KVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQL 1025
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1026 AEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELqga 1105
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI--- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1106 largddetlhknnalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaQQELRTKrEQE 1185
Cdd:TIGR04523 443 ------------------KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK------QKELKSK-EKE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1186 VAELKKaledETKNHEAQIQDMRQRHATALEELSEqleqakrfkanLEKNKQGLETDNKELACEVKvlqqvKAESEHKRK 1265
Cdd:TIGR04523 498 LKKLNE----EKKELEEKVKDLTKKISSLKEKIEK-----------LESEKKEKESKISDLEDELN-----KDDFELKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1266 KLDAQVQELHAKVSE----GDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFakdaagleSQLQDTQELLQEETRQk 1341
Cdd:TIGR04523 558 NLEKEIDEKNKEIEElkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI--------SSLEKELEKAKKENEK- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1342 lnLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1421
Cdd:TIGR04523 629 --LSSIIKNIKSKKNKLKQEV-------KQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITR 699
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1039738675 1422 VLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFD 1464
Cdd:TIGR04523 700 MIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFD 742
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1518-1850 |
5.42e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 60.47 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1518 QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQTRDEQN 1597
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1598 EEKKRLL---LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEA 1674
Cdd:pfam19220 107 EELRIELrdkTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1675 RASRDEIFAQSKESEKKLKSLEAEILQLQ----EELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1751 LEEELEEEQSNMELLNDRFRKTTLQVDT-------LNTELAAERSAAQKSDNARQQLERQ----NKELKAKLQELEGAVK 1819
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTlerrlagLEADLERRTQQFQEMQRARAELEERaemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039738675 1820 S-------------KFKATISALEAKIGQLEEQLEQEAKERAAA 1850
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1414-1863 |
5.57e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1414 LSQRLEEKVLAYDKLE-KTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEerDRAEAEAREKE 1492
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1493 TKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskddvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1572
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1573 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL-----------AVASKKKMEIDLKDLEA 1641
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1642 QIEAA------------------NKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1703
Cdd:COG4717 274 TIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1704 EELASSERARR--HAEQERDELADEIA----NSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDrfrktTLQVD 1777
Cdd:COG4717 354 REAEELEEELQleELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1778 TLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGavkskfKATISALEAKIGQLEEQLEQEAKERAAAN---KLV 1854
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE------DGELAELLQELEELKAELRELAEEWAALKlalELL 502
|
....*....
gi 1039738675 1855 RRTEKKLKE 1863
Cdd:COG4717 503 EEAREEYRE 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1280 |
5.77e-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: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 862 EELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEK-----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 936
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 937 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1016
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1017 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLT 1096
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1097 KKEEELQgALARGDDETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKA--EKQKRDLSEELEALKTELEDTLDTTA 1173
Cdd:TIGR04523 507 ELEEKVK-DLTKKISSLKEKIEKLESEKkEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1174 AQQELRTKREQEVAELKKALEDETKnheaqiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVL 1253
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEK---------------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
410 420
....*....|....*....|....*..
gi 1039738675 1254 QQVKAESEHKRKKLDAQVQELHAKVSE 1280
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1703-1941 |
5.95e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1703 QEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1782
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1783 LAAERSAAQKSDNARQQLERQNK-ELKAKLQELEGAVKSkfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1861
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1862 KEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRG 1941
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1401-1939 |
8.26e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1401 EEAKKKLLKDVealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARyaEE 1480
Cdd:PRK03918 144 DESREKVVRQI----LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE--LP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1481 RDRAEAEAREKETKalslaraleealeakeeferqnkqlraDMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEE 1560
Cdd:PRK03918 218 ELREELEKLEKEVK---------------------------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1561 LEDELQATEDAKLRLEvNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELEAELED-ERKQRALAVASKKKME 1633
Cdd:PRK03918 271 LKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKElEEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1634 I--DLKDLEAQIEAANKARdEVIKQLRKLQAQMKDY-----QRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEEL 1706
Cdd:PRK03918 350 LekRLEELEERHELYEEAK-AKKEELERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1707 ASSERARRH--------AEQERDEL-----------ADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN- 1766
Cdd:PRK03918 429 EELKKAKGKcpvcgrelTEEHRKELleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEl 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1767 ----------------DRFRKTTLQVDTLNTE---LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATIS 1827
Cdd:PRK03918 509 eeklkkynleelekkaEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1828 ALEAKIGQLEEqLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEatRAN 1907
Cdd:PRK03918 589 ELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELR 665
|
570 580 590
....*....|....*....|....*....|..
gi 1039738675 1908 ASRRKLQRELDDATEANEGLSREVSTLKNRLR 1939
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1192-1421 |
8.69e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1192 ALEDETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQV 1271
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1272 QELHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1351
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1352 EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1421
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
870-1400 |
1.02e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.62 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 870 ELLKVKEKQTKVEGELEEMERKHQQLLEEKnilAEQLQAETELF----AEAEEMRARLAAKKQELEEILHDLESRVEEEE 945
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 946 ERNQILQNEKKKMQAHIqdleeqldeeegaRQKLQLEKVTAEAKIKKMEEEV-LLLEDQNSKFIKEKKLMEDRIAECSSQ 1024
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKI-------------REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1025 LAEEEEKAKNLAKIRNKQEV---MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKK 1098
Cdd:pfam12128 453 LNQATATPELLLQLENFDERierAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSALDELELQLFPQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1099 ---------------EEELQGALARG---------------------------DDETLHKNNALKVARELQAQIAELQED 1136
Cdd:pfam12128 533 agtllhflrkeapdwEQSIGKVISPEllhrtdldpevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEA 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1137 FESEKASRNKAEKQKRDLSEELEALKTELEDTLDT-----------TAAQQELRTKREQEVAELKKALEDETKNHEAQIQ 1205
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1206 DMRQRHATALEELSEQLEQAKRFK------------ANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR-------KK 1266
Cdd:pfam12128 693 QLDKKHQAWLEEQKEQKREARTEKqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpdviAK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1267 LDAQVQELHAKVSEGDRLRVELAE-----------KANKLQNELDNVSTLLEEAEKKGIKFAKDA----AGLESQL---Q 1328
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTklrrAKLEMERkasE 852
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1329 DTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKnLEKQVLALQSQLADTKKKVDDDLGTIESL 1400
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
818-1601 |
1.09e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.83 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 818 KKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLE 897
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIR 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 898 EKNILAEQLQAETEL-------FAEAE------EMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQD 964
Cdd:TIGR00606 365 ARDSLIQSLATRLELdgfergpFSERQiknfhtLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 965 LEEQLDEEEGARQ--KLQLEKVTAEAK-IKKMEEEV------LLLEDQNS----KFIKEKKLMEDRIAECSSQLAEEEEK 1031
Cdd:TIGR00606 445 KKEILEKKQEELKfvIKELQQLEGSSDrILELDQELrkaereLSKAEKNSltetLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1032 A-KNLAKIRNKQEVMISD--------------------------------LEERLKKEEKTRQELEKAKRKLDGETTDLQ 1078
Cdd:TIGR00606 525 EqLNHHTTTRTQMEMLTKdkmdkdeqirkiksrhsdeltsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1079 DQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKN--NALKVARELQAQIA---ELQEDFESEKASRN-------- 1145
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERlkEEIEKSSKQRAMLAgatAVYSQFITQLTDENqsccpvcq 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1146 ---KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL 1222
Cdd:TIGR00606 685 rvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK----LQKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1223 EqakRFKANLEKNKQGLETDN------KELACEVKVLQQVKAESEHKRKKLDAQVQELHAkvSEGDRLRVELAEKANKLQ 1296
Cdd:TIGR00606 761 Q---RLKNDIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQ 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1297 NELDNVSTLLEEAEKkgikfakdaaglesqlqdtqeLLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV 1376
Cdd:TIGR00606 836 HELDTVVSKIELNRK---------------------LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1377 LALQSQLADTKKKVDDDLgtieSLEEAKKKLLKDVEAL-SQRLEEKVLAYDKLEKTKNRLQQELDDLTvDLDHQRQIVSN 1455
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDS----PLETFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHGYMK-DIENKIQDGKD 969
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1456 LEKKQKKfdqllAEEKGISARYAEERDRaeaeaREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK 1535
Cdd:TIGR00606 970 DYLKQKE-----TELNTVNAQLEECEKH-----QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1536 NVHELEkskralEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQ---FERDLQTRDEQNEEKK 1601
Cdd:TIGR00606 1040 HLKEMG------QMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQFRDAEEK 1102
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
856-1387 |
1.18e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELE 931
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 932 EILHDLESRVEEEEernQILQNEKKKMQAHIQDLEEQLDEEEGARQKL-QLEKVTAEAKIKKMEEEVLLLEDQnsKFIKE 1010
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELeEMTKFKNNKEVELEELKKILAEDE--KLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1011 KKLMEdRIAEcssQLAEEEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1090
Cdd:pfam05483 424 KKQFE-KIAE---ELKGKEQELIFLLQAREKE---IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1091 LKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQedfESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1170
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1171 TTAAQQELRTKREQEVAELKKA---LEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1247
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1248 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAnklQNELDNVSTLLEEAEKKGIKFAKDAaglESQL 1327
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1328 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK 1387
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1558-1940 |
1.67e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1558 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERKQRALAVASKKKME--ID 1635
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ-EELEELEEELEELEAELEELREELEKLEklLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1636 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDY---QRELEEARASRDEIFAQ--------SKESEKKLKSLEAEILQLQE 1704
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1705 ELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1784
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1785 A--------ERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKL-VR 1855
Cdd:COG4717 287 AllflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1856 RTEKKLKEIFMQV----EDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEANEGLSR 1929
Cdd:COG4717 367 ELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEE 446
|
410
....*....|.
gi 1039738675 1930 EVSTLKNRLRR 1940
Cdd:COG4717 447 ELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1595-1799 |
1.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1595 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEE- 1673
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1674 --------------ARASRDEIFAQSKESEKKLKSLE----------AEILQLQEELASSERARRHAEQERDELADEIAN 1729
Cdd:COG4942 103 keelaellralyrlGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1730 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQ 1799
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1548-1760 |
2.57e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1548 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVA 1627
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1628 SKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELA 1707
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1708 SSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1760
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1119-1322 |
2.80e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1119 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETK 1198
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1199 NHEAQIQDMRQRHATA------------------------LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1254
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1255 QVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAG 1322
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1374-1940 |
3.52e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.08 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1374 KQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIV 1453
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1454 SNLEKKQKKFDQLLAEEKgisARYAEERD--RAEAEAREKETKALSlarALEEALEAKEEFERQNKQLRadmedlmsSKD 1531
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKALT---GKHQDVTAKYNRRRSKIKEQ--------NNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1532 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaqferdlqtrdEQNEEKKRLllkqvrel 1611
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL--------------------EFNEEEYRL-------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1612 EAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1691
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLL----QLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1692 LKSLEAEILQLQEELASS-----ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR----- 1742
Cdd:pfam12128 515 LEERQSALDELELQLFPQagtllHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1743 ------RLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1816
Cdd:pfam12128 595 waaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1817 AVKSKFKATISALEAKIGQLEEQLeQEAKERAAANKLVRRTEKklKEIFMQVEDERRhaDQYKEQMEKANARMKQLKRQL 1896
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALD--AQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738675 1897 EEAEEEATRANASRrklqrelDDATEANEGLSREVSTLKNRLRR 1940
Cdd:pfam12128 750 KALETWYKRDLASL-------GVDPDVIAKLKREIRTLERKIER 786
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1206-1818 |
3.81e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1206 DMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLR 1285
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1286 VELAEKANKLQNELDNVstlleeaekkgikfakdaaglesqlqdtqellqeetrqklnlsSRIRQLEEEKNSLqeqQEEE 1365
Cdd:PRK01156 256 SEIKTAESDLSMELEKN-------------------------------------------NYYKELEERHMKI---INDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1366 EEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLlkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVD 1445
Cdd:PRK01156 290 VYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1446 LDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalslaraleealeakeeferqnkqLRADMED 1525
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA----------------------------IKKELNE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1526 LMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDE---------LQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ 1596
Cdd:PRK01156 414 INVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1597 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEI-DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQR-ELEEA 1674
Cdd:PRK01156 494 DIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLeDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRtSWLNA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1675 RASRD--EIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEiANSASGKSALLDEKRRLEARIAQLE 1752
Cdd:PRK01156 574 LAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE-ANNLNNKYNEIQENKILIEKLRGKI 652
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1753 EELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV 1818
Cdd:PRK01156 653 DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
915-1748 |
4.56e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 915 EAEEMRARLAAKKQELEEILHDLESRVeeeeernqilqnekKKMQAHIQDLEEQLDEEEGARQKLQL--EKVTAEAKIKK 992
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMA--------------RELAELNEAESDLEQDYQAASDHLNLvqTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 993 MEEEVLLLEDQnskfiKEKKLMEdrIAECSSQLAEEEEKAKnlakiRNKQEV-----MISDLEERLKkEEKTR------- 1060
Cdd:PRK04863 353 YQADLEELEER-----LEEQNEV--VEEADEQQEENEARAE-----AAEEEVdelksQLADYQQALD-VQQTRaiqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1061 -QELEKAKRKL---DGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETlhknNALKVARELQAQIaELQED 1136
Cdd:PRK04863 420 vQALERAKQLCglpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEV-SRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1137 FESEKASRNKAEKQkRDLSEELEALKTELEDtldttaAQQELRTKREQE--VAELKKALEdETKNHEAQIQDMRQRHATA 1214
Cdd:PRK04863 495 WDVARELLRRLREQ-RHLAEQLQQLRMRLSE------LEQRLRQQQRAErlLAEFCKRLG-KNLDDEDELEQLQEELEAR 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1215 LEELSEQLEQAkrfkanleknkqgletdnkelacevkvlQQVKAESEHKRKKLDAQVQELHAKVSEGdrlrVELAEKANK 1294
Cdd:PRK04863 567 LESLSESVSEA----------------------------RERRMALRQQLEQLQARIQRLAARAPAW----LAAQDALAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1295 LQneldnvstlleeaEKKGIKFAkDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEK 1374
Cdd:PRK04863 615 LR-------------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1375 QVLA-LQSQLADtkkkvD---DDLGTIES-------------LEEAKKKLLKD---------VEALSQRLEEKVLAYDKL 1428
Cdd:PRK04863 681 RFGGvLLSEIYD-----DvslEDAPYFSAlygparhaivvpdLSDAAEQLAGLedcpedlylIEGDPDSFDDSVFSVEEL 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1429 EKT--------------------------KNR---LQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAE 1479
Cdd:PRK04863 756 EKAvvvkiadrqwrysrfpevplfgraarEKRieqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADP 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1480 ERDRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelekskRALEQQVEEMRTQL 1558
Cdd:PRK04863 836 EAELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ETLADRVEEIREQL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1559 EELEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELeaeleDERKQRALAVASKKKM 1632
Cdd:PRK04863 904 DEAEEAkrfVQQHGNALAQLEpivSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TEVVQRRAHFSYEDAA 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1633 EIDLKD------LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaeiLQLQEEL 1706
Cdd:PRK04863 978 EMLAKNsdlnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG---VPADSGA 1054
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1039738675 1707 AssERARRHaeqeRDELADEIANSASGKSALLDEKRRLEARI 1748
Cdd:PRK04863 1055 E--ERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1452-1922 |
4.70e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1452 IVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskd 1531
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1532 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE-VNMQAMKAQFERDLQTRDEQNEEKKRL--LLKQV 1608
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEELEELLEQLSLATEEELqdLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1609 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQM-------------KDYQRELEEAR 1675
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAaallallglggslLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1676 ASRDEIFAQSKESEKKLKsleAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1755
Cdd:COG4717 280 FLVLGLLALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1756 EEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSdNARQQLERQNKELKAKLQELEGAVKSKFKA-TISALEAKIG 1834
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1835 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQ 1914
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
....*...
gi 1039738675 1915 RELDDATE 1922
Cdd:COG4717 516 PVLERASE 523
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1530-1750 |
4.87e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1530 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVR 1609
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1610 ELEAELEDERKQRALAVASKKKMEID--LKDLEAQIEAANKARDEVIK-------QLRKLQAQMKDYQREL-EEARASRD 1679
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1680 EIFAQSKESEKKLKSLEAEILQLQEELAS-SERARRHAEQERD-ELADEIANSasgksaLLdeKRRLEARIAQ 1750
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1082-1382 |
6.27e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.00 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1082 AELQAQVDELKVQltKKEEELQGALARGDDETLhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL 1161
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTL----------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1162 KTELEDTLDTTAAQQELR------TKREQEVAELKKALeDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKN 1235
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRqlesrlAQTLDQLQNAQNDL-AEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1236 KQGLETDNK-ELACEvkvLQQVKAESEHKRKKLDA--QVQELhakvseGDRLRVELAEKANKLQNELdnvsTLLEEA--E 1310
Cdd:PRK11281 186 GKALRPSQRvLLQAE---QALLNAQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL----QLLQEAinS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1311 KKGIKFAKDAAGLESQlQDTQE-----LLQEETRQKLNLSSRIRQLEEEKNSLQeqqeeeeeaRKNLE-KQVL--ALQSQ 1382
Cdd:PRK11281 253 KRLTLSEKTVQEAQSQ-DEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLT---------QQNLRvKNWLdrLTQSE 322
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1475-1847 |
6.80e-08 |
|
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: 57.21 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1475 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1554
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1555 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQVRELEAELEDERKQRALAVASKKkmei 1634
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1635 dlkdLEAQIEAANKARDEVIKQLRKL-QAQMKDYQRE--LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1711
Cdd:pfam07888 201 ----LAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1712 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERsaaq 1791
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK---- 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1792 ksDNARQQL---ERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKER 1847
Cdd:pfam07888 353 --DCNRVQLsesRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
855-1227 |
7.01e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 855 LQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEL---- 930
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 931 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1010
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1011 KK---------------LMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1075
Cdd:COG4717 271 LIltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1076 DLQDQIAELQAQVdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQkrdls 1155
Cdd:COG4717 351 ELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA----- 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1156 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEaqIQDMRQRHATALEELSEQLEQAKR 1227
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1368-1631 |
8.53e-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: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1368 ARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTvdld 1447
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1448 hqrqivSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1527
Cdd:COG4942 83 ------AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1528 SSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRlLLKQ 1607
Cdd:COG4942 157 ADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEAL 228
|
250 260
....*....|....*....|....
