|
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 ... |
861-1941 |
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: 1474.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 861 TRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDL 940
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 941 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1020
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1021 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAK 1100
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1101 KEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1180
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1181 LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAK 1260
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1261 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE 1340
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1341 TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQK 1420
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1421 LEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALS 1500
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1501 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1580
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1581 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQL 1660
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1661 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAL 1740
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1741 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGS 1820
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1821 VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLE 1900
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 528481571 1901 EAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1941
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-784 |
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: 1435.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14920 231 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14920 311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14920 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKG 661
Cdd:cd14920 471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 742 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14920 631 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
102-784 |
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: 1317.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKE---------SGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYR-FLSNGNIPIPGQQDKDNFQ 340
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd01377 312 VTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH-GKFQKP 579
Cdd:cd01377 391 NHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKsKNFKKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 580 RQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmnETAFGAAYKTK 659
Cdd:cd01377 469 KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 660 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 739
Cdd:cd01377 538 GGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQ 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 528481571 740 RYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd01377 618 RYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-784 |
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: 1245.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14932 235 TMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14932 315 QKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14932 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGaAYKTKKG 661
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd14932 554 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 742 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14932 634 EILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-784 |
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: 1199.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14919 228 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14919 308 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14919 388 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKG 661
Cdd:cd14919 468 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd14919 548 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 742 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14919 628 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
102-784 |
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: 1185.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14921 231 TLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14921 311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14921 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKG 661
Cdd:cd14921 471 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd14921 551 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 742 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14921 631 EILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-784 |
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: 1181.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd15896 155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd15896 235 TMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd15896 315 QKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd15896 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNEtaFGAAYKTKKG 661
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 742 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
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 ... |
102-784 |
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: 1168.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKpRQ 581
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrIVGLDQVAgMNETAFGAayKTKKG 661
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 742 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
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 ... |
102-784 |
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: 1142.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQdKDNFQE 341
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAayKTKKG 661
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd14930 548 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 742 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14930 628 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
90-784 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1105.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 90 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 169
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 170 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkavklQGELERQLLQANPILESFGNAKTVKN 249
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------VGRLEEQILQSNPILEAFGNAKTVRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 250 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-I 328
Cdd:pfam00063 147 NNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 329 PIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRA 408
Cdd:pfam00063 227 TIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 409 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLC 488
Cdd:pfam00063 307 LCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 489 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQ 568
Cdd:pfam00063 387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 569 EQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQvagmN 648
Cdd:pfam00063 464 TFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAA----N 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 649 ETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 728
Cdd:pfam00063 539 ESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGF 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 729 PNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:pfam00063 619 PNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
83-796 |
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: 1008.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 83 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 162
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 163 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklQGELERQLLQANPILESFG 242
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------------VGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 243 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRF 322
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 323 LSNGN-IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENT-AAQKLCHLLGM 400
Cdd:smart00242 225 LNQGGcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 401 NVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQ 480
Cdd:smart00242 305 DPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 481 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDK 560
Cdd:smart00242 384 VNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 561 TFVDKLVQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivg 640
Cdd:smart00242 461 TFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 641 ldqvagmnetafGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEG 720
Cdd:smart00242 534 ------------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLEN 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 721 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEERD 796
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
39-1357 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 913.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 39 VWVPSERHGFEAASIREERGEEVLVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 113
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 114 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 193
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 194 VIQYLAHVASSHkgrkdhniPPESpkavklqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGAN 273
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI-------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 274 IETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQETMEAMHIMSFN 352
Cdd:COG5022 237 IETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 353 HEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADF 432
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 433 AVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 512
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 513 QREGIEWSFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVDKLVQ--EQGTHGKFQKPRQLKDKadFCI 590
Cdd:COG5022 475 VKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 591 IHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVgldqvagmnetafgaayktKKGMFRTVGQLY 670
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRF 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 671 KESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA-- 748
Cdd:COG5022 612 KESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKsw 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 749 --IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDIIIYFQSVCRGYLARKAFAKKQQQL 826
Cdd:COG5022 692 tgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRI 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 827 SALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVkerQVKVENELVEMERKHQQLLEEKNILA 906
Cdd:COG5022 772 KKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFSLKAEVLI 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 907 EQlqaetelFAEAEEMRARLVAKKQelEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeqldeeeAARQKLQLEK 986
Cdd:COG5022 849 QK-------FGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDVKSISS-------------LKLVNLELES 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 987 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEdrvgemTSQLaeEEEKAKNLGKVKNKQEMMMVDleerlKKEEKTRQEL 1066
Cdd:COG5022 907 EIIELKKSLSSDLIENLEFKTELIARLKKLLN------NIDL--EEGPSIEYVKLPELNKLHEVE-----SKLKETSEEY 973
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1067 EKAKRKLDAETTDLQDQIAELQAQIDElkiqLAKKEEELQAVlargdeevaqkNNALKQLRELQAQLAELQEDLE----- 1141
Cdd:COG5022 974 EDLLKKSTILVREGNKANSELKNFKKE----LAELSKQYGAL-----------QESTKQLKELPVEVAELQSASKiisse 1038
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1142 -SEKAARNKAEKLKRD-------LSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR-- 1211
Cdd:COG5022 1039 sTELSILKPLQKLKGLlllennqLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQfi 1118
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1212 ---QRHGTALEEISEQLEQA----KRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEV-MARFSE 1283
Cdd:COG5022 1119 vaqMIKLNLLQEISKFLSQLvntlEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKsKLSSSE 1198
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1284 GEKVKGELADRTHKIQTElDNVSCLLEDAEKKGIKLT------KDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEE 1357
Cdd:COG5022 1199 VNDLKNELIALFSKIFSG-WPRGDKLKKLISEGWVPTeystslKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKL 1277
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
102-784 |
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: 858.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-----------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL-----SNGNIPIPGQQD 335
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 336 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT--DQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 573 HGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdvdrivgldqvagmnetaf 652
Cdd:cd00124 467 HPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 653 gaayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:cd00124 519 -----------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRL 581
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 528481571 733 VFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd00124 582 PFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
102-784 |
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: 782.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFL----ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14927 236 MATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14927 316 YVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 579 PR---QLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdriVGLDQVAgmnETAFGAA 655
Cdd:cd14927 472 PRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTE---DPKSGVK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 656 YKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 734
Cdd:cd14927 546 EKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILY 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 528481571 735 QEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14927 626 ADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
103-784 |
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: 767.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14913 233 ATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKP 579
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 580 RQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqVAGMNETAFGAAYK 657
Cdd:cd14913 469 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADSGKKKVA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 658 TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 736
Cdd:cd14913 540 KKKGsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 737 FRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14913 620 FKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-784 |
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: 747.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippeSPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK----------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14909 311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKP 579
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 580 RQLK---DKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivGLDQVAGMNETAFGAAy 656
Cdd:cd14909 467 KPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAKGGRG- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 657 kTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 736
Cdd:cd14909 541 -KKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481571 737 FRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
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 ... |
102-784 |
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: 727.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG------------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHL-RSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKP 579
Cdd:cd14934 388 NHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 580 RQLKDK---ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqvagmnETAFGAAY 656
Cdd:cd14934 465 KGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 657 KTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 735
Cdd:cd14934 531 KQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYP 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 736 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14934 611 EFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
103-784 |
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: 718.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQ 340
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd01380 226 ETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd01380 306 IVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 500 FNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK--FQ 577
Cdd:cd01380 386 FNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 578 KPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvaelwkdvdrivgldqvagmnetafgaayk 657
Cdd:cd01380 462 KPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR------------------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 658 tKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 737
Cdd:cd01380 509 -KK----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEF 583
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 528481571 738 RQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd01380 584 FSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
103-784 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 706.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPKavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPG----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14917 153 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASIDDAEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14917 232 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 579 PRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqVAGMNETAFGAAY 656
Cdd:cd14917 468 PRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPIEKGKG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 657 KTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 735
Cdd:cd14917 539 KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 528481571 736 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14917 619 DFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
102-784 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 705.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LR-DLLLVSANpsDFHFCSCGAVAVESLDDAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 579 PRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAGmNETAFGAAY 656
Cdd:cd14929 462 PKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 657 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 736
Cdd:cd14929 534 RKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYAD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 737 FRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14929 614 FKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
104-784 |
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: 692.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 183
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 184 GAGKTENTKKVIQYLAHVASSHKGRKDhnippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 263
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKE--------ESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 264 DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQET 342
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 343 MEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQ 422
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 423 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 502
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 503 TMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPRQ 581
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 LKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldqVAGMNETAFGAAYKTK 659
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 660 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 739
Cdd:cd14918 543 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 528481571 740 RYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
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 ... |
103-784 |
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: 691.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPR 580
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 581 QLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnETAFGAAYK- 657
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--------ASAGGGAKKg 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 658 -TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 735
Cdd:cd14912 544 gKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 528481571 736 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14912 624 DFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
103-784 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 687.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnippespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN--------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14916 154 HFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL-DMLLVTNNpyDYAFVSQGEVSVASIDDSEEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14916 233 LATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14916 313 YVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14916 392 FNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 579 PRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldQVAGMNETAFGAAY 656
Cdd:cd14916 469 PRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 657 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 736
Cdd:cd14916 542 KKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 737 FRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14916 622 FRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
103-784 |
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: 686.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPR 580
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 581 QLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldqVAGMNETAFGAAYKT 658
Cdd:cd14910 472 PAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 659 KKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 737
Cdd:cd14910 544 KKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481571 738 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14910 624 KQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-784 |
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: 683.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14923 234 ATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKP 579
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 580 RQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdriVGLDQVAGMNETAFGaayK 657
Cdd:cd14923 470 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---K 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 658 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 737
Cdd:cd14923 544 KKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481571 738 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14923 624 KQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-784 |
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: 677.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYRF--LSNGNIPIPGQQDKDNFQ 340
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKP 579
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 580 RQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAGMNETAFGAAYK 657
Cdd:cd14915 471 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 658 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 737
Cdd:cd14915 544 KKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481571 738 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14915 624 KQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
103-784 |
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: 646.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNF 339
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK-LCHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd14883 223 DHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIRQINVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 498
Cdd:cd14883 303 NVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 499 LFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQK 578
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 579 PRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrIVGLDQVAGMNETAfGAAYKT 658
Cdd:cd14883 459 PDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 659 KKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 738
Cdd:cd14883 537 SKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFV 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 528481571 739 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14883 616 DRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
103-784 |
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: 640.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQE 341
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd01383 221 LKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd01383 301 VKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 502 HTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRq 581
Cdd:cd01383 381 RHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 582 lkDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdrivgldqVAGMNETAFGAAYKTKKG 661
Cdd:cd01383 457 --GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF------------ASKMLDASRKALPLTKAS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 662 MF----RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 737
Cdd:cd01383 522 GSdsqkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEF 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 528481571 738 RQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd01383 602 ARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
103-784 |
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: 637.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkaVKlqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQE 341
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVG---R 418
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 498
Cdd:cd01378 306 SVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 499 LFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVDKLVQEQGTHGKFQ 577
Cdd:cd01378 386 IFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 578 KPRQLKD--KADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmnetafgaa 655
Cdd:cd01378 463 CPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 656 yKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 735
Cdd:cd01378 525 -LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYE 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 736 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd01378 604 KFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
102-784 |
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: 612.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPPespkavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS-----------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNF 339
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSpRIKV 416
Cdd:cd01384 226 RATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 417 GRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEK 495
Cdd:cd01384 305 TPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 496 LQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 575
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 576 FQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmnetafgaa 655
Cdd:cd01384 461 FSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 656 YKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 734
Cdd:cd01384 521 EGTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPF 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 528481571 735 QEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 784
Cdd:cd01384 601 EEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
102-784 |
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: 607.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQ 340
Cdd:cd01381 142 HFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKK--ERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd01381 222 DIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd01381 302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 497 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 575
Cdd:cd01381 382 QQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 576 FQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkDVDRIVGLDqvagmnetafgAA 655
Cdd:cd01381 458 YLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TR 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 656 YKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 735
Cdd:cd01381 525 KKSP-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFE 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 736 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd01381 600 EFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-784 |
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: 570.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLegfnsyrflsngnipIPGQQDKDNFQ 340
Cdd:cd01382 143 IHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT-------DQASMPENTAAQKlchLLGMNVMEF-----TRA 408
Cdd:cd01382 208 RMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 409 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFQLNSFEQLC 488
Cdd:cd01382 285 MQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 489 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQ 568
Cdd:cd01382 363 INYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 569 EQGTHGKFQKPRQ--------LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVG 640
Cdd:cd01382 440 KHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 641 ldqvagmnetafGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEG 720
Cdd:cd01382 520 ------------DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481571 721 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
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 ... |
102-784 |
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: 567.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGfnSYRFLSNGN-IPIPGQQDKDNFQ 340
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVDDVADFE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCH---LLGMNVMEFTRAILSPRIKV- 416
Cdd:cd14872 220 EVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIk 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 417 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd14872 300 GCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 497 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKF 576
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 577 QKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgLDQvagmnetafgaay 656
Cdd:cd14872 457 VYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQ------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 657 KTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 736
Cdd:cd14872 520 KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 737 FRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
102-784 |
7.50e-177 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 552.84 E-value: 7.50e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 176
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 177 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFG 256
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 257 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDK 336
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 337 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKErntDQASMPEN-TAAQKLCH---LLGMNVMEFTRAILSP 412
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE---NDTTVLEDaTTLQSLKLaaeLLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 413 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVDKLVQE 569
Cdd:cd14890 397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 570 QGT-------------HGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdvd 636
Cdd:cd14890 475 FGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 637 rivgldqvagmnetafgaayKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 716
Cdd:cd14890 542 --------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSG 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 717 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14890 600 MMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
102-784 |
1.16e-173 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 544.35 E-value: 1.16e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnippesPKAVKLQGElerQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRFGKYLEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG-NIPIPGQQDKDNFQ 340
Cdd:cd01387 143 FFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ---ASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVG 417
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 418 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 497
Cdd:cd01387 302 RERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 498 QLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQ 577
Cdd:cd01387 381 YYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 578 KPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNetafgAAYK 657
Cdd:cd01387 458 KPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGK-----GRFV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 658 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 737
Cdd:cd01387 531 TMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVF 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481571 738 RQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 784
Cdd:cd01387 611 IDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
102-784 |
1.77e-168 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 530.12 E-value: 1.77e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkavklqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsdLLLEGFNSYRFL-SNGNIPIPGQQDKDNF 339
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASM--PENTAAQKLCHLLGMNVMEFTRAILSPRIKVG 417
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 418 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 497
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 498 QLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVqeqGTHGKFQ 577
Cdd:cd14903 380 QKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 578 K----PRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrIVGLDQVAGMNETAFG 653
Cdd:cd14903 453 DviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 654 AAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 733
Cdd:cd14903 528 RRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLL 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 528481571 734 FQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 784
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 ... |
102-784 |
9.34e-166 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 523.86 E-value: 9.34e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLahVASSHKGrkdHNippespkavklqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG------------SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNFQ 340
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKER-NTDQASMPENTAAQKL-CHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd01385 224 RLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFQLNSFEQLCINYTNE 494
Cdd:cd01385 304 ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 495 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHG 574
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 575 KFQKPrQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdriVGLDQVA----GMNET 650
Cdd:cd01385 460 YYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfrwAVLRA 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 651 AFGAAY--------------------------------KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 698
Cdd:cd01385 531 FFRAMAafreagrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEK 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 699 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQ 778
Cdd:cd01385 609 KPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGK 684
|
....*.