gi 1039738675 1608 VRELEAELEDERKQRALAVASKKK 1631
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1266-1820 |
9.43e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1266 KLDAQVQELHAKVSEGDRLRVELAEKanklQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQ---DTQELLQEETRQKL 1342
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSS----NLELENIKKQIADDEKSHSITLKEIERLSIEYNnamDDYNNLKSALNELS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1343 NLSSRIRQLEEE---KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLE 1419
Cdd:PRK01156 246 SLEDMKNRYESEiktAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1420 E--KVLA--------YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1489
Cdd:PRK01156 326 AiiKKLSvlqkdyndYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1490 EketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL---------------EKSKRALEQQVEE- 1553
Cdd:PRK01156 406 A-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeEKSNHIINHYNEKk 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1554 --MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKkRLLLKQVRELEAELEDERKQRALAVASKKK 1631
Cdd:PRK01156 479 srLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1632 MeiDLKDLEAQ---------------IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFaqsKESEKKLKSLE 1696
Cdd:PRK01156 558 L--KLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI---REIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1697 AEILQLQEELASSERARRHAEQERDELAdeiansasGKSALLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTLQV 1776
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND--------------IEDNLKKSRKAL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738675 1777 DTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKS 1820
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
880-1343 |
9.69e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 880 KVEGELEEMERKHQQLLEeknILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdLESRVEEEEERNQILQNEKKKMQ 959
Cdd:COG4717 50 RLEKEADELFKPQGRKPE---LNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 960 AHIqdleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR 1039
Cdd:COG4717 123 KLL------------QLLPLYQELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1040 NKQEvmisdlEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE------------------ 1101
Cdd:COG4717 187 SLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaalla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1102 LQGALARGDDETLHKNNAL---------------KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1166
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1167 DTLDTTAAQQELRTKREQEVAELKKAledetKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQ-----GLET 1241
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEEleeqlEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1242 DNKELACEVKVLQQVKAESEHKRKKLDA---QVQELHAKVSEgDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAK 1318
Cdd:COG4717 416 GELEELLEALDEEELEEELEELEEELEEleeELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|....*
gi 1039738675 1319 DAAGLESqLQDTQELLQEETRQKLN 1343
Cdd:COG4717 495 LKLALEL-LEEAREEYREERLPPVL 518
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
989-1852 |
1.01e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.75 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 989 KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAK--------NLAKIRNKQEVMISD------------ 1048
Cdd:TIGR01612 815 KSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKekidseheQFAELTNKIKAEISDdklndyekkfnd 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1049 ----LEERLKKEEKTRQELEKAKrKLDG-----ETTdlQDQIAELQAQVDELKVQLTKKEEELQgalargDDETLHKNNA 1119
Cdd:TIGR01612 895 skslINEINKSIEEEYQNINTLK-KVDEyikicENT--KESIEKFHNKQNILKEILNKNIDTIK------ESNLIEKSYK 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1120 LKVARELQAQIAELQEDFEseKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQelRTKREQEVAELKKALEDETKN 1199
Cdd:TIGR01612 966 DKFDNTLIDKINELDKAFK--DASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQ--FDEKEKATNDIEQKIEDANKN 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1200 heaqIQDMRQRHATALEELSEQLEqaKRFKANLEK-NKQGLETDNKELACEVKVLQQVK------------AESEHKRKK 1266
Cdd:TIGR01612 1042 ----IPNIEIAIHTSIYNIIDEIE--KEIGKNIELlNKEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINK 1115
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1267 LDAQVQELHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIK--FAKDAAGLESQLQ------DTQELLQEET 1338
Cdd:TIGR01612 1116 IKDDIKNLDQKI---DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKaiSNDDPEEIEKKIEnivtkiDKKKNIYDEI 1192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1339 RQKLNlssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLalqSQLADTKKKVDDdlgTIESLEeAKKKLLKDVEALSQRL 1418
Cdd:TIGR01612 1193 KKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGKLFL---EKIDEEKKKSEH---MIKAME-AYIEDLDEIKEKSPEI 1262
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1419 EEKVLAYDKLEKTKNRLQQELDD----LTVDLDHQRQIvSNLEKKQKKFDQLLAEEKGIS------ARYAEERDRAEAEA 1488
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI-SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDI 1341
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1489 REKETKALSLARALEEALEakeeferqnKQLRADMEDLMSSKDDVGKNVH-ELEKSKRALEQQVEEmrTQLEELEDELQA 1567
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKI---------KKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDD--INLEECKSKIES 1410
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1568 TEDAKLRLEV--NMQAMKAQF---ERDLQT---RDEQNEEKKRLLLKQVreleaELEDERKQRALAVA---SKKKMEIDL 1636
Cdd:TIGR01612 1411 TLDDKDIDECikKIKELKNHIlseESNIDTyfkNADENNENVLLLFKNI-----EMADNKSQHILKIKkdnATNDHDFNI 1485
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1637 KDLEAQIEAANKARDEV---IKQLRKLQAQMKDYQRE---------------------------LEEARASRDEIFAQSK 1686
Cdd:TIGR01612 1486 NELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDvtellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAE 1565
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1687 ESEKKLKSLEAEILQLQEELASSERARRHAEQERDELAD------EIANSASGKSALLDEKRRLEARIaqleeeleeeqs 1760
Cdd:TIGR01612 1566 KSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKINDCLKETESIEKKI------------ 1633
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1761 nmellndrfrkTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGaVKSKFKATISALEAKIGQLEEQL 1840
Cdd:TIGR01612 1634 -----------SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE-LDSEIEKIEIDVDQHKKNYEIGI 1701
|
970
....*....|..
gi 1039738675 1841 EQEAKERAAANK 1852
Cdd:TIGR01612 1702 IEKIKEIAIANK 1713
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
884-1108 |
1.02e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 884 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIq 963
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 964 dleeqldeeegARQKLQLEKVTAEA-KIKKMEEEVLLLEDQN-SKFIKEKKLME-------DRIAECSSQLAEEEEKAKN 1034
Cdd:COG4942 100 -----------EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKylaparrEQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1035 LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1108
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1287-1918 |
1.88e-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: 56.27 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1287 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNSLQEQQEE 1364
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1365 EEEA-----RKNLEKQVLALQSQLADTKK-------KVDDDLGTIESLEEAKKKLLKDVEAlsqrlEEKVLAYDKLEKtk 1432
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEINDKEK-----QVSLLLIQITEK-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1433 nrlQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerDRAEAEAREKETKALSLARALEEALEAKEEF 1512
Cdd:pfam05483 253 ---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI----------EKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1513 ERQNKQL-------RADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAM 1582
Cdd:pfam05483 320 QIATKTIcqlteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1583 KAQFERDLQTRDEQNEEKKRLLL--KQVRELEAELEDERKQRALAVASKKKmeiDLKDLEAQIEAANKARDEVIKQLRKL 1660
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1661 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERarrhaeqERDELADEIANSASGKSALLDE 1740
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK-------QEERMLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1741 krrLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELaaeRSAAQKSDNARQQLERQNKELKaKLQELEGAVKS 1820
Cdd:pfam05483 550 ---LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM---KILENKCNNLKKQIENKNKNIE-ELHQENKALKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1821 KFKA---TISALEAKIGQLEEQLEqeakerAAANKLVRRTEKKLKEIfmqvEDERRHADQYKEQMEKANARMKQLKrqle 1897
Cdd:pfam05483 623 KGSAenkQLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV---- 688
|
650 660
....*....|....*....|.
gi 1039738675 1898 eaeeeatranasrrKLQRELD 1918
Cdd:pfam05483 689 --------------KLQKEID 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1139-1378 |
1.94e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1139 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALedetKNHEAQIQDMRQRHATALEEL 1218
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1219 SEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1298
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1299 LDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLA 1378
Cdd:COG4942 173 RAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1287-1934 |
2.12e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.39 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1287 ELAEKANKLQNELDNVSTLleEAEKKGIKFA-KDAAGLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNSLQEQQEEE 1365
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESA--ELRLSHLHFGyKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1366 EEARKNLEKQVLALQSQLadtKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQElddltVD 1445
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH---GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSK-----IK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1446 LDHQRQIVSNLEKKQKKFD----QLLAEEKGISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQ 1518
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREardrQLAVAEDDLQALESELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1519 LRADMEDLMSSKDDVGKNVHELEKSKRAL-----------------EQQVEEMRTQLEELEDELQA----------TEDA 1571
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasealrqaSRRLEERQSALDELELQLFPqagtllhflrKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1572 KLRLEVNMQAMKAQFER--------DLQTRDEQNEEKKRLLLKQVRELE-AELEDERKQRAlavaskKKMEIDLKDLEAQ 1642
Cdd:pfam12128 546 DWEQSIGKVISPELLHRtdldpevwDGSVGGELNLYGVKLDLKRIDVPEwAASEEELRERL------DKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1643 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQsKESEKklksleaeiLQLQEELassERARRHAEQERDE 1722
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE-KQSEK---------DKKNKAL---AERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1723 LADEIANSASGKSALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTLQVDTLNTELAAERSAAqksDNARQQL 1800
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGA---KAELKAL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1801 ERQNK-ELKAKLQELEgavkskfkaTISALEAKIGQLEEQLEQEAKERAAanklVRRTEKKLKEIFMQvederrHADQYK 1879
Cdd:pfam12128 753 ETWYKrDLASLGVDPD---------VIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLA 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1880 EQMEKANARMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTL 1934
Cdd:pfam12128 814 TQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1408-1940 |
2.28e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.21 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1408 LKDVEALSQRLEE------KVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEE------KGISA 1475
Cdd:TIGR00606 165 LSEGKALKQKFDEifsatrYIKALETLRQVRQTQGQKVQEHQMELKYLKQ---YKEKACEIRDQITSKEaqlessREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1476 RYAEERDRAEAEAREKE---TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK-RALEQQV 1551
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1552 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER-------------DLQTRDEQNEEKKRLLLKQVRELEAELEDE 1618
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehirardsliqSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1619 RKQRALAVASKKKMEIDLKDLEAQiEAANKARDEVI----------KQLRKLQAQMKDYQRELEEARASRDEIFAQSKES 1688
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKglgrtielkkEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1689 EKKLKSL------------EAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEK-RRLEARIAQ 1750
Cdd:TIGR00606 481 RKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmeMLTKDKMDKDEQiRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1751 LEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVkskFKATIS-AL 1829
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---FDVCGSqDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1830 EAKIGQLEEQLEQEAKERA---AANKL---------------------VRRTEKKLKEIFMQVEDERRHADQYKEQMEKA 1885
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAmlaGATAVysqfitqltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESE 717
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1886 NARMKqlKRQLEEAEEEATRANASRRKlQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:TIGR00606 718 LKKKE--KRRDEMLGLAPGRQSIIDLK-EKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1538-1934 |
2.40e-07 |
|
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: 56.11 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1538 HELEKSKRAL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQfERDLQTRDEQNEEKKRLllkq 1607
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQ-EKIERYQEDLEELTERL---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1608 vRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEviKQLRKLQAQMKdyQRELEEARA-------SRDE 1680
Cdd:COG3096 364 -EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV--QQTRAIQYQQA--VQALEKARAlcglpdlTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1681 IFAQSKESEKKLKSLEAEILQLQEELASSERARR---HAEQERDELADEIANSASGKSA--LLDEKRRLEARIAQleeel 1755
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTAreLLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1756 eeeqsnmellndrfrkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQ 1835
Cdd:COG3096 514 --------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1836 LEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKeqmeKANARMKQLKRQLEEAEEEATRANASR----- 1910
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMqqlle 637
|
410 420
....*....|....*....|....*.
gi 1039738675 1911 --RKLQRELDDATEANEGLSREVSTL 1934
Cdd:COG3096 638 reREATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1331-1551 |
2.88e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1331 QELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1409
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1410 DVEALSQRLEEKVLAYDKLEKTKNRL----QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1485
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1486 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1551
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1517-1733 |
3.46e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1517 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFeRDLQTRDEQ 1596
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERA-RALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1597 NEEKKRLL--------LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1668
Cdd:COG3883 102 VSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1669 RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASG 1733
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1050-1321 |
6.11e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1050 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQ 1129
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---------------------KLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1130 IAELQEDFESEKA---SRNKAEKQKRDLSEELEALK--TELEDTLDTTAAqqelrtkreqevaelkkaledetknheaqI 1204
Cdd:COG3883 74 IAEAEAEIEERREelgERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-----------------------------L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1205 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRL 1284
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039738675 1285 RVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAA 1321
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
860-1083 |
6.91e-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: 53.61 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 860 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELEEILH 935
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 936 DLESRVEEEEERNQILQnekKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEevllLEDQNSKFIKEKKLME 1015
Cdd:COG4942 98 ELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1016 DRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1083
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1302-1875 |
8.79e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.98 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1302 VSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNslqeqqEEEEEARKNLEKQVLALQS 1381
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREA------EAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1382 QLADTKKKVDDDLgTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQK 1461
Cdd:pfam05557 85 LEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1462 kfdqllaeekgisaryaeerDRAEAEAREKETKalslARALEEALEAKEEFERQNKQLR-ADMEDLMSSKDDVGKNVHEL 1540
Cdd:pfam05557 164 --------------------SLAEAEQRIKELE----FEIQSQEQDSEIVKNSKSELARiPELEKELERLREHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1541 EKSKRALEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKAQFE---------RDLQTRDEQNEEKKRLLLKQV 1608
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSWVKLAQdtglnlrspEDLSRRIEQLQQREIVLKEEN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1609 RELEAELEDERKQRalavaskKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQS 1685
Cdd:pfam05557 300 SSLTSSARQLEKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1686 KESEKKLKSLE--AEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNME 1763
Cdd:pfam05557 373 NYSPQLLERIEeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1764 LL--NDRFR--KTTLQVDTLNTELAAERSAA-----QKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1834
Cdd:pfam05557 453 LEleRQRLReqKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738675 1835 QLEEQLEQEAKERAAANKLVRRTEKK---LKEIFMQVEDERRHA 1875
Cdd:pfam05557 533 LPETTSTMNFKEVLDLRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1060-1923 |
9.15e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1060 RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALARgddetLHK-NNAL----KVAR------ELQA 1128
Cdd:PRK04863 292 RRELYTSRRQLAAE----QYRLVEMARELAELNEAESDLEQDYQAASDH-----LNLvQTALrqqeKIERyqadleELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1129 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALE---------DETKN 1199
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1200 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEH-KRKKLDAQVQELHAKV 1278
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1279 SEGDRlRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1358
Cdd:PRK04863 523 SELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1359 qeqqeeeeeaRKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQrleekvlAYDKLEKTKNRL 1435
Cdd:PRK04863 595 ----------IQRLAARApawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV-------ERDELAARKQAL 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1436 QQELDDL----TVDLDHQRQI--------VSNLekkqkkFDQLLAEEKG-ISARYAEER------DraeaeareketkaL 1496
Cdd:PRK04863 658 DEEIERLsqpgGSEDPRLNALaerfggvlLSEI------YDDVSLEDAPyFSALYGPARhaivvpD-------------L 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1497 SLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEKS----------------------KRALE 1548
Cdd:PRK04863 719 SDAA-------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAARE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1549 QQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEEKKRLLLKQVRELEAELED----E 1618
Cdd:PRK04863 786 KRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1619 RKQRALAVASKKKMEiDLKDLEAQIEAAnkARDEVIKQLRKLQAQMKdyqrELEEARASRDE---IFAQSKESEKKLKSL 1695
Cdd:PRK04863 861 QQQRSQLEQAKEGLS-ALNRLLPRLNLL--ADETLADRVEEIREQLD----EAEEAKRFVQQhgnALAQLEPIVSVLQSD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1696 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAllDEKRRLEAriaqleeeleeEQSNMELLNDRFRKTTLQ 1775
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAK-----------NSDLNEKLRQRLEQAEQE 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1776 VDTLNTELaaeRSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKlvr 1855
Cdd:PRK04863 1001 RTRAREQL---RQAQAQLAQYNQVLASLKSSYDAKRQMLQ------------ELKQELQDLGVPADSGAEERARARR--- 1062
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1856 rtekklKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaeeeatranasrRKLQRELDDATEA 1923
Cdd:PRK04863 1063 ------DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL--------------RKLERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1042-1499 |
1.26e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1042 QEVMISDLEERLKKEektRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQlTKKEEELQGALARGDDETLHKNNALK 1121
Cdd:COG4717 40 LAFIRAMLLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1122 VARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1201
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1202 AQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1281
Cdd:COG4717 192 EELQDLAEE----LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1282 DRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLS-----SRIRQLEEEKN 1356
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1357 SLQEQQEEEEEARKNLEKQVL--ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK--TK 1432
Cdd:COG4717 348 ELQELLREAEELEEELQLEELeqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1433 NRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL--AEEKGISARYAEERDRAEAEAREKETKALSLA 1499
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1070-1312 |
1.58e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1070 LDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlhKNNALKVARELQ---AQIAELQEDFESEKASRNK 1146
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ--------KNGLVDLSEEAKlllQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1147 AEKQKRDLSEELEALKTELEDTLDTTAAQQeLRTKREQEVAELKKALEDETKNHEaQIQDMRQRhataLEELSEQLEQ-A 1225
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSARYTPNHP-DVIALRAQ----IAALRAQLQQeA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1226 KRFKANLEKNKQGLETdnkelacevkvlqqvkaesehKRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTL 1305
Cdd:COG3206 312 QRILASLEAELEALQA---------------------REASLQAQLAQLEARLAELPELEAELRR----LEREVEVAREL 366
|
....*..
gi 1039738675 1306 LEEAEKK 1312
Cdd:COG3206 367 YESLLQR 373
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
861-1273 |
1.70e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 861 EEELQAKDEELLKVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 938
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 939 SrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR- 1017
Cdd:COG4717 174 E---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1018 -------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQElEKAKRKLDGETTDLQDQiaELQAQVDE 1090
Cdd:COG4717 251 llliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK-EAEELQALPALEELEEE--ELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1091 LKVQLTKKEEELQGALARGDDetlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1170
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEE-----------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1171 TTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelacev 1250
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE------ 470
|
410 420
....*....|....*....|...
gi 1039738675 1251 kvLQQVKAESEHKRKKLDAQVQE 1273
Cdd:COG4717 471 --LAELLQELEELKAELRELAEE 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1539-1817 |
1.77e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRdeQNEEKKRLL-----------L 1605
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELerirqeeiameI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1606 KQVRELE--------------AELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1671
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1672 EEARASRDEIFAQsKESEKKLKSLEAEILQLQEELASSERaRRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1751
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1752 EEELEEEQSNMELLNDRFRKTTLQVDTLNTElaaERSAAQKSDNARQQLeRQNKELKAKLQELEGA 1817
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1057-1334 |
1.96e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.84 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1057 EKTRQeLEKAKRKLDGETTDLQDQ---------------IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALK 1121
Cdd:pfam00038 18 DKVRF-LEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1122 VARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTEledtldttaaqqelrtkREQEVAELKKALEDETKNHE 1201
Cdd:pfam00038 97 LRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1202 ---AQIQDMrqrhATALEELSEQLE-QAKRFKANLEKN-KQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1276
Cdd:pfam00038 160 mdaARKLDL----TSALAEIRAQYEeIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1277 KVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiKFAKDAAGLESQLQDTQELL 1334
Cdd:pfam00038 236 LKKQKASLERQLAETEERYELQLADYQELISELEA---ELQETRQEMARQLREYQELL 290
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1610-1856 |
2.00e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1610 ELEAELeDERKQRALAVASKKKMEIDLK---DLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1686
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1687 ES------EKKLKSLEAEILQLQEELAS-----------SERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1745
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1746 ARIAQleeeleeeqsnMELLNDrFRKTTLQVDTLNTELAAER----SAAQksdnarQQLERQnkelkakLQELEGAVKSK 1821
Cdd:PRK11281 199 AEQAL-----------LNAQND-LQRKSLEGNTQLQDLLQKQrdylTARI------QRLEHQ-------LQLLQEAINSK 253
|
250 260 270
....*....|....*....|....*....|....*
gi 1039738675 1822 fkatisALEAKIGQLEEQLEQEAKERAAANKLVRR 1856
Cdd:PRK11281 254 ------RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1549-1926 |
3.08e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1549 QQVEEMRTQLEELEDELQATEDAKLRL---EVNMQAMKAQFERDLQTRDEQNEEKK---RLLLKQVRELEAELEDERKQR 1622
Cdd:pfam12128 234 AGIMKIRPEFTKLQQEFNTLESAELRLshlHFGYKSDETLIASRQEERQETSAELNqllRTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1623 ALAVAsKKKMEIDLkdLEAQIEAANKARDEVIK----QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS-LEA 1697
Cdd:pfam12128 314 DAAVA-KDRSELEA--LEDQHGAFLDADIETAAadqeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1698 EILQLQEELASS--ERARRHAEQE----------RDELADEIANSASG----KSALLDEKRRLEARIAQLEEELEEEQSN 1761
Cdd:pfam12128 391 DIAGIKDKLAKIreARDRQLAVAEddlqaleselREQLEAGKLEFNEEeyrlKSRLGELKLRLNQATATPELLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1762 MEL--LNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatiSALEAKIGQLEEQ 1839
Cdd:pfam12128 471 ERIerAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE-----------LQLFPQAGTLLHF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1840 LEQEAKE------RAAANKLVRRTEK--------------------KLKEI----FMQVEDE-RRHADQYKEQMEKANAR 1888
Cdd:pfam12128 540 LRKEAPDweqsigKVISPELLHRTDLdpevwdgsvggelnlygvklDLKRIdvpeWAASEEElRERLDKAEEALQSAREK 619
|
410 420 430
....*....|....*....|....*....|....*...
gi 1039738675 1889 MKQLKRQLEEaeeeatrANASRRKLQRELDDATEANEG 1926
Cdd:pfam12128 620 QAAAEEQLVQ-------ANGELEKASREETFARTALKN 650
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1683-1922 |
3.39e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1683 AQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDeladeIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNM 1762
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1763 ELLNDRFRKTTLQVDTLNtelaaersaaqkSDNARQQLERQNKELKAKLQELEgavkSKFKA---TISALEAKIGQLEEQ 1839
Cdd:COG3206 243 AALRAQLGSGPDALPELL------------QSPVIQQLRAQLAELEAELAELS----ARYTPnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1840 LEQEAKERAAanklvrrtekklkEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEaeeeatranasRRKLQRELDD 1919
Cdd:COG3206 307 LQQEAQRILA-------------SLEAELEALQAREASLQAQLAQLEARLAELPELEAE-----------LRRLEREVEV 362
|
...
gi 1039738675 1920 ATE 1922
Cdd:COG3206 363 ARE 365
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
919-1380 |
4.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 919 MRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVL 998
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 999 LLED--QNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNkqevmisDLEERLKKEEKTRQELEKAKRKLDGET-- 1074
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-------ELEELEAELAELQEELEELLEQLSLATee 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1075 --TDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDD-----ETLHKNNALKVARELQAQIAELQEdFESEKASRNKA 1147
Cdd:COG4717 193 elQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlenelEAAALEERLKEARLLLLIAAALLA-LLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1148 EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKR 1227
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1228 FKANLEKNKQGLETDNKELACEvKVLQQVKAESEHKRKKLDAQVQELHAkvsegdrLRVELAEKANKLQNELDNVSTLLE 1307
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQE-------LKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1308 EAEKKGIKfaKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKN--SLQEQQEEEEEARKNLEKQVLALQ 1380
Cdd:COG4717 424 ALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1584-1922 |
4.17e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1584 AQFERDLQ-TRDEQNEEKKRLL-----LKQVRELEAELEDE---------RKQRALAVASK-KKMEIDLKDLEAQIEAAN 1647
Cdd:COG3096 288 LELRRELFgARRQLAEEQYRLVemareLEELSARESDLEQDyqaasdhlnLVQTALRQQEKiERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1648 KARDEVIKQLRKLQAQmkdyqreLEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR-------HAEQER 1720
Cdd:COG3096 368 EVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcglpdlTPENAE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1721 DELADEIANSASGKSALLDEKRRLeariaqleeeleeeqSNMELLNDRFRKTtLQvdtLNTELAAERSAAQKSDNARQQL 1800
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKL---------------SVADAARRQFEKA-YE---LVCKIAGEVERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1801 eRQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqvederrHADQYKE 1880
Cdd:COG3096 502 -RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----------AAEELEE 557
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039738675 1881 QMEKANARMKQLKRQLEeaeeeatRANASRRKLQRELDDATE 1922
Cdd:COG3096 558 LLAELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRA 592
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1081-1337 |
4.32e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 52.14 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1081 IAELQAQVDELKVQLTKKEEElQGALArgdDETLHKNNALKVARELQAQIAEL---QEDFES--EKASRNKAEKQKRDLS 1155
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAA-QNALA---DKERAEADRQRLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1156 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKALE---DETKNH-EAQIQDMRQRHATALEELSEQLE 1223
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1224 QAKRFKANLEKNKQGLETDNKelacevkvlqqvKAESEHKRKKLDAQVQELHAKVSEGDrlrvelaekanklqneldnVS 1303
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAESD-------------------AN 1741
|
250 260 270
....*....|....*....|....*....|....*
gi 1039738675 1304 TLLEEAEKKGIKFAKDAAGLESQLQ-DTQELLQEE 1337
Cdd:NF012221 1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1599-1894 |
4.44e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1599 EKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR 1678
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1679 DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKsALLDEKRRLEARIAQLEEELEEE 1758
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1759 QSNMELLNdRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELegavkskfKATISALEAKIGQLEE 1838
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1839 QLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRHADQyKEQMEKANARMKQLKR 1894
Cdd:COG1340 231 EIIELQKE-------LRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
861-1447 |
4.67e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 861 EEELQAKDEELLKVKE-------KQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 933
Cdd:PRK01156 189 EEKLKSSNLELENIKKqiaddekSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 934 LHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ---LEKVTAEAKIKKMEEevllLEDQNSKFIKE 1010
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1011 KKLMEDRIAECS----------SQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:PRK01156 345 KSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1081 IAELQAQVDELKVQLTKKEEELQGALAR----------GDDETLH--------KNNALKVARELQAQIAELQEDFESEKA 1142
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlGEEKSNHiinhynekKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1143 SRNKAEKQKRDLSE----ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATALEE 1217
Cdd:PRK01156 505 RKEYLESEEINKSIneynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1218 LSEQLEQAKRFKANLEKNKQGLETDnkelacevkvLQQVKAESEHKRKKLDAQVQELHAKVsegdrlrvelaekanklqN 1297
Cdd:PRK01156 585 NRSRSNEIKKQLNDLESRLQEIEIG----------FPDDKSYIDKSIREIENEANNLNNKY------------------N 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1298 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEllqeetrqklnLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1377
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-----------ITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1378 ALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDV-EALSQ-------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLD 1447
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKKAIgdLKRLrEAFDKsgvpamiRKSASQAMTSLTRKYLFEFNLDFDDIDVDQD 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
812-1309 |
4.98e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 812 ARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWWRVFTKVKpLLQ--VTRQEEELQAKDEELLKVKEKQ 878
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 879 TKV-----------------------------EGELEEMERKHQQLLEekniLAEQLQAETELFAEA-EEMRARLAAKKQ 928
Cdd:COG4913 319 DALreeldeleaqirgnggdrleqlereierlERELEERERRRARLEA----LLAALGLPLPASAEEfAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 929 ELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLeeqldeeegARQKLQLEKvtAEAKIKKMEEEVLLLEDQNSKFI 1008
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASL---------ERRKSNIPA--RLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1009 KEkkLMEDRIAECSSQLAEE-------------EEKAKNLAKI--RNKQEVMISDLEERLKKEEKTRQELEKAK--RKLD 1071
Cdd:COG4913 464 GE--LIEVRPEEERWRGAIErvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPDSlaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1072 GETTDLQDQI-AELQAQVDELKVQltkKEEELQ---------------GALARGDDETLHK-------NNALKVAReLQA 1128
Cdd:COG4913 542 FKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitragqvkgnGTRHEKDDRRRIRsryvlgfDNRAKLAA-LEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1129 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE---DTLDTTAAQQELRTKrEQEVAELKKAlEDETKNHEAQIQ 1205
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAEL-EAELERLDAS-SDDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1206 DMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgDRLR 1285
Cdd:COG4913 696 ELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLEERFAAALGDAVE-RELR 768
|
570 580
....*....|....*....|....
gi 1039738675 1286 VELAEKANKLQNELDNVSTLLEEA 1309
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1402-1652 |
7.80e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1402 EAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKkfdqllaeekgisaryAEER 1481
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----------------ALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1482 DRAEAEAREKETKAlSLARALEEALEAKEEFERQNKQLRADMedLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLE 1559
Cdd:COG4942 84 ELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDflDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1560 ELE---DELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRL--LLKQVRELEAELEDERKQRALAVASKKKMEI 1634
Cdd:COG4942 161 ELAalrAELEAERAELEAL-----------------LAELEEERAALeaLKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*...
gi 1039738675 1635 DLKDLEAQIEAANKARDE 1652
Cdd:COG4942 224 ELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1127-1346 |
7.85e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1127 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQD 1206
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1207 MRQ--RHATALEEL--SEQLEQakrFKANLEKNKQGLETDNKELacevKVLQQVKAESEHKRKKLDAQVQELHAKVSEGD 1282
Cdd:COG3883 95 LYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1283 RLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSS 1346
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1625-1792 |
8.55e-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: 49.15 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1625 AVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQE 1704
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1705 ELASSERARrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1784
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*...
gi 1039738675 1785 AERSAAQK 1792
Cdd:COG1579 156 AELEELEA 163
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1410-1666 |
9.34e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1410 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLD--HQRQIVS--NLEKKQKKFDQllAEEKGISARYAEERDRAE 1485
Cdd:pfam05667 227 NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTeaTSGASRSaqDLAELLSSFSG--SSTTDTGLTKGSRFTHTE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1486 AEAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1563
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVETEEELQQQREEEleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1564 ELQATEDAKLRL---EVNMQAMKAQFE---RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQralavASKKKMEI-DL 1636
Cdd:pfam05667 385 QYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE-----SQRKLEEIkEL 459
|
250 260 270
....*....|....*....|....*....|
gi 1039738675 1637 KDLEAQIEAANKARDEVIKQlrkLQAQMKD 1666
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1517-1736 |
9.51e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1517 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDEL-------QATEDAKLRLEV------------ 1577
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralYRSGGSVSYLDVllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1578 NMQAMKAQFERDLQTRDEQNEEKKRLllkqvRELEAELEDERKQralAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1657
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAEL-----EAKKAELEAKLAE---LEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1658 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA 1736
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1015-1188 |
1.08e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1015 EDRIAECSSQLAEEEEKAKNLakirnKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQ------- 1087
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQlgsgpda 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1088 ---------VDELKVQLTKKEEELQGALARGDDEtlHknnalKVARELQAQIAELQEDFESE--------KASRNKAEKQ 1150
Cdd:COG3206 256 lpellqspvIQQLRAQLAELEAELAELSARYTPN--H-----PDVIALRAQIAALRAQLQQEaqrilaslEAELEALQAR 328
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039738675 1151 KRDLSEELEALKTELEDTLDTTAAQQELrtKREQEVAE 1188
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRL--EREVEVAR 364
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1216-1865 |
1.15e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1216 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSegdRLRVELAEKA--- 1292
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS---AQRVELAERQlqe 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1293 NKLQN-ELDNVSTLLEEAEKKGIKFAKDaaglesqlqdTQELLQEETRQKLNLSSRirqLEEEKNSLQEQQEEEEEARKN 1371
Cdd:COG5022 887 LKIDVkSISSLKLVNLELESEIIELKKS----------LSSDLIENLEFKTELIAR---LKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1372 LEKQVLALQ-SQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1450
Cdd:COG5022 954 PELNKLHEVeSKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1451 QIVSNLEKKQKKfdQLLAEEKGISAryaeerdrAEAEAREKETKALSLARALEEALEAKEEFER--QNKQLRADMEDLMS 1528
Cdd:COG5022 1034 IISSESTELSIL--KPLQKLKGLLL--------LENNQLQARYKALKLRRENSLLDDKQLYQLEstENLLKTINVKDLEV 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1529 SKDDVGKNVHELEK-----SKRALEQQVEEMRTQLeeledeLQATEDAKLRLEVNMQAMKAQFerDLQTRDEQNEEKKRL 1603
Cdd:COG5022 1104 TNRNLVKPANVLQFivaqmIKLNLLQEISKFLSQL------VNTLEPVFQKLSVLQLELDGLF--WEANLEALPSPPPFA 1175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1604 LLKQVRELEAELEDERKQRALAVASKKKMEIDLkdlEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1683
Cdd:COG5022 1176 ALSEKRLYQSALYDEKSKLSSSEVNDLKNELIA---LFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDT 1252
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1684 QSKESEKKLKSLEAEI---LQLQEELASSERARRHAEQER--DELADEIANSAS-GKSALLDEKRRLEARIAQLEEELEE 1757
Cdd:COG5022 1253 PASMSNEKLLSLLNSIdnlLSSYKLEEEVLPATINSLLQYinVGLFNALRTKASsLRWKSATEVNYNSEELDDWCREFEI 1332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1758 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNarqQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLE 1837
Cdd:COG5022 1333 SDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLN---PAEIQNLKSRYDPADKENNLPKEILKKIEALLIK---QE 1406
|
650 660
....*....|....*....|....*...
gi 1039738675 1838 EQLEQEAKeraaanklvRRTEKKLKEIF 1865
Cdd:COG5022 1407 LQLSLEGK---------DETEVHLSEIF 1425
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1403-1669 |
1.19e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1403 AKKKLLKDVealsqrLEEKVLA-YDKLEKTKNR-LQQELDDLTVDLDH-QRQIVS--------------NLEKKQKKFDQ 1465
Cdd:PHA02562 151 ARRKLVEDL------LDISVLSeMDKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1466 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadmedlMSSKDDV----GKNVHELE 1541
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIK------MYEKGGVcptcTQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1542 KSKRALEQQVEEMRTQLEELEDELQatEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEderkq 1621
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIE----- 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039738675 1622 ralavaskkKMEIDLKDLEAQIEAANKARDEVIKQLRKLqaQMKDYQR 1669
Cdd:PHA02562 369 ---------ELQAEFVDNAEELAKLQDELDKIVKTKSEL--VKEKYHR 405
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
667-691 |
1.29e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.29e-05
10 20
....*....|....*....|....*
gi 1039738675 667 YKESLTKLMATLRNTNPNFVRCIIP 691
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
897-1146 |
1.36e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 897 EEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegar 976
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 977 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQevmISDLEERLKKE 1056
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ---AEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1057 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQED 1136
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1039738675 1137 FESEKASRNK 1146
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1029-1438 |
1.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1029 EEKAKNLAKIRNKQEVM----ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQVDELKVQLTKKEEELQG 1104
Cdd:COG4717 52 EKEADELFKPQGRKPELnlkeLKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1105 AlargddetlhknNALKVARELQAQIAELQEDFESEKAsrnkAEKQKRDLSEELEALKTELEdtldttaaqqELRTKREQ 1184
Cdd:COG4717 128 L------------PLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELA----------ELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1185 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE------------------- 1245
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallal 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1246 --------------------------------------LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVE 1287
Cdd:COG4717 262 lglggsllsliltiagvlflvlgllallflllarekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1288 LAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEE----------- 1354
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQleellgeleel 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1355 -----KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDD--DLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDK 1427
Cdd:COG4717 422 lealdEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
490
....*....|.