gi 528481571 779 SKIFFR 784
Cdd:cd01385 685 TKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
102-782 |
4.30e-162 |
|
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: 512.80 E-value: 4.30e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 173
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 174 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPPESpkavklqgeLERQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------VRDRVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 252 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIP 329
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 330 IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-KKERNTDQASMPENTAAQKLCHLLGMNVMEFTRA 408
Cdd:cd14901 231 RDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 409 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFQLNSFEQL 487
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 488 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFV 563
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 564 DKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivgldq 643
Cdd:cd14901 464 NKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 644 vagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 723
Cdd:cd14901 531 ---------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 724 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 782
Cdd:cd14901 590 SRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
103-784 |
5.01e-162 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 511.44 E-value: 5.01e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVAsshkgrkdhnippespKAVklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG----------------KAN--NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGagehLRSDLLLEGFNS-------YRFLSNGNIPIPGQQD 335
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKLpenkpprYLQNDGLTVQDIVNNS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 336 --KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENTAA-QKLCHLLGMNVMEFTRAI 409
Cdd:cd01379 220 gnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 410 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFQLNSFEQL 487
Cdd:cd01379 300 TSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 488 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVDKL 566
Cdd:cd01379 380 CINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 567 vqEQGTHGKFQKpRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivgldqvag 646
Cdd:cd01379 456 --HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ---------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 647 mnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 726
Cdd:cd01379 517 ------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQ 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 727 GFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 784
Cdd:cd01379 579 GFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
102-784 |
1.59e-161 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 510.88 E-value: 1.59e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELS----------LKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNF 339
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKkerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14873 231 REVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 498
Cdd:cd14873 308 EILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 499 LFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQK 578
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 579 PRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgldqvAGMNETAFGAAYKT 658
Cdd:cd14873 461 PRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKH 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 659 KKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 738
Cdd:cd14873 531 RR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFY 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 528481571 739 QRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14873 608 KRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
102-746 |
2.08e-161 |
|
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: 511.16 E-value: 2.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVT---------GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-- 329
Cdd:cd14888 145 LQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPis 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 330 ----------------------IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPE 387
Cdd:cd14888 225 idmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 388 NTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG 464
Cdd:cd14888 305 ASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 465 ASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGV 544
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 545 LALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQST 624
Cdd:cd14888 462 FCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 625 DKFVAELWKD-VDRIVGLdqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKL 703
Cdd:cd14888 540 NPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLF 604
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481571 704 EPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 746
Cdd:cd14888 605 DRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
102-784 |
5.10e-161 |
|
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: 509.69 E-value: 5.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 174
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSR 254
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 255 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQ 333
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 334 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQ----ASMPENTAAQKLCHLLGMNVMEFTRAI 409
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 410 LSPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIF 479
Cdd:cd14892 313 VTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 480 QLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KAT 558
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 559 DKTFVDKLVQEQ-GTHGKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdvdr 637
Cdd:cd14892 470 DKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 638 ivgldqvagmnetafgaayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 717
Cdd:cd14892 536 -------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGV 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 718 LEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 784
Cdd:cd14892 584 LEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-784 |
5.91e-158 |
|
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: 500.37 E-value: 5.91e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD------------------DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD----- 335
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseele 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 336 --KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd14897 223 yyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFQLNSFEQLCI 489
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 490 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQE 569
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 570 QGTHGKFQKPrqLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdvdrivgldqvagmne 649
Cdd:cd14897 460 CGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 650 tafgaayktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 729
Cdd:cd14897 522 ------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYP 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 730 NRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 784
Cdd:cd14897 584 IRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
103-744 |
3.56e-145 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 465.16 E-value: 3.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 168
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 169 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkDHNIPPESPKAVKLQGeLERQLLQANPILESFGNAKT 246
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------DNNLAASVSMGKSTSG-IAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 247 VKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhlrsdlllegfnsyrflsng 326
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 327 nipipGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPENTAAQKL------CHLLG 399
Cdd:cd14900 214 -----AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 400 MNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAG 475
Cdd:cd14900 289 VDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 476 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP 555
Cdd:cd14900 369 FEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 556 KATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDplndnvatLLHQSTdkfvaelwkdV 635
Cdd:cd14900 446 KGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------V 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 636 DrivgldqvagmnetafgaayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 715
Cdd:cd14900 508 D-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561
|
650 660
....*....|....*....|....*....
gi 528481571 716 GVLEGIRICRQGFPNRIVFQEFRQRYEIL 744
Cdd:cd14900 562 GVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-747 |
2.11e-142 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 458.73 E-value: 2.11e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 172
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 173 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAV-KLQGELERQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 252 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE----GFNSYRFLSNG 326
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 327 NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK-KERNTDQASMPENTAA-QKLCHLLGMNVME 404
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 405 FTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 477
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 478 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 555
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 556 KATDKTFVDKLVQEQGTHGKFQKPRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdv 635
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 636 driVGLDQVAGMNETAFGAAYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 715
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 528481571 716 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 747
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
104-784 |
9.58e-142 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 456.68 E-value: 9.58e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 179
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 180 TGESGAGKTENTKKVIQYLAHVAsshkgrkdhnippespkavKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 259
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-------------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 260 RINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN--GNIPIPgQQDKD 337
Cdd:cd14889 144 QLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREV-QYWKK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 338 NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSPRI 414
Cdd:cd14889 222 KYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKTLTCTVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 415 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd14889 300 FTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 573 HGKFQKPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWK-DVDRIVGLDQVAGM---N 648
Cdd:cd14889 457 NSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLpqaG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 649 ETAFGAAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 728
Cdd:cd14889 535 SDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGF 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 729 PNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 784
Cdd:cd14889 609 SWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
102-784 |
8.29e-139 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 447.95 E-value: 8.29e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 174
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 175 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKDHNIPPESPKAVKLqgELERQLLQANPILESFGNAKTVKNDNS 252
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 253 SRFGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPI 330
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGcVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 331 PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK----LCHLLGMNVMEFT 406
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEalatAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 407 RAILSPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFQL-NSF 484
Cdd:cd14891 314 KVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 485 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIDLIErpANPPGVLALLDEECWFPKATD 559
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIA--SKPNGILPLLDNEARNPNPSD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 560 KTFVDKLVQEQGTHGKFQKPRQlKDKAD-FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQStDKFvaelwkdvdri 638
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKF----------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 639 vgLDQVAGMNEtafgaayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 718
Cdd:cd14891 531 --SDQMQELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGIL 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 719 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14891 579 QTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
102-784 |
1.09e-135 |
|
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: 439.22 E-value: 1.09e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkavklqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------RQPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQDKDNFQ 340
Cdd:cd14896 143 HLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ--ASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 497
Cdd:cd14896 302 GRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 498 QLFNHTMFILEQEEYQREGIEWSFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQ 577
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 578 KPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGmnetafgaayk 657
Cdd:cd14896 459 KPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 658 tkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 737
Cdd:cd14896 526 -------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 528481571 738 RQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14896 599 LARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
102-784 |
5.51e-135 |
|
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: 437.45 E-value: 5.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkavklqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA---------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIPIPGQQDKDN 338
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 339 FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASmpenTAAQKLCHLLGMNVMEFTR--AILSPRIKV 416
Cdd:cd14904 223 FASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRI----SNGSQLSQVAKMLGLPTTRieEALCNRSVV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 417 GR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 495
Cdd:cd14904 299 TRnESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 496 LQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGT 572
Cdd:cd14904 379 LQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 573 HGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgldqvaGMNETAF 652
Cdd:cd14904 455 NESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKE 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 653 GAAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:cd14904 524 GKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRL 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 528481571 733 VFQEFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 784
Cdd:cd14904 603 TPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
102-746 |
1.22e-132 |
|
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: 433.16 E-value: 1.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 171
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 172 REDQSILCTGESGAGKTENTKKVIQYLAHVasshkGRKDHNIPPESPKAVKLQgeleRQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-----GRDQSSTEQEGSDAVEIG----KRILQTNPILESFGNAQTIRNDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 252 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN---GNI 328
Cdd:cd14902 152 SSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 329 PIPGQQDKDN--FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKE-RNTDQASMPENTAAQ--KLCHLLGMNVM 403
Cdd:cd14902 232 RKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 404 EFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAG 475
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 476 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFP 555
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 556 KATDKTFVDKLVQEQGTHGKfqkprqlkdkadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkDV 635
Cdd:cd14902 469 KGSNQALSTKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 636 DRIVGLDQVAGMNETAFGAAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 713
Cdd:cd14902 529 VVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMR 608
|
650 660 670
....*....|....*....|....*....|...