gi 1039738675 1428 LEKTKNRLQQE 1438
Cdd:COG4717 502 LEEAREEYREE 512
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1001-1243 |
1.53e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.93 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1001 EDQNSKFIKEKKLMEdRIAECSSQLAEEEEKAKNLAKIRNKQEVmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKVSV--KSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1081 IAELQAQVDELKVqLTKKEEELQgaLARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-------AEKQKRD 1153
Cdd:PRK05771 116 IKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1154 LSEELEALKTELEDTLDTTAAQQELRTKrEQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSEQLEQAkRFKANLE 1233
Cdd:PRK05771 193 VEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIE-LERAEAL 266
|
250
....*....|
gi 1039738675 1234 KNkqGLETDN 1243
Cdd:PRK05771 267 SK--FLKTDK 274
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1322-1807 |
1.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1322 GLESQLQDTQELLQEE--TRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKK---KVD 1391
Cdd:PRK04863 227 GVRKAFQDMEAALRENrmTLEAIRVTQSDRDLfkhliTESTNYVAADYMRHANERRVHLEEALELRRELYTSRRqlaAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1392 DDLGTI----ESLEEAKKKLLKDVEALSQRL---EEKVLAYDKLEktknRLQQELDDLTVDLDHQRQIVSNLekkqkkfd 1464
Cdd:PRK04863 307 YRLVEMarelAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIE----RYQADLEELEERLEEQNEVVEEA-------- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1465 qllaeekgisaryAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKsk 1544
Cdd:PRK04863 375 -------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN-- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1545 raLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQTRDEQNEEKKRLLLKQV-RELeaeLEDERKQRA 1623
Cdd:PRK04863 440 --AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIAGEVSRSEAWDVaREL---LRRLREQRH 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1624 LAvASKKKMEIDLKDLE---AQIEAANKARDEVIKQLRKLQAQMKDYQRELEEarasrdeifaqskesekklksLEAEIL 1700
Cdd:PRK04863 511 LA-EQLQQLRMRLSELEqrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---------------------LEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1701 QLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLND---RFRKTTLQVD 1777
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQlleRERELTVERD 648
|
490 500 510
....*....|....*....|....*....|
gi 1039738675 1778 tlntelaaeRSAAQKsdnarQQLERQNKEL 1807
Cdd:PRK04863 649 ---------ELAARK-----QALDEEIERL 664
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1056-1350 |
1.78e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1056 EEKTRQELEKAKrklDGETTDLQDQIAELQAQVDELkvqltkkeEELQGALARGDDETLHKNNALKVARELQAQIAElqe 1135
Cdd:PRK10929 25 EKQITQELEQAK---AAKTPAQAEIVEALQSALNWL--------EERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1136 dfESEKASRNKAEKQKRDLSEELEALKTELEDtlDTTAAQQElrtkreqevaelkkaledetknheaqiQDMRQRHATAL 1215
Cdd:PRK10929 91 --ERDEPRSVPPNMSTDALEQEILQVSSQLLE--KSRQAQQE---------------------------QDRAREISDSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1216 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkAESEHKRkkldAQVQELH-AKVS-----EGDRLRVELA 1289
Cdd:PRK10929 140 SQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ--AESAALK----ALVDELElAQLSannrqELARLRSELA 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 1290 EK-ANKLQNELDNVSTLL--------EEAEKKGIKFAKDAAGLE----SQLQDTQELLQE--ETRQKLNL-SSRIRQ 1350
Cdd:PRK10929 214 KKrSQQLDAYLQALRNQLnsqrqreaERALESTELLAEQSGDLPksivAQFKINRELSQAlnQQAQRMDLiASQQRQ 290
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1635-1929 |
1.96e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1635 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1714
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1715 HAEQERDELADEIANsasgKSALLdekRRLEARIAQLEEELEeeqsNMELLNDRFRKTTLQVDTLNTELAAER-SAAQKS 1793
Cdd:pfam19220 101 EAEAAKEELRIELRD----KTAQA---EALERQLAAETEQNR----ALEEENKALREEAQAAEKALQRAEGELaTARERL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1794 DNARQQLERQNK----------ELKAKLQELEG----------AVKSKFKATISALEAKIGQLEEQLEQEAKERA----- 1848
Cdd:pfam19220 170 ALLEQENRRLQAlseeqaaelaELTRRLAELETqldatrarlrALEGQLAAEQAERERAEAQLEEAVEAHRAERAslrmk 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1849 --AANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEG 1926
Cdd:pfam19220 250 leALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEM 329
|
...
gi 1039738675 1927 LSR 1929
Cdd:pfam19220 330 LTK 332
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
852-1352 |
2.06e-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: 49.73 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 852 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQA-----ETELFAEAEEMRARLAAK 926
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE----LDDRNMEVQRLEAllkamKSECQGQMERQMAAIQGK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 927 KQELEEI---LHDLESrvEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEakIKKMEEEVLLLEDQ 1003
Cdd:pfam15921 457 NESLEKVsslTAQLES--TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE--ITKLRSRVDLKLQE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1004 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGEttdLQDQIAE 1083
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKE---INDRRLE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1084 LQaqvdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKt 1163
Cdd:pfam15921 606 LQ----EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK- 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1164 eledtldttaaqQELRTKREqevaelkkalEDETKNHEAQIQdmrqrhataLEELSEQLEQAKrfkaNLEKNKQGleTDN 1243
Cdd:pfam15921 681 ------------RNFRNKSE----------EMETTTNKLKMQ---------LKSAQSELEQTR----NTLKSMEG--SDG 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1244 KELACEVKVLQQVKAesehKRKKLDA---QVQELHAKVSEGDRLRVELAEKANKLQNELDNVST----------LLEEAE 1310
Cdd:pfam15921 724 HAMKVAMGMQKQITA----KRGQIDAlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmageleVLRSQE 799
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1311 KK------GIKFAKDAAGLE-SQLQD-TQELLQEETRQKLNLSSRIRQLE 1352
Cdd:pfam15921 800 RRlkekvaNMEVALDKASLQfAECQDiIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1194-1416 |
2.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1194 EDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesehkrKKLDAQVQE 1273
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI------------------DKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1274 LHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGI-KFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLE 1352
Cdd:COG3883 77 AEAEI---EERREELGERARALYRSGGSVSYLDVLLGSESFsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1353 EEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1416
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1550-1895 |
2.27e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1550 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL--AVA 1627
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1628 SKKKMEIDLKDLEAQIEAANKARD-----EVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1702
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1703 QEELASSERARRHAEQErdeladeiansaSGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1782
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVA------------TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1783 LAAERSAAQKSDNARQQLERQNKELKaklqelegavkskfkatisaleakigQLEEQLEQEAKERAAANKLVRRTEKKLK 1862
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAE--------------------------LCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350
....*....|....*....|....*....|...
gi 1039738675 1863 EIFMQVEDERRHADQYKEQMEKANARMKQLKRQ 1895
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1380-1598 |
3.62e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1380 QSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK 1459
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1460 QKK-------FDQLLAeekgiSARYAEERDRAEAeareketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDD 1532
Cdd:COG3883 95 LYRsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1533 VGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNE 1598
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1057-1227 |
4.19e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1057 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ--LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1134
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1135 EDFES--EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1212
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170
....*....|....*
gi 1039738675 1213 TALEELSEQLEQAKR 1227
Cdd:COG3206 327 AREASLQAQLAQLEA 341
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1609-1723 |
4.50e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1609 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEifaqSKES 1688
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR----EIRK 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1039738675 1689 EKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1723
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
975-1190 |
5.41e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 975 ARQKLQlekvTAEAKIKKMEEE--VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEEr 1052
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1053 LKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKKEEELQGALargddetlhkNNALKVARELQAQ 1129
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASL----------EAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1130 IAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEVAELK 1190
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1027-1298 |
5.53e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1027 EEEEKAKNLAKIRNKQEvmisdlEERLKKEEKTRQEleKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1106
Cdd:PRK05035 442 EQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1107 ARGDDETLHKNNALKVARELQAQIAELQEDfESEKAS------RNKAEKQkrdlseELEALKTELEDTLDTTAAQQELRT 1180
Cdd:PRK05035 514 PDNSAVIAAREARKAQARARQAEKQAAAAA-DPKKAAvaaaiaRAKAKKA------AQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1181 KREQEVAELKKALEDETKNHEAQIQDMRQRHATAleelseqLEQAKRFKANLE-KNKQGLETDNKELAcevkvlqqVKAE 1259
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAA-------IARAKAKKAEQQaNAEPEEPVDPRKAA--------VAAA 651
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039738675 1260 SEHKRKKLDAQVQELHAKVSEGDRLRVELAE-----KANKLQNE 1298
Cdd:PRK05035 652 IARAKARKAAQQQANAEPEEAEDPKKAAVAAaiaraKAKKAAQQ 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1319-1499 |
5.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1319 DAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVD------- 1391
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1392 ----------------------DDLGTIESLEEAKKKLLKDVEALSQRLEEKvlaydklektKNRLQQELDDLTVDLDHQ 1449
Cdd:COG3883 97 rsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAK----------KAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1450 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA 1499
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1124-1273 |
5.66e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1124 RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEvaelkkALEDETKNHEAQ 1203
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRNNKEYE------ALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1204 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE 1273
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1323-1692 |
5.81e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1323 LESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1402
Cdd:pfam07888 36 LEECLQERAELLQAQEAAN-------RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1403 AKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL-----------EKKQKKFDQLLAEEK 1471
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaerKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1472 GISARYAEERDRAEaearEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1551
Cdd:pfam07888 189 SLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1552 EEM-RTQLEELEDELQATE------DAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRal 1624
Cdd:pfam07888 265 AQRdRTQAELHQARLQAAQltlqlaDASLALREG-RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER-- 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1625 avaskKKMEIDLkdleAQIEAANKA-RDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1692
Cdd:pfam07888 342 -----EKLEVEL----GREKDCNRVqLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1283-1488 |
6.30e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1283 RLRVELAEKANK-LQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLNLSSRIRQLEEEknslqeq 1361
Cdd:COG3206 167 ELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAE------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1362 qeeeeeaRKNLEKQVLALQSQLADTKKKVDDDLG--TIESLEEAKKKLLKDVEALSQRLEEK----VLAYDKLEKTKNRL 1435
Cdd:COG3206 235 -------LAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQL 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1436 QQELDDLTVDLDHQRQI----VSNLEKKQKKFDQLLAEEKGISARYAE-ERDRAEAEA 1488
Cdd:COG3206 308 QQEAQRILASLEAELEAlqarEASLQAQLAQLEARLAELPELEAELRRlEREVEVARE 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1138-1353 |
6.47e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1138 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAElkkALEDETKNHEAQIQDMRQRhataLEE 1217
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEFRQKNGLV---DLSEEAKLLLQQLSELESQ----LAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1218 LSEQLEQAKRFKANLEKNKQGLETDNKELAcEVKVLQQVKAEsehkRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQN 1297
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELL-QSPVIQQLRAQ----LAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1298 ELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1353
Cdd:COG3206 306 QLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1011-1351 |
7.36e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1011 KKLMEDRIAECSSQLAEEEE--------KAKN--------LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1074
Cdd:pfam06160 55 DDIVTKSLPDIEELLFEAEElndkyrfkKAKKaldeieelLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1075 TDLQDQ-------IAELQAQVDELKVQLTKKEEELQGalarGDDETlhknnALKVARELQAQIAELQEDFESEKASRNKA 1147
Cdd:pfam06160 135 KTLLANrfsygpaIDELEKQLAEIEEEFSQFEELTES----GDYLE-----AREVLEKLEEETDALEELMEDIPPLYEEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1148 EKQKRDLSEELEALKTELED---TLDTTAAQQELRTKREQeVAELKKALED-ETKNHEAQIQDMRQRhataLEELSEQLE 1223
Cdd:pfam06160 206 KTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEIEER----IDQLYDLLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1224 QAKRFKANLEKNKQGLETD-------NKELACEVKVLQQ---VKAESEHKRKKLDAQVQELHAKVsegDRLRVELAEKA- 1292
Cdd:pfam06160 281 KEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKRY---DEIVERLEEKEv 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1293 --NKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1351
Cdd:pfam06160 358 aySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1060-1224 |
7.96e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1060 RQEL---EKAKRKLDGETTDLQDQIA-------ELQAQVDELKVQLTKKEEE---LQGALARGDDEtlhknnalkvAREL 1126
Cdd:PRK09039 45 SREIsgkDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGA----------GAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1127 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELedtldttaaqqelrtkreQEVAELKKALEDETKNHEAQIQD 1206
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL------------------AALEAALDASEKRDRESQAKIAD 176
|
170
....*....|....*...
gi 1039738675 1207 MRQRHATALEELSEQLEQ 1224
Cdd:PRK09039 177 LGRRLNVALAQRVQELNR 194
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1635-1866 |
8.35e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1635 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskeSEKKLKSLE-AEILQLQEELASSERAR 1713
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL------EAAALQPGEeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1714 RHAEQERDELADEIANSASgksaLLDE-KRRLEaRIAQleeeleeEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQk 1792
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLE- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1793 SDNAR-QQLE-RQN--------------------KELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKE---- 1846
Cdd:COG0497 293 FDPERlEEVEeRLAllrrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaa 367
|
250 260
....*....|....*....|.
gi 1039738675 1847 -RAAANKLVRRTEKKLKEIFM 1866
Cdd:COG0497 368 rKKAAKKLEKAVTAELADLGM 388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1258-1435 |
9.43e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1258 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEE 1337
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1338 TRQKLnlssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQR 1417
Cdd:COG1579 99 ESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAK 171
|
170
....*....|....*....
gi 1039738675 1418 LEEKVLA-YDKLEKTKNRL 1435
Cdd:COG1579 172 IPPELLAlYERIRKRKNGL 190
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
859-1207 |
9.45e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 859 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleEKNILAEQlqaetelfaeaeemRARLAAKkQELEEILHDLE 938
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLN--------------QARLQAL-EDLEKILTEKE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 939 SrveeeeernqiLQNEKKKMQAHIQDLEEQLdeeegarqklqleKVTAEAKIKkmeeeVLLLEDQNSKFIKEKKLMEDRI 1018
Cdd:PLN02939 167 A-----------LQGKINILEMRLSETDARI-------------KLAAQEKIH-----VEILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1019 AECSSQLAEEEE--KAKNLAkIRNKQEVM------ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIaelqAQVDE 1090
Cdd:PLN02939 218 GLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDV----SKLSP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1091 LKVQ-LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTELEDTL 1169
Cdd:PLN02939 293 LQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASD 371
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039738675 1170 DTTAAQQELRTKREQEVAELKKALEDETKNH--EAQIQDM 1207
Cdd:PLN02939 372 HEIHSYIQLYQESIKEFQDTLSKLKEESKKRslEHPADDM 411
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1539-1940 |
1.01e-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: 47.66 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDE 1618
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--------LQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1619 RKQraLAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL--- 1695
Cdd:TIGR00618 273 RAQ--EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtl 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1696 ------------EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE-----------KRRLEARIAQLE 1752
Cdd:TIGR00618 351 hsqeihirdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQReqatidtrtsaFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1753 EELEEEQSNMELLnDRFRKTTLQVDTLntELAAERSAAQKSDNARQQLerQNKELKAKLQELEGAVKSKFKATISALEAK 1832
Cdd:TIGR00618 431 KQQELQQRYAELC-AAAITCTAQCEKL--EKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1833 IGQLEEQLEQEAKERAAANKLVRRT----------EKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeee 1902
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC------- 578
|
410 420 430
....*....|....*....|....*....|....*...
gi 1039738675 1903 ATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1253-1380 |
1.07e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1253 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAglESQLQDTQE 1332
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1039738675 1333 LLQEETRqklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1380
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
852-1255 |
1.13e-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: 46.81 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 852 KPLLQVTRQEEELQAKD--EELLKVKEKQTKVEGELEEMERKhqqlleekniLAEQLQAETELFAEAEEMRARLAAKKQE 929
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQE----------RAELLQAQEAANRQREKEKERYKRDREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 930 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 1009
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1010 EKKLMEDRIAECSSQLAEEEEKAKNLakirnkqEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1089
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1090 ELKvqltKKEEELQGALA--RGDDETLH--KNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALK--- 1162
Cdd:pfam07888 224 TAH----RKEAENEALLEelRSLQERLNasERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1163 ----TELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL---EKN 1235
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKE 379
|
410 420
....*....|....*....|
gi 1039738675 1236 KQGLETDNKELACEVKVLQQ 1255
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQLEQ 399
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1091-1296 |
1.14e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1091 LKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL---EALKTELED 1167
Cdd:PRK09039 44 LSREISGKDSALD---------------------RLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1168 TLDTTAAQqelRTKREQEVAELKKALEDEtknheaqiQDMRQRHATALEELSEQLEQAKRfkanleknkqgletdnkELA 1247
Cdd:PRK09039 103 LLAELAGA---GAAAEGRAGELAQELDSE--------KQVSARALAQVELLNQQIAALRR-----------------QLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039738675 1248 cevkVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQ 1296
Cdd:PRK09039 155 ----ALEAALDASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
980-1473 |
1.28e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 980 QLEKVTAEA-------KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSS-QLAEEEEKAKNLAKIRNKQEVMISDLEE 1051
Cdd:TIGR01612 1154 DLEDVADKAisnddpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKdKTSLEEVKGINLSYGKNLGKLFLEKIDE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1052 RLKKEEKTRQELEKAKRKLDgettDLQDQIAELQaqvDELKVQLTKKEEELQGALARGDDETLH---KNNALKVArELQA 1128
Cdd:TIGR01612 1234 EKKKSEHMIKAMEAYIEDLD----EIKEKSPEIE---NEMGIEMDIKAEMETFNISHDDDKDHHiisKKHDENIS-DIRE 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1129 QIAELQEDFeSEKASRN-----------KAEKQKRDLSEELEALkTELEDTLDTTAAQQELRTKRE--QEVAELKKALED 1195
Cdd:TIGR01612 1306 KSLKIIEDF-SEESDINdikkelqknllDAQKHNSDINLYLNEI-ANIYNILKLNKIKKIIDEVKEytKEIEENNKNIKD 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1196 ETKNHEAQIQDMRQRhaTALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKL-------D 1268
Cdd:TIGR01612 1384 ELDKSEKLIKKIKDD--INLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLllfknieM 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1269 AQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQE----ETRQKLNL 1344
Cdd:TIGR01612 1462 ADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKysalAIKNKFAK 1541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1345 SSR-----IRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK---------D 1410
Cdd:TIGR01612 1542 TKKdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKisdikkkinD 1621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1411 VEALSQRLEEKV--LAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGI 1473
Cdd:TIGR01612 1622 CLKETESIEKKIssFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKI 1686
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1069-1495 |
1.29e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1069 KLDGETTDLQDQIAELQAQVDelkvqlTKKEEELQGALARGDDETLHKNNALKVarelqaqiaelQEDFESEKASRNKAE 1148
Cdd:NF012221 1355 EIDEVGSDLGDSLTGSVTQVE------TPDLNAMQNALNIDESVLSTQAPNLIV-----------NGDFEQGAEGWNSTY 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1149 KQKRDLS--------EELEALKTELeDTLDTTAAQQELRTKREQEVAELK----KALEDETKNHEAQIQDMRQRHATALE 1216
Cdd:NF012221 1418 GVEASHSasvyglraEGHGARVSEL-DTYTNTSLYQDLSNLTAGEVIALSfdfaRRAGLSTNNGIEVLWNGEVVFASSGD 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1217 ELSEQLEQAK----------RFKANLEKNKQGLETDNKELACEVKvlQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRV 1286
Cdd:NF012221 1497 ASAWQQKTLKltakagsnrlEFKGTGHNDGLGYILDNVVATSESS--QQADAVSKHAKQDDAAQNALADKERAEADRQRL 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1287 ElAEKanklQNELDNVSTLLEEAEkkgikfAKDAAGLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEKNSLQEQQEEE 1365
Cdd:NF012221 1575 E-QEK----QQQLAAISGSQSQLE------STDQNALETNGQAQRDAILEESRAvTKELTTLAQGLDALDSQATYAGESG 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1366 EEARKNLEKQVLA-LQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTV 1444
Cdd:NF012221 1644 DQWRNPFAGGLLDrVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG------EQNQANAEQDIDDAKA 1717
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1445 DLDHQRQivsnlEKKQKKFDQLLAEEKGiSARYAEERDRAEAEAREKETKA 1495
Cdd:NF012221 1718 DAEKRKD-----DALAKQNEAQQAESDA-NAAANDAQSRGEQDASAAENKA 1762
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
855-1069 |
1.35e-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: 47.04 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 855 LQVTRQEEelqaKDEELLKVKEKQTKVEGE-LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 933
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISrMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 934 LHDLESrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIkEKKL 1013
Cdd:pfam17380 426 RAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKEL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1014 MEDRIAecssqLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1069
Cdd:pfam17380 502 EERKQA-----MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1596-1916 |
1.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1596 QNEEKKRLLLKQVRELEAELEDERKQRALA----VASKKKMEI---DLKDLEAQIEAA----NKARDEVI--KQLRKLQA 1662
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEqyrlVEMARELAElneAESDLEQDYQAAsdhlNLVQTALRqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1663 QMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA----------RRHAEQERDE---LADEIAN 1729
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERakqLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1730 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRkttlQVDTLNTELAAERSAAQKSDNARQqLERQNKELKA 1809
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSRSEAWDVARE-LLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1810 KLQELEgavkskfkatisALEAKIGQLEEQLEQEAkeraAANKLVRRTEKKLKeifMQVEDErrhaDQYKEQMEKANARM 1889
Cdd:PRK04863 511 LAEQLQ------------QLRMRLSELEQRLRQQQ----RAERLLAEFCKRLG---KNLDDE----DELEQLQEELEARL 567
|
330 340
....*....|....*....|....*..
gi 1039738675 1890 KQLKRQLEEAEEEATRANASRRKLQRE 1916
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQLEQLQAR 594
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1517-1852 |
1.62e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1517 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMR---TQLEELEDELQATEDAKLRLEVNMQAMKAQ------FE 1587
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDYNNLKSALNELSSLedmknrYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1588 RDLQTRDE--QNEEKKRLLLKQVRELEAELEDE----RKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQ 1661
Cdd:PRK01156 256 SEIKTAESdlSMELEKNNYYKELEERHMKIINDpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1662 AQMKDY---QRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALL 1738
Cdd:PRK01156 336 KDYNDYikkKSRYDDLNNQILEL----EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1739 DEKRR-----------LEARIAQLEEELEEEQSNMELLNDRFR-----------KTTLQVDTLNTELAAERSAAQKSDNA 1796
Cdd:PRK01156 412 NEINVklqdisskvssLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIE 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1797 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1852
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1543-1698 |
1.67e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1543 SKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQV---RELEAEL---- 1615
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERsarREAEAELerlq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1616 -------EDERKQRALAVASKKKMEIDLKDLEAQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1685
Cdd:pfam09787 121 eelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
|
170
....*....|...
gi 1039738675 1686 KESEKKLKSLEAE 1698
Cdd:pfam09787 201 ERMEQQIKELQGE 213
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1267-1625 |
1.73e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1267 LDAQVQEL---HAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLN 1343
Cdd:pfam19220 36 IEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1344 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVL 1423
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1424 AYDKLEKTKNRLQQELDDltvdldhQRQIVSNLEKKqkkfdqlLAEEKgisaryaEERDRAEAEAREK----ETKALSLA 1499
Cdd:pfam19220 189 ELAELTRRLAELETQLDA-------TRARLRALEGQ-------LAAEQ-------AERERAEAQLEEAveahRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1500 RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE--V 1577
Cdd:pfam19220 248 MKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerA 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1578 NM-----QAMKAQFER------DLQTRDEQNE---EKKRLLLKQ-VRELEAELEDERKQRALA 1625
Cdd:pfam19220 328 EMltkalAAKDAALERaeeriaSLSDRIAELTkrfEVERAALEQaNRRLKEELQRERAERALA 390
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1642-1922 |
1.86e-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: 46.66 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1642 QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKSLEAEILQLQEElassERARRHAE 1717
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1718 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnDRFRKTTLQVDTLNtELAAERSAAQKSDNAR 1797
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1798 QQLERQNKELKAKLQELEgavKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRT-EKKLKEIFMQ-VEDERRHA 1875
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039738675 1876 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1922
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
902-1222 |
1.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 902 LAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE-------SRVEEEEERNQILQNEKKKMQAhiqdleeqlDEEEG 974
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVASAEREIAELEAELERL---------DASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 975 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkQEVMISDLEERLK 1054
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA---------RLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1055 KEEKTRQELEKAKRkldgettdLQDQIAELQAQVDELKVQLTKKeeeLQGALARGDDETLHKNNALKVARELQAQIAELQ 1134
Cdd:COG4913 757 AALGDAVERELREN--------LEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1135 ED----FESE-KASRNKAEKQKR-DLSEELEALKTELEDTLDT-------------TAAQQELRTKREQEVAELKKALED 1195
Cdd:COG4913 826 EDglpeYEERfKELLNENSIEFVaDLLSKLRRAIREIKERIDPlndslkripfgpgRYLRLEARPRPDPEVREFRQELRA 905
|
330 340
....*....|....*....|....*..
gi 1039738675 1196 ETKNHEAQIQDMRQRHATALEELSEQL 1222
Cdd:COG4913 906 VTSGASLFDEELSEARFAALKRLIERL 932
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1030-1165 |
1.95e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1030 EKAK-NLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLtkkEEELQGALar 1108
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAI-- 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 1109 gddetlhkNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTEL 1165
Cdd:PRK00409 580 --------KEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKKEKKK 627
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1028-1497 |
2.08e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1028 EEEKAKNLAKIRNKQEVMISDL----EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQ 1103
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1104 GALARgdDETLHKNNALKVARELQAQIAE------------LQEDFESEKAS------RNKAEKQKRDLSEELEALKTEL 1165
Cdd:pfam07111 215 AQVTL--VESLRKYVGEQVPPEVHSQTWElerqelldtmqhLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1166 EDTLD---TTAAQQELRTKREQeVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD 1242
Cdd:pfam07111 293 SDSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1243 N---KELACEVKVLQQVKAESEHKRKKLDAQVQ-----------ELHAKVSEGDRLRVELAEKANKLQNELDNVSTL--- 1305
Cdd:pfam07111 372 RmsaKGLQMELSRAQEARRRQQQQTASAEEQLKfvvnamsstqiWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIkgl 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1306 ------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ---KLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEK 1374
Cdd:pfam07111 452 markvaLAQLRQESCPPPPPAPPVDADLSLELEQLREERNRldaELQLSAHLIQQEvgRAREQGEAERQQLSEVAQQLEQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1375 QVLALQSQLADTKKKVDDDL-GTIESLEEA---KKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTVDLDHQR 1450
Cdd:pfam07111 532 ELQRAQESLASVGQQLEVARqGQQESTEEAaslRQELTQQQEIYGQALQEKV------AEVETRLREQLSDTKRRLNEAR 605
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1039738675 1451 QIVSNLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKALS 1497
Cdd:pfam07111 606 REQAKAVVSLRQIQHRATQEK----ERNQELRRLQDEARKEEGQRLA 648
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1516-1648 |
2.27e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 46.21 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1516 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDE 1595
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYE-DLETRLT 761
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1596 QNEEKKRLLLKQVRELEAELEDERKqralavaSKKKMEIDLKDLEAQIEAANK 1648
Cdd:pfam05911 762 ELEAELNELRQKFEALEVELEEEKN-------CHEELEAKCLELQEQLERNEK 807
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1579-1973 |
2.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1579 MQAMKAQFERDLQTRDEQ----NEEKKRLLLKQVRELEAELEDERKQralaVASKKKMEIDLKDLEAQIEAANKARDEVI 1654
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1655 KQLRKLQaQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGK 1734
Cdd:COG4717 116 EELEKLE-KLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1735 SA----LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE-----------LAAERSAAQKSDNARQQ 1799
Cdd:COG4717 191 EEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1800 LERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1879
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1880 EQMEKANARMKQLKRQLEEAEEEA--TRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR-GGPISFSSSRSGRRQL 1956
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEElLGELEELLEALDEEEL 430
|
410
....*....|....*..
gi 1039738675 1957 HIEGASLELSDDDTESK 1973
Cdd:COG4717 431 EEELEELEEELEELEEE 447
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
911-1485 |
2.29e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 911 ELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEErnqiLQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKI 990
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 991 KKMEEEVLLLED---QNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkqeVMISDLEERLKKEEKTRQeleKAK 1067
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKN-----------NYYKELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1068 RKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGA--LARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1145
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLsvLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1146 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL--- 1222
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNMeml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1223 ---------------EQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDA-QVQELHAKVSEGDRLRV 1286
Cdd:PRK01156 450 ngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1287 ELAEKANKLqNELDNVSTLLEEA--EKKGIKFakdaaglesqlqdtqELLQEETRQKLNLSSRIRQLEEEknSLQEQQEE 1364
Cdd:PRK01156 530 DLEDIKIKI-NELKDKHDKYEEIknRYKSLKL---------------EDLDSKRTSWLNALAVISLIDIE--TNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1365 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIE---SLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDD 1441
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEneaNNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE 671
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039738675 1442 LTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1485
Cdd:PRK01156 672 ITSRIN---DIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1370-1894 |
2.30e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1370 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQ 1449
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1450 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSS 1529
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQ-------LAEAQKEAELLRKQLSKTQEELEAQVTLVESL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1530 KDDVGKNV--------------------HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD 1589
Cdd:pfam07111 224 RKYVGEQVppevhsqtwelerqelldtmQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1590 LQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVAS--------------------KKKMEIDL-----KDLEAQIE 1644
Cdd:pfam07111 304 CRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAElqeqvtsqsqeqailqralqDKAAEVEVermsaKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1645 AANKAR-------DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL----------KSLEAEILQLQEELA 1707
Cdd:pfam07111 384 RAQEARrrqqqqtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQ 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1708 SSERARRHAEQERDELADEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNME---------LLNDRFRKTTLQVDT 1778
Cdd:pfam07111 464 ESCPPPPPAPPVDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAErqqlsevaqQLEQELQRAQESLAS 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1779 LNTELAAERSAAQKSD----NARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLEEQLEQEAKERAAANKLV 1854
Cdd:pfam07111 543 VGQQLEVARQGQQESTeeaaSLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARREQAKAVVSLRQIQ 619
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1039738675 1855 RRT--EKKLKEIFMQVEDERRhadqyKEQMEKANARMKQLKR 1894
Cdd:pfam07111 620 HRAtqEKERNQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1655-1940 |
2.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1655 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAE---QERDELADEIANSA 1731
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1732 SGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqvdtlntelAAERSAAQKSDNARQQLERQNKELKAKL 1811
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1812 QELEgavkskfkATISALEAKIGQLEEQLeqeaKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANaRMKQ 1891
Cdd:PRK03918 310 REIE--------KRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELER 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1039738675 1892 LKRQLeeaeeeatrANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:PRK03918 377 LKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1782-1894 |
2.62e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1782 ELAAERSAAQKSDNARQ--QLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEK 1859
Cdd:COG2433 398 EREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|....*
gi 1039738675 1860 KLKEIfmqvEDERRHADQYKEQMEkanaRMKQLKR 1894
Cdd:COG2433 477 LEREL----EEERERIEELKRKLE----RLKELWK 503
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1276 |
2.83e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 854 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEME---RKHQQLLEEKNI---LAEQLQAET----ELFAEAEEMRARL 923
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKndiEEQETLLGTIMPeeeSAKVCLTDVtimeRFQMELKDVERKI 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 924 AAKKQELEEIlhDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQL---EKVTAEAKIKKMEEEVLLL 1000
Cdd:TIGR00606 809 AQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQF 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1001 EDQNSKFIKEkklMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:TIGR00606 887 EEQLVELSTE---VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1081 IAELQAQvdelkvQLTKKEEELQGALARGDDETLHKNnalkvarelqaqiaELQEDFESEKASRNKAEKQKRDLSEELEA 1160
Cdd:TIGR00606 964 IQDGKDD------YLKQKETELNTVNAQLEECEKHQE--------------KINEDMRLMRQDIDTQKIQERWLQDNLTL 1023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1161 LKTELEDTLDTTAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL-EKNKQGL 1239
Cdd:TIGR00606 1024 RKRENELKEVEEELKQHLKEMGQMQVLQMKQ----EHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELrEPQFRDA 1099
|
410 420 430
....*....|....*....|....*....|....*..
gi 1039738675 1240 ETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1276
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHS 1136
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
861-1145 |
2.90e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 861 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETElfaEAEEMRARLAAKKQELEEilhdlesr 940
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEE-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 941 veeeeeRNQILQNEKKKMQahiqdleeqldeeegaRQKLQLEKVtaeakikkmeeEVLLLEDQNSKFIKEKKLMeDRIAE 1020
Cdd:COG3883 84 ------RREELGERARALY----------------RSGGSVSYL-----------DVLLGSESFSDFLDRLSAL-SKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1021 CSSQLAEEEEKAKnlAKIRNKQevmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEE 1100
Cdd:COG3883 130 ADADLLEELKADK--AELEAKK----AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039738675 1101 ELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1145
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1636-1894 |
3.08e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1636 LKDLEAQIEAANKARDEVIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKSLEAEILQLQEELASSERarRH 1715
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1716 AEQERDeLADEIANS-----ASGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERS 1788
Cdd:PRK11637 120 AAQERL-LAAQLDAAfrqgeHTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1789 AAQKSDNARQQLERQNKELKAKLQELEGAVKSkfkaTISALEAKIGQLEEQLEQeakeraaanklVRRTEKKLKEIFMQV 1868
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQARNERKK----TLTGLESSLQKDQQQLSE-----------LRANESRLRDSIARA 252
|
250 260
....*....|....*....|....*..
gi 1039738675 1869 EDE-RRHADQYKEQMEKANARMKQLKR 1894
Cdd:PRK11637 253 EREaKARAEREAREAARVRDKQKQAKR 279
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1539-1659 |
3.34e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD---------------LQTRDEQNEEKKRL 1603
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnnkeyeaLQKEIESLKRRISD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1604 LLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRK 1659
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1650-1815 |
3.42e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1650 RDEVIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkSLEAEILQLQEELASSERARRHAEQERDELADEiAN 1729
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1730 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttlQVDTLNTELAAERSAAQKSDNARQQLERQ------ 1803
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 1039738675 1804 --NKELKAKLQELE 1815
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1081-1358 |
3.76e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.62 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1081 IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKnnalkVARELQAQIAE------LQEDFESEKASRNKAEKQK--- 1151
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK-----LKKEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1152 -RDLSEELEALKTELEDTLDTTAAQQELRTKRE--QEVAELKKALEDETKNHEAQiQDMRQRHATALE--ELSEQLEQAK 1226
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFKEVMDrpEIKEKMEALK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1227 RFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELD----- 1300
Cdd:PLN03229 585 AEVASSGASSGDeLDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINkkier 664
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1301 --NVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1358
Cdd:PLN03229 665 viRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
884-1482 |
4.03e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 884 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeilhdLESRVEEEEERNQILQNEKKKmqahiq 963
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIIIKEIKD------ 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 964 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED--------------------RIAECss 1023
Cdd:TIGR01612 1556 -----------AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflkisdikkKINDC-- 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1024 qLAEEEEKAKNLAKIR-NKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQVDELKVQLTKKEEEL 1102
Cdd:TIGR01612 1623 -LKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1103 QGALARGDDETLHKNNalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKR 1182
Cdd:TIGR01612 1698 EIGIIEKIKEIAIANK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGC 1772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1183 EQEVAElkkalEDETKNheaQIQDMRqrhATALEELSEQLEQAKRFKANLeknkqgletDNKELACEVKVLQQVKAESEH 1262
Cdd:TIGR01612 1773 LETVSK-----EPITYD---EIKNTR---INAQNEFLKIIEIEKKSKSYL---------DDIEAKEFDRIINHFKKKLDH 1832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1263 KRKKLDAQvqelHAKVSEG-DRL-----RVELAEKANKLQNELDNVSTLL------------EEAEKKGIKFAKDAAGLE 1324
Cdd:TIGR01612 1833 VNDKFTKE----YSKINEGfDDIsksieNVKNSTDENLLFDILNKTKDAYagiigkkyysykDEAEKIFINISKLANSIN 1908
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1325 SQLQDTQEL-------------LQEETRQKL-------NLSSRIRQLEEEKNSLQEQQEEEEEARKNlEKQVLAL---QS 1381
Cdd:TIGR01612 1909 IQIQNNSGIdlfdniniailssLDSEKEDTLkfipspeKEPEIYTKIRDSYDTLLDIFKKSQDLHKK-EQDTLNIifeNQ 1987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1382 QLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE---------------KVLAYDKLEKTKNRLQQELDDLTVDL 1446
Cdd:TIGR01612 1988 QLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKFGIDF 2067
|
650 660 670
....*....|....*....|....*....|....*...
gi 1039738675 1447 DHQ--RQIVSNLEKKQKKFDQLLAEEKGISARYAEERD 1482
Cdd:TIGR01612 2068 DVKamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1425-1867 |
4.15e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1425 YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEAREKETKALsLARALEE 1504
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1505 ALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1584
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1585 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1664
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1665 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1744
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1745 EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1824
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1039738675 1825 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQ 1867
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1539-1707 |
4.63e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQ-----NEEKKRLLLKQVRELEA 1613
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-KWEEKARLalekgREDLAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1614 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQ---------------------MKDYQRELE 1672
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvnealsgidsddatsalerMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1039738675 1673 EARASRDEIfAQSKESEKKLKSLEAEIlQLQEELA 1707
Cdd:COG1842 179 ARAEAAAEL-AAGDSLDDELAELEADS-EVEDELA 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
853-1226 |
4.66e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 853 PLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNI-LAEQLQAETElfaeaEEMRArLAAKKQELE 931
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPE-----AELRQ-LNRRRVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 932 EILHDLESrvEEEEERNQILQnekkkmqahiqdleeqldeeegARQKLQLekvtaeakIKKMEEEVLLLEDQNskfikek 1011
Cdd:PRK04863 851 RALADHES--QEQQQRSQLEQ----------------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1012 klMEDRIAECSSQLAEEEEKA-------KNLAKIRNKQEVMISDLE--ERLKKE-EKTRQELEKAKRKLDGETTDLQ--- 1078
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDPEqfEQLKQDyQQAQQTQRDAKQQAFALTEVVQrra 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1079 ----DQIAELQAQVDELKVQLTKKEEELQGALARGDDEtlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDL 1154
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ----------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1155 SEELEALKTELEDTLDTTAA------QQELRTKREQEvAELKKALEDETKNHEAQiqdmrQRHATALEE----LSEQLEQ 1224
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARarrdelHARLSANRSRR-NQLEKQLTFCEAEMDNL-----TKKLRKLERdyheMREQVVN 1113
|
..