gi 528481571 714 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 746
Cdd:cd14902 609 SVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
102-784 |
1.45e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 431.64 E-value: 1.45e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 171
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 172 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPEspkavklQGELERQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-------KLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 252 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HLRSDLLLEGFNSYRFL 323
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 324 SNGNIPIPGQ-QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPE---NTAAQKLCHLLG 399
Cdd:cd14908 234 GQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 400 MNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFE 477
Cdd:cd14908 314 VDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 478 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-K 556
Cdd:cd14908 393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 557 ATDKTFVDKLV--------QEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLM-KNMDPLNdnvatllhqstdkf 627
Cdd:cd14908 470 GSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 628 vaelwkdvdrivgldqvagmnetafgaayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 707
Cdd:cd14908 536 -----------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKR 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 708 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMIRALELD 770
Cdd:cd14908 586 VTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSM 664
|
730
....*....|....*...
gi 528481571 771 PNL----YRIGQSKIFFR 784
Cdd:cd14908 665 KNIpedtMQLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
100-837 |
2.44e-127 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 421.75 E-value: 2.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 100 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 179 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkavklqgelERQLLQANPILESFGNAKTVKNDNSSRFGKF 258
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI--------------QNAIMAANPVLEAFGNAKTIRNNNSSRFGRF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 259 IRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDN 338
Cdd:PTZ00014 251 MQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 339 FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASM--PENTAA-QKLCHLLGMNVMEFTRAILSPR 413
Cdd:PTZ00014 331 FEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFQLNSFEQLCINYTN 493
Cdd:PTZ00014 411 TYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITN 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 494 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQEQGTH 573
Cdd:PTZ00014 490 EMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNN 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 574 GKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnetafg 653
Cdd:PTZ00014 567 PKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG------------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 654 aayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 733
Cdd:PTZ00014 633 ---KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 734 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFF-RTGV--LAHLEEERDLKITDIIIYFQSVC 810
Cdd:PTZ00014 708 FAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAAkeLTQIQREKLAAWEPLVSVLEALI 787
|
730 740
....*....|....*....|....*..
gi 528481571 811 RGYLARKAFAKKqqqlsaLKVLQRNCA 837
Cdd:PTZ00014 788 LKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-784 |
1.25e-126 |
|
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: 415.17 E-value: 1.25e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPEspkavKLQGelerqllqANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE-----KLNA--------ALTVLEAFGNVRTALNGNATRFSQLFSL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSyrflSNGNIPIPGQQDKD---- 337
Cdd:cd01386 144 DFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDkqka 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 338 --NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAI------ 409
Cdd:cd01386 220 aaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhls 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 410 ------LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGfeiFQLN- 482
Cdd:cd01386 300 ggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG---FQNPa 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 483 --------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERP---ANPP--------- 542
Cdd:cd01386 376 hsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrr 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 543 GVLALLDEECWFPKATDKTFVDKLVQEQG--THGKFQKPRQLKDKA-DFCIIHYAGR--VDYKADEWLMK-NMDPLNDNV 616
Cdd:cd01386 456 GLLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 617 ATLLHQSTDKFvaelwkdvdrivgldqvagmnetafgAAYKtKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRCIIPNH 696
Cdd:cd01386 536 TQLLQESQKET--------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQH 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 697 EkrAGKLEPH--------------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGK 757
Cdd:cd01386 585 N--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADER 662
|
730 740
....*....|....*....|....*..
gi 528481571 758 QACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd01386 663 KAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
103-745 |
4.67e-126 |
|
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: 413.96 E-value: 4.67e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 170
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 171 --DREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrKDHNIPPESPKAVKLQGElerQLLQANPILESFGNAKTVK 248
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESS------KHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 249 NDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNS--YR 321
Cdd:cd14895 146 NDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAqeFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 322 FLSNGNIPI--PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD---------------QAS 384
Cdd:cd14895 226 YISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 385 MPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK 461
Cdd:cd14895 306 PSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 462 ----------RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPC 531
Cdd:cd14895 386 falnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVC 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 532 IDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKAD--FCIIHYAGRVDYKADEWLMKNM 609
Cdd:cd14895 465 LEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 610 DPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGmfrtVGQLYKESLTKLMATLRNTNPNFV 689
Cdd:cd14895 541 DQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYI 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 690 RCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 745
Cdd:cd14895 617 RCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
102-782 |
1.94e-124 |
|
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: 407.45 E-value: 1.94e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIPpespKAVklqgelerqlLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRIQ----TAI----------MAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIK 415
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 416 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFQLNSFEQLCINYTNE 494
Cdd:cd14876 304 AGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 495 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQEQGTHG 574
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 575 KFqKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnetafga 654
Cdd:cd14876 459 KF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG-------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 655 ayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 734
Cdd:cd14876 524 --KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPF 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481571 735 QEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 782
Cdd:cd14876 600 EEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-746 |
4.69e-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: 392.68 E-value: 4.69e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 177
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 178 LCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGK 257
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 258 FIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIpgqqDKD 337
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 338 NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTA---AQKLCHLLGMNVMEFTRAILSPRI 414
Cdd:cd14880 227 CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 415 KVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd14880 307 RAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 573 HGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAf 652
Cdd:cd14880 464 GNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAP- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 653 gaayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:cd14880 543 ----------VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRV 612
|
650
....*....|....