gi 1039738675 1225 AK 1226
Cdd:PRK04863 1114 AK 1115
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1544-1698 |
4.97e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1544 KRALEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQTRDEQNEEKKRLLLKQVRELEAELED 1617
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1618 ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKs 1694
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 1039738675 1695 LEAE 1698
Cdd:PRK12704 184 EEAD 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1593-1863 |
5.01e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1593 RDEQNEEKKRLLLKQVRELEAELEDERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1671
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLrKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1672 EEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1751
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1752 EEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEA 1831
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270
....*....|....*....|....*....|..
gi 1039738675 1832 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1863
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1539-1938 |
5.60e-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: 45.01 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDE 1618
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQ-IKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1619 RKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQSKESEKKLKSLEAE 1698
Cdd:TIGR04523 116 KEQ-------KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-------ELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1699 ILQLQEELASSERARRHAEQerdeladeianSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDT 1778
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLEL-----------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1779 LNTELaaersaaqksDNARQQLERQNKELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKERAAAnklvrrTE 1858
Cdd:TIGR04523 251 TQTQL----------NQLKDEQNKIKKQLSEKQKELEQN-----NKKIKELEKQLNQLKSEISDLNNQKEQD------WN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1859 KKLKEIFMQVEDERRhadQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:TIGR04523 310 KELKSELKNQEKKLE---EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
985-1312 |
5.81e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 985 TAEAKIKKMEEEVLLL---EDQNSKFIKE---------KKLMEDR------IAECSSQLAEEEE---KAKNLAKIRNKQE 1043
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEefsQFVELTESGDYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1044 --VMISDLEERLKKEEKTRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQ------------LTKKEEELQGALArg 1109
Cdd:PRK04778 196 arEILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeIQDLKEQIDENLA-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1110 DDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE---LRTKREQEV 1186
Cdd:PRK04778 271 LLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsytLNESELESV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1187 AELKKALEDETKNHEAQIQDMRQRHATA------LEELSEQLEQAKRFKANLEKNKQGLETDnkELACEVKVLQQVKAES 1260
Cdd:PRK04778 351 RQLEKQLESLEKQYDEITERIAEQEIAYselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKD--ELEAREKLERYRNKLH 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1261 EHKRK------------------KLDAQVQELHAKVSEGdRLRVElaekanKLQNELDNVSTLLEEAEKK 1312
Cdd:PRK04778 429 EIKRYleksnlpglpedylemffEVSDEIEALAEELEEK-PINME------AVNRLLEEATEDVETLEEE 491
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1537-1938 |
6.16e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1537 VHELEKSKrALEQQVEEMRTQLEELEDELQATEDAKLR----LEVN---MQAMKAQFERdLQTRDEQNEEKKRLLLKQVR 1609
Cdd:pfam05701 31 IQTVERRK-LVELELEKVQEEIPEYKKQSEAAEAAKAQvleeLESTkrlIEELKLNLER-AQTEEAQAKQDSELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1610 ELEAELEDErkqraLAVASKKKMEIDLKDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESE 1689
Cdd:pfam05701 109 EMEQGIADE-----ASVAAKAQLEVAKARHAAAVAELKSVKEE----LESLRKEYASLVSERDIAIKRAEEAVSASKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1690 KKLKSLEAEILQLQEELASSERARRHAEQERDELA-----DEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNMEL 1764
Cdd:pfam05701 180 KTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1765 LNDrfrkttlqvdtLNTELAAERSAAQKSDNARQQLERQ-NKELKAKL----QELEGAVKSKFKAT--ISALEAKIGQLE 1837
Cdd:pfam05701 259 LLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALasakKELEEVKANIEKAKdeVNCLRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1838 EQLEQEAKERAAanklVRRTEKKLKEIFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKL 1913
Cdd:pfam05701 328 SELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAA 403
|
410 420
....*....|....*....|....*
gi 1039738675 1914 QRELDDATEANEGLSREVSTLKNRL 1938
Cdd:pfam05701 404 REELRKAKEEAEQAKAAASTVESRL 428
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1539-1677 |
6.21e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ-NEEKKRLLLKQVRELEAELED 1617
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1618 ERKqrALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAS 1677
Cdd:cd22656 191 LNE--EYAAKLKAKID-ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1267-1935 |
6.46e-04 |
|
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: 44.81 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1267 LDAQVQELHakvSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnLSS 1346
Cdd:pfam10174 1 LQAQLRDLQ---RENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQH---LQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1347 RIRQLEEEKnslqeqqeeeeEARKNLEKqvlALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDvealsqrleekvlaYD 1426
Cdd:pfam10174 75 TIQALQDEL-----------RAQRDLNQ---LLQQDFTTSPVDGEDKFSTPELTEENFRRLQSE--------------HE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1427 KLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaEEKGISARYAEERDR-----AEAEAREKETKALSLARA 1501
Cdd:pfam10174 127 RQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML-QSKGLPKKSGEEDWErtrriAEAEMQLGHLEVLLDQKE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1502 LEEALEAKEEFER-QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEE--------------------------- 1553
Cdd:pfam10174 206 KENIHLREELHRRnQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhtedreeeikqmevykshsk 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1554 -MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRD------EQNEEKKRLLLKQVRELEAELEdeRKQRALAV 1626
Cdd:pfam10174 286 fMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkeslTAKEQRAAILQTEVDALRLRLE--EKESFLNK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1627 ASKKKMEI---------DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEa 1697
Cdd:pfam10174 364 KTKQLQDLteekstlagEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1698 EILQLQEELAssERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1777
Cdd:pfam10174 443 EALSEKERII--ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1778 TLNTELAAERSAAQKsdnarqqLERQNKelkaKLQELEGAVKSKfkatiSALEAKIGQLEEQLEQEAKERAAANKLVRRt 1857
Cdd:pfam10174 521 SLEIAVEQKKEECSK-------LENQLK----KAHNAEEAVRTN-----PEINDRIRLLEQEVARYKEESGKAQAEVER- 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1858 ekkLKEIFMQVEDERRHADQYKEQMEKANARmkQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLK 1935
Cdd:pfam10174 584 ---LLGILREVENEKNDKDKKIAELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1005-1163 |
6.90e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1005 SKFIK-EKKLMEDR---------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1074
Cdd:COG2433 350 NKFERvEKKVPPDVdrdevkarvIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1075 TDLQDQIAELQAQVDELKVQLTK-KEEELQGALARgddetlhknnalkvaRElqaqIAELQEDFESEKASRNKAEKQKRD 1153
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEaRSEERREIRKD---------------RE----ISRLDREIERLERELEEERERIEE 490
|
170
....*....|
gi 1039738675 1154 LSEELEALKT 1163
Cdd:COG2433 491 LKRKLERLKE 500
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1320-1921 |
7.17e-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: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1320 AAGLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQladtkKKVD---DDLGT 1396
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMA---RELEELSARESDLEQDYQAASDHLNLVQTALRQQ-----EKIEryqEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1397 IES-LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL---QQELDDLTVDLDHQRQIVSNLEKKQKkfdqlLAEEKG 1472
Cdd:COG3096 359 LTErLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyQQALDVQQTRAIQYQQAVQALEKARA-----LCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1473 ISARYAEERdRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD--DVGKNVHELEKSKRALEQ 1549
Cdd:COG3096 434 LTPENAEDY-LAAFRAKEQQaTEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1550 QVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQTRDEQNEEKKrlllkqvrELEAELEDERKQRALAVASK 1629
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLA--------ELEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1630 KKMEIDLKDLEAQI--------------EAANKARDEVIKQLRKLQAQMKDYQRELE---EARASRDEIFAQSKESEKKL 1692
Cdd:COG3096 581 SELRQQLEQLRARIkelaarapawlaaqDALERLREQSGEALADSQEVTAAMQQLLErerEATVERDELAARKQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1693 KSL-------EAEILQLQEELA---------------------------------------------------------- 1707
Cdd:COG3096 661 ERLsqpggaeDPRLLALAERLGgvllseiyddvtledapyfsalygparhaivvpdlsavkeqlagledcpedlyliegd 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1708 ---------------------SSERARR-----------------HAEQ---ERDELADEIANSASGKSALLDEKRRLEA 1746
Cdd:COG3096 741 pdsfddsvfdaeeledavvvkLSDRQWRysrfpevplfgraarekRLEElraERDELAEQYAKASFDVQKLQRLHQAFSQ 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1747 RIAQLEEELEEEQSNMELLNDRFRKTTLQvDTLNTELAAERSAAQKSDNARQQLERQNK------------------ELK 1808
Cdd:COG3096 821 FVGGHLAVAFAPDPEAELAALRQRRSELE-RELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrleELR 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1809 AKLQELEGAVKS--KFKATISALEAKIGQL------EEQLEQEAKERAAANKLVRRTEKKLKEIFmqvedERRHADQYKE 1880
Cdd:COG3096 900 EELDAAQEAQAFiqQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVV-----QRRPHFSYED 974
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1039738675 1881 --QMEKANARM-KQLKRQLEEAEEEATRANASRRKLQRELDDAT 1921
Cdd:COG3096 975 avGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYN 1018
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1034-1266 |
7.25e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1034 NLAKIR-NKQEVMISDLEERLKKEE-KTRQELEKAKRKLDGE-TTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1110
Cdd:PHA02562 172 NKDKIReLNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1111 DETlhknNALKVARELQAQIAelqedfeSEKASRNKAEKQ----------KRDLSEElEALKTELEDTLDTTAAQQELRT 1180
Cdd:PHA02562 252 DPS----AALNKLNTAAAKIK-------SKIEQFQKVIKMyekggvcptcTQQISEG-PDRITKIKDKLKELQHSLEKLD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1181 KREQEVAELKKALEDETKNheaqIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAE- 1259
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKK----LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTk 395
|
....*..
gi 1039738675 1260 SEHKRKK 1266
Cdd:PHA02562 396 SELVKEK 402
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1623-1839 |
7.38e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1623 ALAVASKKKMEIDLKDLEAqieAANKARDEVIKQL---------RKLQAQ-MKDYQRELEE----ARASRDEIFAQSKE- 1687
Cdd:PRK10929 19 AATAPDEKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1688 ----SEKKLKSLEAEILQLQEELAssERARRhAEQERDElADEIANSASGKSALLDEKRRL----EARI-AQLEEELEEE 1758
Cdd:PRK10929 96 rsvpPNMSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1759 QSNMELLNDRFRKTTLQVDTLntELAaersaaQKSDNARQQLER--------QNKELKAKLQELEGAVKS-KFKATISAL 1829
Cdd:PRK10929 172 QAQLTALQAESAALKALVDEL--ELA------QLSANNRQELARlrselakkRSQQLDAYLQALRNQLNSqRQREAERAL 243
|
250
....*....|
gi 1039738675 1830 EaKIGQLEEQ 1839
Cdd:PRK10929 244 E-STELLAEQ 252
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
861-1223 |
8.04e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.36 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 861 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESR 940
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 941 VEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAE 1020
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1021 CSSQLAEEEEKAKN-----LAKIRNKQEVMISDLEERLKKEEKTRqeLEKAKRKLDgettDLQDQIAELQAQVDE-LKVQ 1094
Cdd:pfam09731 244 LVDQYKELVASERIvfqqeLVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREID----QLSKKLAELKKREEKhIERA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1095 LTKKEEELqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKrdLSEELEALKTELEDTLDTTAA 1174
Cdd:pfam09731 318 LEKQKEEL---------DKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--LRTELERQAEAHEEHLKDVLV 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039738675 1175 QQELRTKREQEvAELKKALEDETKNHEAQIQDMrqrhATALEELSEQLE 1223
Cdd:pfam09731 387 EQEIELQREFL-QDIKEKVEEERAGRLLKLNEL----LANLKGLEKATS 430
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
975-1114 |
1.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 975 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR---------NKQEVM 1045
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1046 ISDLEERLK----KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETL 1114
Cdd:COG1579 105 ISDLEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1588-1894 |
1.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1588 RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLK-------DLEAQIEAANKARDEVIKQLRKL 1660
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelaQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1661 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELA----DEIANSASGKSA 1736
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldelLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1737 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1816
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1817 AVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKR 1894
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1046-1203 |
1.23e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.67 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1046 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARE 1125
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1126 -LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELKKALEDETKNHEAQ 1203
Cdd:pfam12795 160 aLKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1124-1312 |
1.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1124 RELQAQIAELQEdFESEKAsrnKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQevaelKKALEDETKNHEAQ 1203
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELA------ALEARLEAAKTE-----LEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1204 IQDMRQRhataLEELSEQLEQAKRFK--ANLEKNKQGLETDNKELAcevKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1281
Cdd:COG1579 68 IEEVEAR----IKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|.
gi 1039738675 1282 DRLRVELAEKANKLQNELDNVSTLLEEAEKK 1312
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1539-1750 |
1.32e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDE 1618
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1619 RKQRALAVASKKKMEidlkdleaqiEAANKARDEVIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKSLEAE 1698
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1699 ILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1607-1797 |
1.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1607 QVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1686
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1687 ESEKKLKSLEA--------------------------EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE 1740
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 1741 KRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNAR 1797
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
856-1210 |
1.51e-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: 43.58 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEELLKVKEKqtkvegeLEEMERKHQQLleekNILAEQLQAETELFAEAEEMRARLAAKKQELE---E 932
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEqdsE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 933 ILHDLESRVeeeeERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEAKIK-----KMEEEVLLLEDQNSKF 1007
Cdd:pfam05557 188 IVKNSKSEL----ARIPELEKELERLREHNKHLNENI------ENKLLLKEEVEDLKRKlereeKYREEAATLELEKEKL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1008 IKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMI---SDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1084
Cdd:pfam05557 258 EQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKeenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1085 QAQVDEL--KVQLTKKEEELQGALARGDDETLHKNNA----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL 1158
Cdd:pfam05557 338 KALVRRLqrRVLLLTKERDGYRAILESYDKELTMSNYspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQA 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039738675 1159 EALKTELeDTLDTTAAQQELRTKREqEVAELKKALEDetknHEAQIQDMRQR 1210
Cdd:pfam05557 418 QTLEREL-QALRQQESLADPSYSKE-EVDSLRRKLET----LELERQRLREQ 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1247-1495 |
1.68e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1247 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1326
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1327 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSlqeqqeeeeearKNLE---KQVLALQSQLADTKKKVDDDLGTIESLEEA 1403
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGS------------ESFSdflDRLSALSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1404 KKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDR 1483
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|..
gi 1039738675 1484 AEAEAREKETKA 1495
Cdd:COG3883 229 AAAAAAAAAAAA 240
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1624-1878 |
1.70e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1624 LAVASKKKMEIDLKDLE--AQIEAANKARDEVIKQ--------LRKLQAQMKDYQRELEEARASRDEIFA--QSK--ESE 1689
Cdd:PHA02562 147 LSAPARRKLVEDLLDISvlSEMDKLNKDKIRELNQqiqtldmkIDHIQQQIKTYNKNIEEQRKKNGENIArkQNKydELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1690 KKLKSLEAEILQLQEELAsserarrhaeqerdELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSN-------- 1761
Cdd:PHA02562 227 EEAKTIKAEIEELTDELL--------------NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctq 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1762 -MELLNDRFRKTTLQVDTLNTELaaersaaQKSDNARQQLERQNKELKA---KLQELEGAVkSKFKATISALEAKIGQLE 1837
Cdd:PHA02562 293 qISEGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEIMDEFNEqskKLLELKNKI-STNKQSLITLVDKAKKVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039738675 1838 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQY 1878
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
977-1150 |
1.73e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 977 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLE------ 1050
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1051 --------------------ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1110
Cdd:COG3883 113 sfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039738675 1111 DETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQ 1150
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1597-1933 |
1.77e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1597 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDL-------KDLEAQIEAANKARDEVIKQLRkLQAQMKDYQR 1669
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVEMARELeelsareSDLEQDYQAASDHLNLVQTALR-QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1670 ELEEArasrdeifaqskesEKKLKSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAria 1749
Cdd:COG3096 355 DLEEL--------------TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL----------KSQLADYQQALDV--- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1750 QLEEELEEEQSNMELLNDRfrkTTLQVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQeLEGAVKSKFKATISAL 1829
Cdd:COG3096 408 QQTRAIQYQQAVQALEKAR---ALCGLPDLTPENAEDYLAAFRAK--EQQATEEVLELEQKLS-VADAARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1830 EAKIGQLE-EQLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRhadQYKEqMEKANARMKQLKRQLEEAEEEATRANA 1908
Cdd:COG3096 482 CKIAGEVErSQAWQTARE-------LLRRYRSQQALAQRLQQLRA---QLAE-LEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
330 340
....*....|....*....|....*
gi 1039738675 1909 SRRKLQRELDDATEANEGLSREVST 1933
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAE 575
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1127-1492 |
1.84e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1127 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEalkteledtldttaaqqelrtkREQEVAELKKALEDETkNHEAQIQD 1206
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----------------------RRRKLEEAEKARQAEM-DRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1207 MRQRHATALEELSEQLEQAKRfKANLEKNKQgletdnKELACEVKVLQQVKAESEHKRKKLDAQVQELHA----KVSEGD 1282
Cdd:pfam17380 338 EQERMAMERERELERIRQEER-KRELERIRQ------EEIAMEISRMRELERLQMERQQKNERVRQELEAarkvKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1283 RLRvelaeKANKLQNELDNVSTLLEEAEKKGIKFakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQ 1362
Cdd:pfam17380 411 RQR-----KIQQQKVEMEQIRAEQEEARQREVRR------LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1363 EEEEEARKNLEKQ-VLALQSQLADTKKKVDDdlgtieslEEAKKKLLKdvealsQRLEEKVLAYdkLEKTKNRLQQELDD 1441
Cdd:pfam17380 480 EKEKRDRKRAEEQrRKILEKELEERKQAMIE--------EERKRKLLE------KEMEERQKAI--YEEERRREAEEERR 543
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039738675 1442 LTVDLDHQRQIVSNLEKKqkkfdqllaeekgisaryAEERDRAEAEAREKE 1492
Cdd:pfam17380 544 KQQEMEERRRIQEQMRKA------------------TEERSRLEAMERERE 576
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1665-1863 |
1.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1665 KDYQRELEEARASRDEIFAQSK---ESEKKLKSLEAeilqlQEELassERARRHAEQERDELADEIAnsasgksalldek 1741
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKkeaEAIKKEALLEA-----KEEI---HKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1742 rRLEARIAQLEeeleeeqsnmELLNDRFRkttlQVDTLNTELaaersaaqksDNARQQLERQNKELKAKLQELEGAVKSK 1821
Cdd:PRK12704 86 -KLEKRLLQKE----------ENLDRKLE----LLEKREEEL----------EKKEKELEQKQQELEKKEEELEELIEEQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039738675 1822 FKA--TISAL---EAKiGQLEEQLEQEAKERAAanKLVRRTEKKLKE 1863
Cdd:PRK12704 141 LQEleRISGLtaeEAK-EILLEKVEEEARHEAA--VLIKEIEEEAKE 184
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
856-1087 |
1.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKKQELEEILH 935
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 936 D--------------LESR-----VEEEEERNQILQNEKKKMQAHIQdleeqldeeegARQKLQLEKVTAEAKIKKMEEE 996
Cdd:COG3883 94 AlyrsggsvsyldvlLGSEsfsdfLDRLSALSKIADADADLLEELKA-----------DKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 997 VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD 1076
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250
....*....|.