gi 528481571 733 VFQEFRQRYEILTP 746
Cdd:cd14880 613 SHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-747 |
1.69e-117 |
|
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: 390.11 E-value: 1.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 179
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 180 TGESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFI 259
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSS-NQQQNNNNNNNNNS-------IEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 260 RINFDVTGYIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEG-FNSYRFL------------- 323
Cdd:cd14906 153 KIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 324 -SNGNIPIPGQQDKD-NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQAS--MPENTAA-QKLCHLL 398
Cdd:cd14906 233 sSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 399 GMNVMEFTRAILSPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQGAS 466
Cdd:cd14906 313 GYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 467 FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLA 546
Cdd:cd14906 393 FIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 547 LLDEECWFPKATDKTFVDKLVQE-QGTHGKFQkpRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTD 625
Cdd:cd14906 470 LLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 626 KFVAELWKdvdrivgldqvagMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEP 705
Cdd:cd14906 547 FLKKSLFQ-------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNN 612
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528481571 706 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 747
Cdd:cd14906 613 VHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
102-784 |
8.25e-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: 374.22 E-value: 8.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 176 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRF 255
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 256 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQ 334
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 335 DKDNFQETMEAMHIMsFNHEEILSMLKVVSAVLQFGNIVFKKERN--TDQASMPENTAA-QKLCHLLGMNVMEFTRAILS 411
Cdd:cd14886 223 DQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIIT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 412 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFQLNSFEQLC 488
Cdd:cd14886 302 KVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 489 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVdklvq 568
Cdd:cd14886 378 INYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFT----- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 569 eQGTHGKFQKPRQLKDKA---DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLdqva 645
Cdd:cd14886 450 -SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN---- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 646 gmnetafgaayktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 725
Cdd:cd14886 525 -------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIH 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528481571 726 QGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14886 590 RGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-784 |
2.96e-111 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 370.29 E-value: 2.96e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 178
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 179 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippeSPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKF 258
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSS---------NTSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 259 IRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDL-LLEGFNSYRFLSNGNI----PIPG 332
Cdd:cd14875 152 IKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 333 Q--QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAIL 410
Cdd:cd14875 232 KtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 411 sprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFQLNSFEQLCI 489
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 490 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQE 569
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 570 QGTHGK-FQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdrivgLDQVAGMN 648
Cdd:cd14875 465 WANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 649 ETAfgaayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 728
Cdd:cd14875 535 RRK------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGY 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 729 PNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 784
Cdd:cd14875 603 PVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
102-741 |
7.37e-107 |
|
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: 359.41 E-value: 7.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 170
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 171 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKND 250
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 251 NSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-----AGEHLRSDLLLEGFNSYRFLS 324
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 325 NG--NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-----KKERNT--DQASMPENTAA---- 391
Cdd:cd14899 240 QSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 392 -QKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT---------- 460
Cdd:cd14899 320 fTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 461 ----KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE 536
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 537 RpaNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLN 613
Cdd:cd14899 479 H--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 614 DNVATLLHQSTDKFVAELWK-DVDRIVGLDQVAGMNETAFGAAYKTKKGMFrTVGQLYKESLTKLMATLRNTNPNFVRCI 692
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 693 IPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 741
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
102-784 |
6.30e-96 |
|
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: 327.76 E-value: 6.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 173
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 174 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqgeLERQLLQANPILESFGNAKTVKNDNSS 253
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG--------------LEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 254 RFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFnsyrflsngnipiPG 332
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGD-------------PE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 333 QQDKDNFQETMEAMHIMSFNHEEIlsmLKVVSAVLQFGNIVFKKERNTDQASMPENTA--------AQKLCHLL------ 398
Cdd:cd14887 214 STDLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkcls 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 399 -GMNVMEFTRAILS--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 457
Cdd:cd14887 291 sGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 458 DRTKR-------------QGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREG--IEW 519
Cdd:cd14887 371 QRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 520 SFIDFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVDKLVQ--EQ 570
Cdd:cd14887 451 DCSAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKniIN 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 571 GTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLhQSTDKFVaelwkdvdRIVGLDQVAGMNet 650
Cdd:cd14887 531 SAKYKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGVR-- 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 651 afgaAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 730
Cdd:cd14887 600 ----AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPC 672
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 528481571 731 RIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 784
Cdd:cd14887 673 RLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
103-748 |
2.32e-95 |
|
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: 321.46 E-value: 2.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 182
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDvtGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLlegfNSYRFLSNGNIPIPGQQDKDNFQET 342
Cdd:cd14898 139 FD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 343 MEAMHIMSFNHEEILSMlkvvsAVLQFGNIVFKKERNTDQASmpeNTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQ 422
Cdd:cd14898 213 MKSLGIANFKSIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 423 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 502
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 503 TMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLvqeqgthGKFQKPRqL 582
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 583 KDKADFCII--HYAGRVDYKADEWLMKNMDplndnvatllhqstdkfvaelwkdvdrivgldqvaGMNETAFGAAYKTKK 660
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDE 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 661 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 740
Cdd:cd14898 475 GSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEER 554
|
....*...
gi 528481571 741 YEILTPNA 748
Cdd:cd14898 555 YRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
99-783 |
8.64e-95 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 321.81 E-value: 8.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 99 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 168
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 169 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKAVKLQGelerQLLQANPILESFGNAKTVK 248
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTKLSS----QISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 249 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN- 327
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGc 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 328 ---IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMpENTAA-QKLCHLLGMN 401
Cdd:cd14879 223 hplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 402 VMEFtRAILSPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGf 476
Cdd:cd14879 302 PEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPG- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 477 eiFQL------NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDE 550
Cdd:cd14879 376 --FQNrsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 551 EC-WFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD---FCIIHYAGRVDYKADEWLMKNMDPLndnvatllhqSTDk 626
Cdd:cd14879 451 QTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 627 FVAelwkdvdrivgldqvagmnetafgaayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 706
Cdd:cd14879 520 FVN--------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKR 566
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 707 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSKIFF 783
Cdd:cd14879 567 RVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
102-784 |
1.61e-90 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 309.82 E-value: 1.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 179 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKF 258
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT------------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 259 IRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG----NIPIPGQ 333
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 334 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd14878 223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFQLNSFEQLCIN 490
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 491 YTNEKLQQLFNHTMFILEQEEYQREGIewsfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATD 559
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 560 KTFVDKL---VQEQGTHGKFQKPRQ------LKDK-ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVA 629
Cdd:cd14878 450 PNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 630 ELwkdvdrivgldqvagmnetafgaaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 709
Cdd:cd14878 530 HL------------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVS 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 710 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKIFFR 784
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 ... |
102-784 |
4.20e-88 |
|
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: 302.32 E-value: 4.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAhvasshkgrkdhnippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL-------------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 342 TMEAMHIMSFnHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENT--AAQKLCHLLGMNVMEFTRAILSPRIKV 416
Cdd:cd14937 218 LMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 417 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 497 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGKF 576
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 577 QKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIvglDQVAGMNETAFGaay 656
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVS---ESLGRKNLITFK--- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 657 ktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQE 736
Cdd:cd14937 525 -------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDV 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481571 737 FRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 784
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 ... |
102-736 |
9.81e-80 |
|
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: 279.10 E-value: 9.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 173
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 174 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNippespkavklqgELERQLLQANPILESFGNAKTVKNDNSS 253
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT-------------ERIDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 254 RFGKFIRINFD---------VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHLRSDLLLEGFNSYRFL 323
Cdd:cd14884 144 RCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 324 SN----------GNIPIPG----------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerntdqa 383
Cdd:cd14884 224 NPdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 384 smpentaaqkLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ 463
Cdd:cd14884 297 ----------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 464 GA-----------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCI 532
Cdd:cd14884 367 DEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 533 DLIERpanppgVLALLDE-----ECWFPKATDKTFVD-------KLVQEQGTHGK-------FQKPRQLKDKADFCIIHY 593
Cdd:cd14884 446 IFIAK------IFRRLDDitklkNQGQKKTDDHFFRYllnnerqQQLEGKVSYGFvlnhdadGTAKKQNIKKNIFFIRHY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 594 AGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivgldqvagmnetafgAAYKTKKGMFRTVGQLYKES 673
Cdd:cd14884 520 AGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKE 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 674 LTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 736
Cdd:cd14884 577 LDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
103-771 |
7.34e-76 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 266.21 E-value: 7.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 176 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpkavklqgELERQLLQANPILESFGNAKTVKNDNSSRF 255
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET--------DAFKHLAAAFTVLRSLGSAKTATNSESSRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 256 GKFIRINFdVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFN--SYRFLSNGNIPIPGQ 333
Cdd:cd14881 133 GHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 334 QDKDNFQETMEAMHIMSFnheEILSMLKVVSAVLQFGNIVFkKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd14881 212 EDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFQLNSFE 485
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 486 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKTFVD 564
Cdd:cd14881 364 HLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 565 KLVQEQGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdvdrivgldqv 644
Cdd:cd14881 440 KIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 645 agmneTAFGaayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 724
Cdd:cd14881 499 -----CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLM 564
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 725 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 771
Cdd:cd14881 565 AGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
105-783 |
1.03e-71 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 256.82 E-value: 1.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 105 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 174
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSR 254
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPR------PDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 255 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---LRSDLLL-EGFNSYRFLSN----- 325
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadpla 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 326 GNIPIpgqqDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF------KKERN-------TDQASMPENTAAQ 392
Cdd:cd14893 237 TNFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 393 KL--CHLLGMNVMEF-----TRAILSpriKVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DR 459
Cdd:cd14893 313 ILlaAKLLEVEPVVLdnyfrTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 460 TKRQG----ASFIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWSFIDFGL 526
Cdd:cd14893 390 YEKSNivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 527 DLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD------------FCIIHYA 594
Cdd:cd14893 470 EQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 595 GRVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvaelwkdVDRIVGLDQVAGmNETAFGAAYKTKKG----MFRTVGQLY 670
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAA-ASSEKAAKQTEERGstssKFRKSASSA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 671 KESLT--------------KLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 736
Cdd:cd14893 619 RESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGH 698
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 528481571 737 FRQRYeiltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 783
Cdd:cd14893 699 FFRRY---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
103-784 |
5.10e-70 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 250.01 E-value: 5.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnippespkavklqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN-GNIPIPGQQDKDNF 339
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtdQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 420 YVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 500 FNHTMFILEQEEYQREGIEW-SFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGKF-Q 577
Cdd:cd14905 367 YLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 578 KPRQlkdkadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKF-------------VAELWKDVD-------- 636
Cdd:cd14905 440 KPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakks 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 637 --RIVGL---------DQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKL 703
Cdd:cd14905 514 plSIVKVllscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTF 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 704 EPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIF 782
Cdd:cd14905 594 DVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIF 671
|
..
gi 528481571 783 FR 784
Cdd:cd14905 672 LR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
102-749 |
1.42e-68 |
|
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: 244.78 E-value: 1.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 180
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 181 GESGAGKTENTKKVIQYLAHvasshkgrkdhniPPESPKAVKLQGELERqllqanpILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS-------------QPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 261 INFDvTGYIVGANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14874 131 LLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPE--NTAAQKLCHLLGMNVMEFTRAILSPRIKV 416
Cdd:cd14874 210 KHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 417 GrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 497 QQLFNHTMFILEQEEYQREGIEwsfIDF----GLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 573 HGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdvdrivgldqvagmNETAf 652
Cdd:cd14874 438 RSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------------SYSS- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 653 gaaykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:cd14874 502 -----NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKI 576
|
650
....*....|....*..
gi 528481571 733 VFQEFRQRYEILTPNAI 749
Cdd:cd14874 577 SKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
103-744 |
5.64e-63 |
|
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: 228.47 E-value: 5.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 183 SGAGKTENTKKVIQYLAHVASShkgrkdhnippespkavkLQGELERqLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDG------------------NRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHLRSDLLLEGFNsYRFL--SNGNIPIPGQQDKDN 338
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKLKYRRDD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 339 -------FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILS 411
Cdd:cd14882 222 pegnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 412 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFQLNSFEQ 486
Cdd:cd14882 300 YCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 487 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECwfPKATDKTFVDKL 566
Cdd:cd14882 377 LMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYIMDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 567 VQEQgtHGKFQKPrqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAG 646
Cdd:cd14882 452 IKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 647 MnetafgaayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 723
Cdd:cd14882 520 M---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKA 584
|
650 660
....*....|....*....|.
gi 528481571 724 CRQGFPNRIVFQEFRQRYEIL 744
Cdd:cd14882 585 RQKGFSYRIPFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
124-268 |
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 528481571 124 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 202
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 203 SSHKGRKDHNIppeSPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 268
Cdd:cd01363 81 FNGINKGETEG---WVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
103-782 |
5.02e-59 |
|
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: 218.17 E-value: 5.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 182 ESGAGKTENTKKVIQYLAHVA--SSHKGRKDHNIPPESPKAV---KLQGELERQLLQANPILESFGNAKTVKNDNSSRFG 256
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgSRRLPTNLNDQEEDNIHNEentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 257 KFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDK 336
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 337 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNI-----VFKKE---------------------RNTDQASMPENTA 390
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 391 AQKL-CHLLGMNVMEFTRAILSPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 467
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 468 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANppGVLAL 547
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 548 LDEECWFPKATDKT-FVDKLVQEQGTHGKF-QKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTD 625
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 626 KFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHEKRA- 700
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 701 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRIGQSK 780
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 528481571 781 IF 782
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1088-1947 |
6.60e-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: 146.35 E-value: 6.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1088 QAQIDELkiqLAKKEEELQAVLargdEEVA-------QKNNALKQLRELQAQLA-------ELQEDLESEKAARNKAEKL 1153
Cdd:TIGR02168 143 QGKISEI---IEAKPEERRAIF----EEAAgiskykeRRKETERKLERTRENLDrledilnELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1154 KrDLSEELEALKTELEdTLDTTAAQQELRSKREQEvaelkkaiddetrnheSQIQEMRQRHGTALEEISEQLEQAKRVKG 1233
Cdd:TIGR02168 216 K-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELEELTAELQELEEKLEELRLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1234 NLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1313
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1314 KKGIKLTKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEeknnlleqqeeeeesrknlekQLATLQAQLVETKKKL 1393
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET-------LRSKVAQLEL---------------------QIASLNNEIERLEARL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1394 EDDVGALEGLEEVKRKLQKDMEvtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQivsNLEKKQKKFDQMLAEE 1473
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAEREL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1474 KTISAR-YAEERDRAEAEAREKDTKALSMARA--------LDEALEAKEEFER-LNKQLRAEMEDLI-SSKDDVGKNVHE 1542
Cdd:TIGR02168 485 AQLQARlDSLERLQENLEGFSEGVKALLKNQSglsgilgvLSELISVDEGYEAaIEAALGGRLQAVVvENLNAAKKAIAF 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1543 LEKSK--------------RTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF---DRDLQARDEQNEEKKR 1605
Cdd:TIGR02168 565 LKQNElgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1606 ALV-----KQVREMEAELEDERKQRALAVAAK---KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1677
Cdd:TIGR02168 645 YRIvtldgDLVRPGGVITGGSAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1678 RTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQleee 1757
Cdd:TIGR02168 725 SR-------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---- 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1758 leeEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSkFKASIAALEAKIL 1837
Cdd:TIGR02168 794 ---LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1838 QLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS-RRKL 1916
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEY 949
|
890 900 910
....*....|....*....|....*....|....*...