gi 1039738675 1077 LQDQIAELQAQ 1087
Cdd:COG3883 243 AASAAGAGAAG 253
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1607-1744 |
2.03e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1607 QVRELEAELEDERKQRALAVASKKKMEIdlkdLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR---------AS 1677
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarrrvlAP 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1678 RDEIFAQSKESEKKL-KSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1744
Cdd:pfam00529 135 IGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
903-1496 |
2.05e-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: 43.19 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 903 AEQLQAETELfaeaEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQdleeqldeeegarqKLQLE 982
Cdd:pfam05557 2 AELIESKARL----SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR--------------LLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 983 KVTAEAKIKKMEEEVLLL---EDQNSKFIKEKKLMEDRIAECSSQLAEEeekaknLAKIRNKQEVMISDLEERLKKEEKT 1059
Cdd:pfam05557 64 EAEAEEALREQAELNRLKkkyLEALNKKLNEKESQLADAREVISCLKNE------LSELRRQIQRAELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1060 RQELEKAKRKLdgetTDLQDQIAELQAQVDELKVQLTK-KEEELQGALARGDDETlhknnaLKVARELQAQIAELQEDFE 1138
Cdd:pfam05557 138 QERLDLLKAKA----SEAEQLRQNLEKQQSSLAEAEQRiKELEFEIQSQEQDSEI------VKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1139 SEKASRNKAEKQKRD---LSEELEALKTELEdtldttaaqQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATA 1214
Cdd:pfam05557 208 RLREHNKHLNENIENkllLKEEVEDLKRKLE---------REEKYREEAATLELEKEkLEQELQSWVKLAQDTGLNLRSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1215 lEELSEQLEQAKRFKANLEKNKQGLETDnkelaceVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1294
Cdd:pfam05557 279 -EDLSRRIEQLQQREIVLKEENSSLTSS-------ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1295 LQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEearknLEK 1374
Cdd:pfam05557 351 LTKERDGYRAILESYDKE-LTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE-----REL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1375 QVLALQSQLAD---TKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYD--------------KLEKTKNRLQQ 1437
Cdd:pfam05557 425 QALRQQESLADpsySKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDydpkktkvlhlsmnPAAEAYQQRKN 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1438 ELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERdRAEAEAREKETKAL 1496
Cdd:pfam05557 505 QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESAELKNQRL 562
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
976-1220 |
2.12e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 42.86 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 976 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE--KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERL 1053
Cdd:COG5391 306 FEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVfaKRLEQNQNSILNEGVVQAETLRSSLKELLTQLQDEIKSRESLI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1054 KkeekTRQELEKAKrkldgettdlqdqiAELQAQVDELKVQLTKKEEElqgalargDDETLHKNNALKVARELQAQIAE- 1132
Cdd:COG5391 386 L----TDSNLEKLT--------------DQNLEDVEELSRSLRKNSSQ--------RAVVSQQPEGLTSFSKLSYKLRDf 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1133 LQEDFESEKasRNKAEKQKRDLSEELEALKTELEDTldTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1212
Cdd:COG5391 440 VQEKSRSKS--IESLQQDKEKLEEQLAIAEKDAQEI--NEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWK 515
|
....*...
gi 1039738675 1213 TALEELSE 1220
Cdd:COG5391 516 SVKEQLDR 523
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1054-1433 |
2.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1054 KKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAEL 1133
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELE---------------------QAREELEQL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1134 QEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKK---ALEDETKNHEAQIQDMRQR 1210
Cdd:COG4372 65 EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1211 HATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1290
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1291 KANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK 1370
Cdd:COG4372 225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1371 NLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKN 1433
Cdd:COG4372 305 AALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1632-1794 |
2.35e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1632 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ---RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAs 1708
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1709 seRARRHAEQE---RDELADEIANSASGKSALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAA 1785
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
....*....
gi 1039738675 1786 ERSAAQKSD 1794
Cdd:pfam00529 203 AKLDLERTE 211
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1653-1896 |
2.48e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1653 VIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEE----LASSERARRHAE---QERDELAD 1725
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtLAKAQQVNAESErtlGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1726 EIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTlntelaAERSAAQKSDNarqQL 1800
Cdd:pfam06008 90 AIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE------AELKAAQDLLS---RI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1801 ERQNKELKAKLQELEGAVKSKfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKE 1880
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
250
....*....|....*.
gi 1039738675 1881 QMEKANARMKQLKRQL 1896
Cdd:pfam06008 237 TLKTARDSLDAANLLL 252
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1077-1341 |
2.67e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1077 LQDQIAELQAQVDELKVQLTKKEEELQgalargddetLHKNNaLKVARELQAQ-IAELQEDFESEKASRNKAEKQKRDLS 1155
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIK----------TYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1156 EELEALKTELEdtlDTTAAQQELRTKReqevAELKKALEDETKNHEaqiqdMRQRHA---TALEELSEQLEQakrfkanL 1232
Cdd:PHA02562 241 DELLNLVMDIE---DPSAALNKLNTAA----AKIKSKIEQFQKVIK-----MYEKGGvcpTCTQQISEGPDR-------I 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1233 EKNKQGLetdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTL------- 1305
Cdd:PHA02562 302 TKIKDKL------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLvdkakkv 363
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039738675 1306 ---LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQK 1341
Cdd:PHA02562 364 kaaIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1791-1939 |
3.16e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1791 QKSDNARQQLERQNKELKAKLQELEGAVkSKFKA---------TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1861
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL-EEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1862 KEIFMQVEDERRHAdqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA-NEGLSREVSTLKNRLR 1939
Cdd:COG3206 250 GSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELE 323
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
987-1979 |
3.23e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 987 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQlAEEEEKAKNLAKIRNKQEVMISDLE--------ERLKKEEK 1058
Cdd:TIGR01612 578 EKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDK-NEYIKKAIDLKKIIENNNAYIDELAkispyqvpEHLKNKDK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1059 TRQELEKAKRKL-DGETTDLQDQIA-----------ELQAQVDELKVQLTKKEEELQGAlargDDET--LHKNNALKVAR 1124
Cdd:TIGR01612 657 IYSTIKSELSKIyEDDIDALYNELSsivkenaidntEDKAKLDDLKSKIDKEYDKIQNM----ETATveLHLSNIENKKN 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1125 ELQAQIAELQEDFESEKAsrnkaekqkRDLSEELEALKT---ELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1201
Cdd:TIGR01612 733 ELLDIIVEIKKHIHGEIN---------KDLNKILEDFKNkekELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDN 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1202 AQIQDMRQRHATALE----------ELSEQLEQAKRFK----------ANLEKN-KQGLETDNKELAcevKVLQQVKAES 1260
Cdd:TIGR01612 804 IKDEDAKQNYDKSKEyiktisikedEIFKIINEMKFMKddflnkvdkfINFENNcKEKIDSEHEQFA---ELTNKIKAEI 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1261 EhkrkklDAQVQELHAKVSEGDRLrveLAEKANKLQNELDNVSTLLEEAEKkgIKFAKDAAGLESQLQDTQELLQEETRQ 1340
Cdd:TIGR01612 881 S------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTLKKVDEY--IKICENTKESIEKFHNKQNILKEILNK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1341 KLNLSsrirqleEEKNSLQeqqeeeeearKNLEKQvlaLQSQLADTKKKVDDDL--GTIESLEEAKKKLLKDVEALSQRL 1418
Cdd:TIGR01612 950 NIDTI-------KESNLIE----------KSYKDK---FDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANL 1009
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1419 ---EEKVL--AYDKLEKTKNRLQQELDDLTVDLDH-QRQIVSNLEKKQKKFDQLLAeeKGISARYAEERDRAEA------ 1486
Cdd:TIGR01612 1010 gknKENMLyhQFDEKEKATNDIEQKIEDANKNIPNiEIAIHTSIYNIIDEIEKEIG--KNIELLNKEILEEAEInitnfn 1087
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1487 EAREKetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ 1566
Cdd:TIGR01612 1088 EIKEK----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1567 AT---EDAKlRLEVNMQAMKAQFERDLQTRDEQNEekkrlLLKQVRELEAELEDERKQRALAVA---------------S 1628
Cdd:TIGR01612 1161 KAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEEVKGINLSygknlgklflekideE 1234
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1629 KKKMEIDLKDLEAQIEAAnkarDEVIKQLRKLQAQM---KDYQRELEEARASRDE-----IFAQSKES------EKKLK- 1693
Cdd:TIGR01612 1235 KKKSEHMIKAMEAYIEDL----DEIKEKSPEIENEMgieMDIKAEMETFNISHDDdkdhhIISKKHDEnisdirEKSLKi 1310
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1694 ----SLEAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEKRRLEARIAQLEEELEEEQSNMEL 1764
Cdd:TIGR01612 1311 iedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEK 1390
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1765 LNDRFR------------KTTL----------QVDTLNTELAAERSaaqKSDNARQQLERQNKELKAKLQELEGA----- 1817
Cdd:TIGR01612 1391 LIKKIKddinleeckskiESTLddkdidecikKIKELKNHILSEES---NIDTYFKNADENNENVLLLFKNIEMAdnksq 1467
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1818 --VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKlKEIFMQVEDE-------------RRHADQYKEQM 1882
Cdd:TIGR01612 1468 hiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDvtellnkysalaiKNKFAKTKKDS 1546
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1883 EKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE-------GLSREVSTLKNRLRRGGPISFSSSRSGRRQ 1955
Cdd:TIGR01612 1547 EIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDksnkaaiDIQLSLENFENKFLKISDIKKKINDCLKET 1626
|
1130 1140
....*....|....*....|....
gi 1039738675 1956 LHIEGASLELSDDDTESKTSDVND 1979
Cdd:TIGR01612 1627 ESIEKKISSFSIDSQDTELKENGD 1650
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1040-1313 |
3.23e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1040 NKQEVMISDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHK 1116
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1117 NNALKVARELQAQIAELQEdfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK---REQEVAELKKAL 1193
Cdd:COG1340 81 DELNEKLNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKikeLEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1194 EDETKNHE--AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQV 1271
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1039738675 1272 QELHAKVSEGDRLRVEL-AEKANKLQNELDNVSTLLEEAEKKG 1313
Cdd:COG1340 237 KELRELRKELKKLRKKQrALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
981-1108 |
3.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 981 LEKVTAEAKIKKMEEEVllledqnSKFIKE-KKLMEDRIAECSSQLAEEEEKAKNLA----KIRNKQevmISDLEERLK- 1054
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-------KRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFekelRERRNE---LQKLEKRLLq 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1055 KEEKTRQELEKAKRKlDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1108
Cdd:PRK12704 94 KEENLDRKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1552-1938 |
3.32e-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: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1552 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFerdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1631
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1632 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSKESEKKLKSLEAEILQLQEElasser 1711
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-------KIKELEKQLNQLKSEISDLNNQ------ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1712 arrhAEQERD-ELADEIANSAsgksallDEKRRLEARIAQLeeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAA 1790
Cdd:TIGR04523 304 ----KEQDWNkELKSELKNQE-------KKLEEIQNQISQN-------NKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1791 QKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVED 1870
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQ-INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039738675 1871 ERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
846-954 |
3.33e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 846 RVFTKVKPLLQVTRQEEELQAKDEELlkVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAA 925
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 1039738675 926 KKQELEEILHDLESRVEEEEERNQILQNE 954
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1524-1674 |
3.41e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.44 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1524 EDLMSSKD-DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQT---------- 1592
Cdd:COG1193 506 RELLGEESiDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAREEAEEilrearkeae 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1593 ------RDEQNEEKK-RLLLKQVRELEAELEDERKQRA-----------------------------LAVASKK------ 1630
Cdd:COG1193 586 elirelREAQAEEEElKEARKKLEELKQELEEKLEKPKkkakpakppeelkvgdrvrvlslgqkgevLEIPKGGeaevqv 665
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1631 ---KMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL-------EEA 1674
Cdd:COG1193 666 gilKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSKASTVSPELdlrgmrvEEA 719
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
856-1008 |
3.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEellkVKEKQTKVEGELEEMERKHQQ----LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELE 931
Cdd:PRK12704 52 EAIKKEALLEAKEE----IHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 932 EILHDLEsrveeeeernQILQNEKKKMQaHIQDLEEQLdeeegARQKLqLEKVTAEAK------IKKMEEEVLLLEDQNS 1005
Cdd:PRK12704 128 KKEEELE----------ELIEEQLQELE-RISGLTAEE-----AKEIL-LEKVEEEARheaavlIKEIEEEAKEEADKKA 190
|
...
gi 1039738675 1006 KFI 1008
Cdd:PRK12704 191 KEI 193
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1530-1705 |
3.57e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1530 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqamkaQFERDLQTRDEQNEEKKrlllkqvR 1609
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE---------------KLKEELEEKKEKLQEEE-------D 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1610 ELEAELEDERKQRalavaskkkmeidlkdleaqIEAANKARDEVIKQLRKLQAQMKDYQ--RELEEARASRDEIfAQSKE 1687
Cdd:PRK00409 566 KLLEEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKGGYASVkaHELIEARKRLNKA-NEKKE 624
|
170
....*....|....*...
gi 1039738675 1688 SEKKLKSLEAEILQLQEE 1705
Cdd:PRK00409 625 KKKKKQKEKQEELKVGDE 642
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1169-1442 |
3.68e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1169 LDTTAAQQELRTK-RE--QEVAELKKALEdETKNHEAQIQDMRQRHATALEELS---------EQLEQAKRFKANLEKNK 1236
Cdd:COG0497 147 LDAFAGLEELLEEyREayRAWRALKKELE-ELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1237 QGLETDNKELA-CEVKVLQQV-KAESE-HKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNVSTlleeaekkg 1313
Cdd:COG0497 226 EALQEALEALSgGEGGALDLLgQALRAlERLAEYDPSLAELAERLES---ALIELEEAASELRRYLDSLEF--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1314 ikfakdaaglesqlqDTQELlqEETRQKLNLssrIRQLeeeknslqeqqeeeeeARK---NLEkQVLALQSQLADTKKKV 1390
Cdd:COG0497 294 ---------------DPERL--EEVEERLAL---LRRL----------------ARKygvTVE-ELLAYAEELRAELAEL 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1391 DDDLGTIESLEEAKKKLLKDVEALSQRLEEK-VLAYDKLEKtknRLQQELDDL 1442
Cdd:COG0497 337 ENSDERLEELEAELAEAEAELLEAAEKLSAArKKAAKKLEK---AVTAELADL 386
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1325-1584 |
3.82e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1325 SQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAK 1404
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1405 KKLLKDVEALSQRLEEKVLAYDKLEKTK---NRLQQELDDL-------TVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-- 1472
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLewrqqteVLSPEEEKELVEKIKELEKELEKAKKALEKne 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1473 ----ISARYAEERDRAEAEAREKETkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1548
Cdd:COG1340 161 klkeLRAELKELRKEAEEIHKKIKE----LAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1039738675 1549 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1584
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1636-1729 |
3.85e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1636 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES--EKKLKSLEAEILQLQEELAsserar 1713
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAiaRKEIKDLQKELEKLNEEYA------ 196
|
90
....*....|....*.
gi 1039738675 1714 RHAEQERDELADEIAN 1729
Cdd:cd22656 197 AKLKAKIDELKALIAD 212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-1041 |
3.88e-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: 41.67 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 856 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLL------EEKNILAEQLQAETelFAEAEEMRARLAAKKQE 929
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlGRQPPLALLLSPED--FLDAVRRLQYLKYLAPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 930 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 1009
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEE-------ERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
170 180 190
....*....|....*....|....*....|..
gi 1039738675 1010 EKKLMEDRIAECSSQLAEEEEKAKNLAKIRNK 1041
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1627-1728 |
4.32e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1627 ASKKKMEID-----LKDLEAQIEAANKARDEVIK-----------QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1690
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039738675 1691 KLKSLEAEILQLQEELAS-SERARRHAEQERDEL-ADEIA 1728
Cdd:COG0542 479 ELEQRYGKIPELEKELAElEEELAELAPLLREEVtEEDIA 518
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
976-1234 |
4.50e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 976 RQKlQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKlMEDRIAECssqlaEEEEKAKNLAKI-RNKQEVMISDLEERLK 1054
Cdd:pfam02029 85 RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEK-RDSRLGRY-----KEEETEIREKEYqENKWSTEVRQAEEEGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1055 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1134
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1135 EDFESEKASRNKAEKQKRDL----SEELEALKTEledtldttaaQQElrtkREQEVAELKKALEDETKNHEAQIQDMRQr 1210
Cdd:pfam02029 238 EEAEVFLEAEQKLEELRRRRqekeSEEFEKLRQK----------QQE----AELELEELKKKREERRKLLEEEEQRRKQ- 302
|
250 260
....*....|....*....|....