gi 528481571 1917 QRELDDA-------TEASEGLSREVNTLKNRLRRGGPV 1947
Cdd:TIGR02168 950 SLTLEEAealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
874-1705 |
1.37e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 145.58 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 874 LIKVKERQVKVENELVEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARL-VAKKQELEEILHDLESRVEEEEERNQ 952
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 953 SLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEE 1032
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1033 EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG 1112
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1113 DEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEvael 1192
Cdd:TIGR02168 417 ERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAEREL---- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1193 kkaidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNK-ELTNEV---KSLQQAKSESEHKRK 1268
Cdd:TIGR02168 485 -----AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEAalgGRLQAVVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1269 K-LEAQLQEVMAR--FSEGEKVKG-ELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQE-ETRQ 1343
Cdd:TIGR02168 560 KaIAFLKQNELGRvtFLPLDSIKGtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAlELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1344 KLNLSSRIRQLEEEK-----------NNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1412
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1413 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERDRAEAEAR 1492
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1493 EKDTKALSMARALDEALEAKEEFERLNKQ---LRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ 1569
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1570 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEkKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEaa 1649
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSE-LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-- 939
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1650 nkardeaikqlRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1705
Cdd:TIGR02168 940 -----------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1051-1817 |
2.82e-33 |
|
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: 140.96 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1051 DLEERLKKEEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1130
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1131 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqELRSKREQEVAELKKAiDDETRNHESQIQEM 1210
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE----------ELKEELESLEAELEEL-EAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1211 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLqqakseSEHKRKKLEAQLQEVMARFSEGEKVKGE 1290
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI------EELLKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1291 LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLLEQQEEEEE 1370
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1371 S---RKNLEKQLAT-----LQAQLVETKKKLEDDVGALEGLEEVK-----------RKLQKDMEVTSQKLEEKAIAFDKL 1431
Cdd:TIGR02168 528 LisvDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1432 EKTKNRLQQELDDLmvdLDHQRqIVSNLE-----KKQKKFDQML--AEEKTISARYAEERdraeaEAREKDTKALSMARA 1504
Cdd:TIGR02168 608 VKFDPKLRKALSYL---LGGVL-VVDDLDnalelAKKLRPGYRIvtLDGDLVRPGGVITG-----GSAKTNSSILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1505 LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQA 1584
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1585 MKAQFDRDLQARDEQNEEKKRAlvkqvremEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ 1664
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEA--------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1665 AQMKDYQRELEEARTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1744
Cdd:TIGR02168 831 RRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1745 RRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSA--------AQKSENARQQLERQNKDLKSKLQE 1816
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 528481571 1817 L 1817
Cdd:TIGR02168 984 L 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1014-1753 |
3.32e-31 |
|
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: 134.42 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1014 KKLLEDRVGemTSQLAEEEEKAKN-LGKVKNKQEMMMVDLEERLKKEEKTRQELEKA-------KRKLDAETTDLQDQIA 1085
Cdd:TIGR02169 156 RKIIDEIAG--VAEFDRKKEKALEeLEEVEENIERLDLIIDEKRQQLERLRREREKAeryqallKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1086 ELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnkaekLKRDLsEELEALK 1165
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKL----TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-----VKEKI-GELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1166 TELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESD 1245
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1246 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMarfSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvss 1325
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1326 lESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1405
Cdd:TIGR02169 454 -EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1406 VKRKLQKDME-----------VTSQKLEEKAIAFDKLEKTK-------NRLQQELDDL--------------MVDLDHQR 1453
Cdd:TIGR02169 533 VGERYATAIEvaagnrlnnvvVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1454 Q-----------IVSNLEKKQKKFDQM--------LAE-----------EKTISARYAEERDRAEAEAREKDtkalSMAR 1503
Cdd:TIGR02169 613 EpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1504 ALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1583
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1584 AMKAQFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKL 1663
Cdd:TIGR02169 769 ELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1664 QAQMKDYQRELEEARTSRDEIFTQSKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1736
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810
....*....|....*..
gi 528481571 1737 KAALLDEKRRLEARIAQ 1753
Cdd:TIGR02169 926 LEALEEELSEIEDPKGE 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
990-1871 |
3.44e-31 |
|
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: 134.42 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 990 EAKIKKMEEDIllleDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKtrQELEKA 1069
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1070 KRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLRELQAQLAELQEDLESEKAARN 1148
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1149 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaidDETRNHESQIQEMRQRHGTALEEIS---EQL 1225
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1226 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1305
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1306 SCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLLEQQEEEEESRknlekq 1378
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNR------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1379 latLQAQLVEtkkkleDDVGALEGLEEVKRK-----------LQKDMEVTSQKLEEKA--------IAFDklEKTKNRLQ 1439
Cdd:TIGR02169 549 ---LNNVVVE------DDAVAKEAIELLKRRkagratflplnKMRDERRDLSILSEDGvigfavdlVEFD--PKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1440 QELDDLMV--DLDHQRQIVSN----------LEKKQKKFDQMLAEEKTISaRYAEERDRAEAEAREKDtkalSMARALDE 1507
Cdd:TIGR02169 618 YVFGDTLVveDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1508 ALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1587
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1588 QFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQM 1667
Cdd:TIGR02169 773 DLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1668 KDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1747
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1748 EARIAQLEEELEEEQSNMELLNDrFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfka 1827
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE--------- 999
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 528481571 1828 siaaleakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQV 1871
Cdd:TIGR02169 1000 --------------------EERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1636 |
2.19e-29 |
|
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: 128.25 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 842 LRHWQWWRLftkvkpLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEE 921
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 922 MRARLVAKKQELEEILHDLESrveEEEERNQSLQNEKKKmqshiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDIL 1001
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLER---QLEELEAQLEELESK------------------LDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1002 LLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLq 1081
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1082 dQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEEL 1161
Cdd:TIGR02168 434 -ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1162 EAlKTELEDTLDTTAAQQELRSKREQEV-AELKKAIDD-ETRNHESQIQ----------------EMRQRHGTALEeiSE 1223
Cdd:TIGR02168 513 KN-QSGLSGILGVLSELISVDEGYEAAIeAALGGRLQAvVVENLNAAKKaiaflkqnelgrvtflPLDSIKGTEIQ--GN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1224 QLEQAKRVKGNLEKNKQTLESDNK---------ELTNEVKSLQQAksesEHKRKKLEAQLQEVMA---RFSEGEKVKGEL 1291
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNA----LELAKKLRPGYRIVTLdgdLVRPGGVITGGS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1292 ADRTHKI---QTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1368
Cdd:TIGR02168 666 AKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1369 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSqkleekaIAFDKLEKTKNRLQQELDDLMVD 1448
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-------EELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1449 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1528
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1529 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVnMQAMKAQFDRDLQARDEQNEEK 1603
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRL 977
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 528481571 1604 KRAL----------VKQVREMEAELEDERKQRALAVAAKKKLE 1636
Cdd:TIGR02168 978 ENKIkelgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
979-1753 |
4.78e-28 |
|
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: 124.02 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 979 RQKLQLEKVTAEA----KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEE 1054
Cdd:TIGR02169 200 LERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1055 RLKKEEKTRQ-ELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG---DEEVAQKNNALKQL---- 1126
Cdd:TIGR02169 280 KIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelEREIEEERKRRDKLteey 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1127 RELQAQLAELQEDLES-EKAARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhES 1205
Cdd:TIGR02169 360 AELKEELEDLRAELEEvDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1206 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF---- 1281
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRavee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1282 ---SEGEKVKGELAD-----RTHKIQTE------LDNVSCLLEDAEKKGIKLTKDVsslesQLQDTQELLQEETRQKLNL 1347
Cdd:TIGR02169 515 vlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRR-----KAGRATFLPLNKMRDERRD 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1348 SSRIR------------QLEEEKNNLLEQQEEEEESRKNLEKQLATL-QAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1414
Cdd:TIGR02169 590 LSILSedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1415 EVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAE 1490
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1491 AREKDTKALSMARaLDEALEAKEefERLNKqLRAEMEDLisSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1570
Cdd:TIGR02169 750 EQEIENVKSELKE-LEARIEELE--EDLHK-LEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1571 TEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAAN 1650
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1651 KARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKE------NEKKLKSLEAEILQLQEDLASSERARRHAEQERD 1724
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
810 820
....*....|....*....|....*....
gi 528481571 1725 ELADEISNSASGKAALLDEKRRLEARIAQ 1753
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
231-725 |
1.49e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 118.69 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 231 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------KDERTFHVFYQ 299
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 300 LLAGAGEH-----LRSDLLLEGFN--SYRFLSNGNIPIPG--------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVS 364
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 365 AVLQFGNIVFKKERNTDQASMPEN---TAAQKLCHLLGMNVMEFTRAIL---SPRIKVGRDYVQKAQTKEQADFAVEALA 438
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLmtkSVSLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 439 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQlfnh 502
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 503 tmfileqEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVDKLVQEQGT 572
Cdd:cd14894 565 -------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 573 HGKfQKPRQLKDKA----------DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgLD 642
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ---LG 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 643 QVAGMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 722
Cdd:cd14894 714 WSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQME 792
|
...
gi 528481571 723 ICR 725
Cdd:cd14894 793 ICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1375-1947 |
5.44e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.96 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1375 LEKQLATLQAQ---------LVETKKKLEDDVGAL--EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELD 1443
Cdd:COG1196 198 LERQLEPLERQaekaeryreLKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1444 DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1523
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1524 AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfDRDLQARDEQNEEK 1603
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1604 KRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE 1683
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1684 IftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE-----LADEISNSASGKAALLDEKRRLEARIAQLEEEL 1758
Cdd:COG1196 517 A--GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1759 EEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKilq 1838
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1839 leEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQR 1918
Cdd:COG1196 672 --AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580 590
....*....|....*....|....*....|...