gi 1039738675 1211 hATALEELSEQlEQAKRFKANLEK 1234
Cdd:pfam02029 303 -EEAERKLREE-EEKRRMKEEIER 324
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
988-1226 |
5.03e-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: 42.07 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 988 AKIKKMEEEVLLLEDqnskFIKEKKLMEDRIAECSSQLAEEEEKAkNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1067
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEKKL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1068 RKLDGETTDLQDQiAELQAQVDELKVQLTKKEEELQGALArgddetlHKNNALKVARELQAQIAELQEDFESEKAS---- 1143
Cdd:pfam18971 638 ESKSGNKNKMEAK-AQANSQKDEIFALINKEANRDARAIA-------YTQNLKGIKRELSDKLEKISKDLKDFSKSfdef 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1144 RNKAEKQKRDLSEELEALKTELED----------TLDTTAAQQELRTKREQEVAELKKALEDetknHEAQIQD--MRQRH 1211
Cdd:pfam18971 710 KNGKNKDFSKAEETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSD----LENSVKDviINQKV 785
|
250
....*....|....*
gi 1039738675 1212 ATALEELSEQLEQAK 1226
Cdd:pfam18971 786 TDKVDNLNQAVSVAK 800
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1227-1492 |
5.22e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1227 RFKANLEKNKQgLETDNKELACEVKVLQQVK-AESEHKRKKLDAQVQELHAKVsegdrlrVELAEKANKLQNELDNVSTL 1305
Cdd:pfam00038 12 RLASYIDKVRF-LEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQL-------DTLTVERARLQLELDNLRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1306 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLqeqqeeeeeaRKNLEKQVLALQSQLAD 1385
Cdd:pfam00038 84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFL----------KKNHEEEVRELQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1386 TKKKVD------DDLGTI-----ESLEEAKKKLLKDVEAL-SQRLEEKVLAYDK----LEKTKNRLQQ---ELDDLTVDL 1446
Cdd:pfam00038 154 TQVNVEmdaarkLDLTSAlaeirAQYEEIAAKNREEAEEWyQSKLEELQQAAARngdaLRSAKEEITElrrTIQSLEIEL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039738675 1447 DHQRQIVSNLEKKqkkfdqlLAEEKgisARYAEERDRAEAEAREKE 1492
Cdd:pfam00038 234 QSLKKQKASLERQ-------LAETE---ERYELQLADYQELISELE 269
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1086-1204 |
5.43e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1086 AQVDELKVQLTKKEEELQgALARGDDETLHKNnalkvARELQAQIAELQEDFESEKAsRNKAEKQkrdLSEELEALKTEL 1165
Cdd:COG0542 411 EELDELERRLEQLEIEKE-ALKKEQDEASFER-----LAELRDELAELEEELEALKA-RWEAEKE---LIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039738675 1166 EDTLDTTAAQQELRTKREQEVAELKKALEDE-TKNHEAQI 1204
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAEV 520
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1416-1883 |
5.55e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1416 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL---LAEEKGISARYAEERDRAEAEAREKE 1492
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1493 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKR-----------------ALEQQVEEMR 1555
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1556 TQLEELEDELQATEDAKLRLEVnMQAMKAQFERDLQTRDEQNEEKKRL---------LLKQVRELEAELEDERKQRALAV 1626
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELegyemdynsYLKSIESLKKKIEEYSKNIERMS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1627 ASKKKMeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKSLEAEIL------ 1700
Cdd:PRK01156 391 AFISEI---LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL-------SRNMEMLNGQSVcpvcgt 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1701 QLQEElaSSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARiaqleeELEEEQSNMELLNDRFRKTTLQVDTLN 1780
Cdd:PRK01156 461 TLGEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR------KEYLESEEINKSINEYNKIESARADLE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1781 TELAAERSAAQKSDNARQQLERQNKelkAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQeakeraaANKLVRRTEKK 1860
Cdd:PRK01156 533 DIKIKINELKDKHDKYEEIKNRYKS---LKLEDLDSKRTSWLNALAVISLIDIETNRSRSNE-------IKKQLNDLESR 602
|
490 500
....*....|....*....|...
gi 1039738675 1861 LKEIFMQVEDERRHADQYKEQME 1883
Cdd:PRK01156 603 LQEIEIGFPDDKSYIDKSIREIE 625
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1647-1893 |
5.65e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1647 NKARDEVIKQLRKLQA-QMKDYQRE-----LEEARASRDEI------FAQSKESEKKLKSLEAEIlqlqeELASSERARR 1714
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEElsnerLRKLRSLLTKLsealdkLRSYLPKLNPLREEKKKV-----SVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1715 HAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQ------SNMELLNDrFRKTTLQVDTLNTELAAERS 1788
Cdd:PRK05771 90 DVEEELEKIEKEI-------KELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLG-FKYVSVFVGTVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1789 AAQKSDNA-----------------RQQLERQNKELK-AKLQELEGAVKSKFKATISALEAKIGQLEEQLEqeakeraaa 1850
Cdd:PRK05771 162 LESDVENVeyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039738675 1851 nklvrRTEKKLKEIFMQVEDERRHADQYKEQM-EKANARMKQLK 1893
Cdd:PRK05771 233 -----SLLEELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
857-1220 |
5.83e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 857 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELeeilHD 936
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEN----SS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 937 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV------LLLEDQNSKFIKE 1010
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILesydkeLTMSNYSPQLLER 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1011 KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKeeKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1090
Cdd:pfam05557 382 IEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA--LRQQESLADPSYSKEEVDSLRRKLETLELERQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1091 LKVQLTKKEEELQGALARGDDET-------LHKNNALKVARELQAQIAELQEDFESekasrnkaekqkrdLSEELEALKT 1163
Cdd:pfam05557 460 LREQKNELEMELERRCLQGDYDPkktkvlhLSMNPAAEAYQQRKNQLEKLQAEIER--------------LKRLLKKLED 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 1164 ELEDTLdttAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSE 1220
Cdd:pfam05557 526 DLEQVL---RLPETTSTMNFKEVLDLRKELESA----ELKNQRLKEVFQAKIQEFRD 575
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1033-1388 |
5.83e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1033 KNLAKIRNKQEVMISDLEERLKKE--EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKKEEELQGALARGD 1110
Cdd:NF033838 91 KKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAE----KKAKDQKEEDRRNY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1111 DETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKAE-KQKRDLSEELEALKTELEDtLDTTAAQQELRTKREQEvAE 1188
Cdd:NF033838 167 PTNTYKTLELEIAEsDVEVKKAELELVKEEAKEPRDEEKiKQAKAKVESKKAEATRLEK-IKTDREKAEEEAKRRAD-AK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1189 LKKALEDETKNHEAQIQDMRQRHAtALEELSEqlEQAKRFKANLEKNKQGLET--------DNKELACEVKVLQQVKA-- 1258
Cdd:NF033838 245 LKEAVEKNVATSEQDKPKRRAKRG-VLGEPAT--PDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVEEAKKKak 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1259 --ESEHKR-------KKLDAQVQELHAKVSEGDrlrVELA-EKANKLQNElDNVSTLLEEAEKKgikfAKDAAGLESQLQ 1328
Cdd:NF033838 322 dqKEEDRRnyptntyKTLELEIAESDVKVKEAE---LELVkEEAKEPRNE-EKIKQAKAKVESK----KAEATRLEKIKT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1329 DTQELlQEETRQKLNLSSRIRQLEEEK-------------------------NSLQEQQEEEEEARKNLEKQVLALQSQL 1383
Cdd:NF033838 394 DRKKA-EEEAKRKAAEEDKVKEKPAEQpqpapapqpekpapkpekpaeqpkaEKPADQQAEEDYARRSEEEYNRLTQQQP 472
|
....*
gi 1039738675 1384 ADTKK 1388
Cdd:NF033838 473 PKTEK 477
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1055-1098 |
5.89e-03 |
|
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467481 [Multi-domain] Cd Length: 103 Bit Score: 38.29 E-value: 5.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1039738675 1055 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKK 1098
Cdd:cd23165 60 SLEEAQERLEKAKEELEEEIEKLEEEIDEIEEEMKELKVQLYAK 103
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1539-1747 |
6.01e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1539 ELEKSKRALEQQVEEMRTQLEELEdeLQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELE 1612
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLpdflehAKEQNKELK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1613 AELEderkqralavASKKKMEIDLKDLEAQieaankarDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1692
Cdd:PRK04778 331 EEID----------RVKQSYTLNESELESV--------RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1693 KSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAR 1747
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERY----------RNKLHEIKRYLEKS 437
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1022-1266 |
6.58e-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: 40.95 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1022 SSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL----------------Q 1085
Cdd:pfam15905 72 SKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellkakfsedgtQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1086 AQVDELKVQLTKKEEEL----QGALARGDDETLHKNNALKVARELQAQIAELQE---DFESEKASRNKAEKQKRDLSEEL 1158
Cdd:pfam15905 152 KKMSSLSMELMKLRNKLeakmKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEKIEEKSETEKLLEYITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1159 EALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQg 1238
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD--------LNEKCKLLESEKEELLREYEEKE- 302
|
250 260
....*....|....*....|....*...
gi 1039738675 1239 lETDNKELACEVKVLQQVKAESEHKRKK 1266
Cdd:pfam15905 303 -QTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1077-1268 |
6.97e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.11 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1077 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD--ETL----HKNNAL--------KVARELQAQIAELQEDFESEKA 1142
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKflENLaslkHENDNLssmlnrkeRRLKDLEDQLSELKNSYEELTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1143 SRNKAEKQKRDLSEELEALKTELE------DTLdtTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQR---HAT 1213
Cdd:pfam17078 88 SNKQLKKRLENSSASETTLEAELErlqiqyDAL--VDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRissNDK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1214 ALEELSEQLEQAKRFKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLD 1268
Cdd:pfam17078 166 DIDTKLDSYNNKFKNLDNIYVNKnNKLLTKLDSLAQLLDLPSWLNLYPESRNKILE 221
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1049-1223 |
7.47e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.55 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1049 LEERLKKEEKTRQELEK-----AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARgddetlhknNALKVA 1123
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQ---------NVEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1124 RELQAQIAELQEDFesekasRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELKKALEDETK 1198
Cdd:pfam01442 73 QRLEPYTEELRKRL------NADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*....
gi 1039738675 1199 NHEAQ----IQDMRQRHATALEELSEQLE 1223
Cdd:pfam01442 147 EVQAQlsqrLQELREKLEPQAEDLREKLD 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
892-1101 |
7.88e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 892 HQQLLEEKNILAEQLQAE-----TELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQahiqdle 966
Cdd:PHA02562 200 YNKNIEEQRKKNGENIARkqnkyDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 967 eqldeeegarqklQLEKV-----------TAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNL 1035
Cdd:PHA02562 273 -------------QFQKVikmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039738675 1036 AKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE 1101
Cdd:PHA02562 340 LELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
867-1084 |
8.00e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 867 KDEELLKVKEKQTKVEGELEEMErkhqQLLEEKNILAEQLQAETelFAEAEEMRarlaakkQELEEILHDLESRVEEEEE 946
Cdd:PRK05771 41 SNERLRKLRSLLTKLSEALDKLR----SYLPKLNPLREEKKKVS--VKSLEELI-------KDVEEELEKIEKEIKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 947 RNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKFIKEKKLME---------- 1015
Cdd:PRK05771 108 EISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgTVPEDKLEELKLESDVENVEYISTDKGyvyvvvvvlk 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039738675 1016 DRIAECSSQLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1084
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
850-1090 |
8.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 850 KVKPLLQVTRQEEELQAKDEELLKVK------------------EKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETE 911
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKelaeqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 912 LFAEAEEMRARLAAKKQELEEILHDLESR----VEEEEERNQILQ----------NEKKKMQAHIQDLEEQLDEEEGARQ 977
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 978 KLQLekvtAEAKIKKMEEEvllLEDQNSKFIKEK-KLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKE 1056
Cdd:PRK03918 634 ELAE----TEKRLEELRKE---LEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
250 260 270
....*....|....*....|....*....|....
gi 1039738675 1057 EKTRQELEKAKRKLDgETTDLQDQIAELQAQVDE 1090
Cdd:PRK03918 707 EKAKKELEKLEKALE-RVEELREKVKKYKALLKE 739
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1081-1233 |
8.34e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1081 IAELQAQVDELKVQLTKKEEELQGALARGDD-ETLHKNNAlkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1159
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRlQALESELA-----ISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1160 ALKTELED------TLDTT-AAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL 1232
Cdd:pfam00529 128 RRRVLAPIggisreSLVTAgALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDL 207
|
.
gi 1039738675 1233 E 1233
Cdd:pfam00529 208 E 208
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1640-1741 |
8.36e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1640 EAQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKslEAEILQLQEELAS-SERARRHAEQ 1718
Cdd:COG0711 37 ADGLAEAERAKEE-------AEAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAEIEQ 107
|
90 100
....*....|....*....|...
gi 1039738675 1719 ERDELADEIANSASGKSALLDEK 1741
Cdd:COG0711 108 ERAKALAELRAEVADLAVAIAEK 130
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1125-1428 |
8.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1125 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAledetknheaqi 1204
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1205 qdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVlQQVKAESEHKRKKLDAQVQELHAkvsegdrl 1284
Cdd:COG1340 80 ---RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-QQTEVLSPEEEKELVEKIKELEK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1285 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1364
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKELRKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039738675 1365 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKllKDVEALSQRLEEKVLAYDKL 1428
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKKGEKL 282
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1187-1458 |
8.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1187 AELKKALEDETK--NHEAQIQDMRQRHATaleelsEQLEQAKRFKANLEKnKQGLETDNKELacevKVLQQVKAESEHKr 1264
Cdd:PHA02562 166 SEMDKLNKDKIRelNQQIQTLDMKIDHIQ------QQIKTYNKNIEEQRK-KNGENIARKQN----KYDELVEEAKTIK- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1265 kkldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAA---GLESQLQDTQELLQEETRQK 1341
Cdd:PHA02562 234 ----AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcpTCTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1342 LNLSSRIRQLEEEKNSLQEQQEEEEEARKNLekqvLALQSQLADTKkkvdddlGTIESLEEAkkklLKDVEALSQRLEEK 1421
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKL----LELKNKISTNK-------QSLITLVDK----AKKVKAAIEELQAE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039738675 1422 VLAYDK-LEKtknrLQQELDDLTVDLD------HQRQIVSNLEK 1458
Cdd:PHA02562 374 FVDNAEeLAK----LQDELDKIVKTKSelvkekYHRGIVTDLLK 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
951-1106 |
8.62e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 951 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFikEKKLMEDRIAECSSQLAEEEE 1030
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039738675 1031 KAKNLAKIRNKQEVMISDLEERLKKE-EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1106
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEElAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
1456-1648 |
8.76e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.84 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1456 LEKKQKKFDQLLAEEKGISARYAEERDRAEAeAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD-DVG 1534
Cdd:COG5414 202 IEEVEKKVDDLLEKDMKAESVSVVLKDEKEL-ARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGMSEEDlDVG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1535 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLrlevnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAE 1614
Cdd:COG5414 281 AAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEI-----------GEEKEEDDENEENERHTELLADELNELEKG 349
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039738675 1615 LEDERKQ--RALAVASKKKMEIDLKDLEAQIEAANK 1648
Cdd:COG5414 350 IEEKRRQmeSATNPILQKRFESQLNVLLKELELKRK 385
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
860-1067 |
8.98e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 860 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQ-QLLEEKNILAEQLQAETELFAE--AEEMRARlaakKQELEEilhd 936
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQrRLQQEQLERAEKMREELELEQQrrFEEIRLR----KQRLEE---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 937 lESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQnskfikeKKLM- 1014
Cdd:pfam15709 399 -ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAeKQRQKELEMQLAEEQ-------KRLMe 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039738675 1015 --EDRIAECSSQLAEEEEKAKNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1067
Cdd:pfam15709 471 maEEERLEYQRQKQEAEEKARLEAEERRQKE----EEAARLALEEAMKQAQEQAR 521
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1691-1940 |
9.12e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1691 KLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1770
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1771 KTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATisALEAKIGQLEEQLEqEAKERAAA 1850
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK--ELVEKIKELEKELE-KAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1851 NKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSRE 1930
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|
gi 1039738675 1931 VSTLKNRLRR 1940
Cdd:COG1340 239 LRELRKELKK 248
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1175-1386 |
9.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1175 QQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1254
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1255 QVKAESEHKRKKLDAQ-VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEL 1333
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039738675 1334 LQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADT 1386
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1391-1931 |
9.59e-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: 40.86 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1391 DDDLGTIESLEEAKKKLLKDVEALSQ--------------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL 1456
Cdd:pfam05483 67 DSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkqkenKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDL 146
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1457 EKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlMSSKDDVGKN 1536
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKI 224
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1537 VHELEKSKRAL---EQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKaQFERDLQTRDEQNEEkkrlLLKQVRELEA 1613
Cdd:pfam05483 225 QHLEEEYKKEIndkEKQVSLLLIQITEKENKMK---DLTFLLEESRDKAN-QLEEKTKLQDENLKE----LIEKKDHLTK 296
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1614 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE----SE 1689
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1690 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANsasgKSALLDEKRRLEaRIAQLEEELEeeQSNMELLNDRF 1769
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEKKQFE-KIAEELKGKE--QELIFLLQARE 449
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410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1770 RkttlQVDTLNTELAAERSAaqksdnaRQQLERQNKELKAKLqELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAA 1849
Cdd:pfam05483 450 K----EIHDLEIQLTAIKTS-------EEHYLKEVEDLKTEL-EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1850 ANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQ----LKRQLEEAEEEATRANASRRKLQRELDDATEANE 1925
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQkgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
....*.
gi 1039738675 1926 GLSREV 1931
Cdd:pfam05483 598 NLKKQI 603
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| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1215-1616 |
9.97e-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: 40.65 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1215 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1294
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1295 LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEK 1374
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR-------KEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1375 QVLALQSQLADTKKKVdddlgtiesleeakkkllkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1454
Cdd:pfam07888 193 EFQELRNSLAQRDTQV-------------------------LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1455 NLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKeTKALSLARALEEALEAKEEFERQNKQLRADMEdlmssKDDVG 1534
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL-TLQLADASLALREGRARWAQERETLQQSAEAD-----KDRIE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1535 KNVHELEKskraLEQQVEEMRTQLEELEDELQATEDAKL----RLEVNMQAMKAQFeRDLQTRDEQNEEKKRLLLKQVRE 1610
Cdd:pfam07888 322 KLSAELQR----LEERLQEERMEREKLEVELGREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQ 396
|
....*.
gi 1039738675 1611 LEAELE 1616
Cdd:pfam07888 397 LEQRLE 402
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| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
984-1188 |
9.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 984 VTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKaknLAKIRNKQEVMISDLEERLKKEEKTRQEL 1063
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1064 EKAKRKL--DGETTD-----------------------LQDQIAELQAQVDELKVQLTKKEEELQGALARGDDEtlhKNN 1118
Cdd:COG3883 89 GERARALyrSGGSVSyldvllgsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEAL---KAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039738675 1119 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1188
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
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