gi 528481571 1919 ELDDATEAS----EGLSREVNTLKNRLRRGGPV 1947
Cdd:COG1196 750 EEALEELPEppdlEELERELERLEREIEALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1557 |
2.47e-25 |
|
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: 115.15 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 859 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 938
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 939 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1018
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1019 DRVGEMTSQLAEEEEKAKNLGKVKNKQEM--------MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI---AEL 1087
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEGY 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1088 QAQIDelkiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE----DLESEKAARNKAEKLKRDLSEELEA 1163
Cdd:TIGR02168 536 EAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVK 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1164 LKTELEDTL-----------DTTAAQQELRSKREQEVAELKK--------AIDDETRNHESQIQEMRQRhgtaLEEISEQ 1224
Cdd:TIGR02168 610 FDPKLRKALsyllggvlvvdDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRRE----IEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1225 LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDN 1304
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1305 VSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQA 1384
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1385 QLVETKKKLEDDVGALEGLEEVKRKLQKD-------MEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1457
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1458 NLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1536
Cdd:TIGR02168 926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFL 1005
|
730 740
....*....|....*....|.
gi 528481571 1537 GKNVHELEKSKRTLEQQVEEM 1557
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEI 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1125-1872 |
1.43e-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: 112.52 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1125 QLRELQAQLAELQEDLESEKAARNKAEKlkrDLSEELEALKTELEDTLDT----TAAQQELRSKREQEVAELKKA---ID 1197
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVI---DLQTKLQEMQMERDAMADIrrreSQSQEDLRNQLQNTVHELEAAkclKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1198 DETRNHESQIQEMRQ---RHGTALEEISEQLEQAKRVKGnleknKQTLESDNKElTNEVKSLQQAKSESehkRKKLEAQL 1274
Cdd:pfam15921 163 DMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASG-----KKIYEHDSMS-TMHFRSLGSAISKI---LRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1275 QEVMAR-FSEGEKVKGELADRTHKI----QTELDNVSCLLEDAEKKGIKLTKDVSSLESQ---LQDTQELLQEETRQKLn 1346
Cdd:pfam15921 234 SYLKGRiFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1347 lSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLVETKKKLEDDVgalegleevkRKLQKDMEVTSQKLEEKAI 1426
Cdd:pfam15921 313 -SMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI----------EELEKQLVLANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1427 AFDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKTISARYAEERDR-AEAEAREKDTKAL---- 1499
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMksec 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1500 --SMARALdEALEAKEEFERLNKQLRAEMEdliSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQAT--E 1572
Cdd:pfam15921 443 qgQMERQM-AAIQGKNESLEKVSSLTAQLE---STKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1573 DAKLRLEVNMQAMKAQFDRdlqardeqNEEKkralvkQVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIE-AANK 1651
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLK--------NEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1652 ARDEAIKQLRK--LQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1729
Cdd:pfam15921 582 GRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1730 ISNSASGKAALLDEKRRLEARIaqleeelEEEQSNMELLNDRFRkttMQVDTLNTELAGERSAAQKSENA---------- 1799
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNF-------RNKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSMEGSdghamkvamg 731
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1800 -RQQLER---QNKDLKSKLQELEGSVK--SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1872
Cdd:pfam15921 732 mQKQITAkrgQIDALQSKIQFLEEAMTnaNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
932-1694 |
2.04e-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: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 932 ELEEILHDLEsRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQ--------LEKVTAEAKIKKMEEDILLL 1003
Cdd:TIGR02169 171 KKEKALEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1004 EDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1083
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1084 IAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELqedlesEKAARNKAEKLKrDLSEELEA 1163
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------DKEFAETRDELK-DYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1164 LKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLE 1243
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1244 SDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF-------SEGEKVKGELAD-----RTHKIQTE------LDNV 1305
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1306 SCLLEDAEKKGIKLTKDVS------------------------------------------------------------- 1324
Cdd:TIGR02169 553 VVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaa 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1325 ----------SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1394
Cdd:TIGR02169 633 rrlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1395 DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1474
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1475 TISARyaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQV 1554
Cdd:TIGR02169 793 IPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1555 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDR------DLQARDEQNEEKKRALVKQVREMEAELEdERKQRALA 1628
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqieKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEE 949
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1629 VAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEI--FTQSKENEKK 1694
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIleRIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
920-1550 |
2.13e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 920 EEMRARL--------VAKK-QELEEILHDLESRVeeeeernqsLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE 990
Cdd:COG1196 196 GELERQLeplerqaeKAERyRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 991 AKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKAK 1070
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1071 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKA 1150
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1151 EKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR 1230
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1231 VKGNLEKNKQTLESDNKELTNEVkslQQAKSESEHKRKKLEAQL---------QEVMARFSEGEKVKGELADRTHKIQTE 1301
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGL---AGAVAVLIGVEAAYEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1302 L------------DNVSCLLEDAEKKGIK-LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1368
Cdd:COG1196 577 LpldkiraraalaAALARGAIGAAVDLVAsDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1369 EESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1448
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEE-------LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1449 LDHQRQIVSNLEkkqkkFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlSMAR-------ALDEALEAKEEFERLNKQ 1521
Cdd:COG1196 730 LEAEREELLEEL-----LEEEELLEEEALEELPEPPDLEELERELERLER-EIEAlgpvnllAIEEYEELEERYDFLSEQ 803
|
650 660
....*....|....*....|....*....
gi 528481571 1522 LraemEDLISSKDDVGKNVHELEKSKRTL 1550
Cdd:COG1196 804 R----EDLEEARETLEEAIEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1334-1899 |
3.02e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1334 QELLQEETRQKLNLSS-RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1412
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1413 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1492
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1493 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1572
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1573 DAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAlvKQVREMEAELEDERKQRALAVAAKKKLEM---------DLKDVE 1643
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavaVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1644 AQIEAANKARDEAIKQ--LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQ 1721
Cdd:COG1196 534 AAYEAALEAALAAALQniVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1722 ERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEeqsnMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQ 1801
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE----GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1802 QLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQY 1881
Cdd:COG1196 690 EEELELEEALLAEEEEE-----------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 528481571 1882 KEQMEKANSRMKQLKRQL 1899
Cdd:COG1196 759 PPDLEELERELERLEREI 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
979-1568 |
3.51e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 107.84 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 979 RQKLQLEKV-TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1057
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1058 KEEKTRQELEKAKRkldaETTDLQDQIAELQAQIDELKIQLAKKEEELqavlargdEEVAQKNNALKQLRELQAQLAELQ 1137
Cdd:PRK03918 232 ELEELKEEIEELEK----ELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1138 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ---EVAELKKAID--DETRNHESQIQEMRQ 1212
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1213 RH-GTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE---------------SEHKRKKLeaqLQE 1276
Cdd:PRK03918 380 RLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKEL---LEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1277 VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK--KGIKLTKDVSSLESQLQ--DTQELLQ-----EETRQKLN- 1346
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKkyNLEELEKkaeeyEKLKEKLIk 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1347 LSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAI 1426
Cdd:PRK03918 537 LKGEIKSLKKE-----------LEKLEELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1427 AFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErdraeaEAREKDTKALSMARALD 1506
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELA 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1507 EALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1568
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1624 |
2.46e-22 |
|
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: 105.54 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 864 EEEMQAKDEELIKVKERQVKVE-------NELVEMERKHQQLLEEKNILAEQLQAE-TELFAEAEEMRARLVAKKQELEE 935
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 936 ILHDLESRVEEEEERNQSLqNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEakIKKMEEDILLLEDQNSKFLKEKK 1015
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1016 LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK 1095
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1096 IQLAKKEEELQavlaRGDEEVAQKNNALKQLRELQAQLAELQED-----------LESEKAARNKAEKLKRDLSEELEAL 1164
Cdd:TIGR02169 406 RELDRLQEELQ----RLSEELADLNAAIAGIEAKINELEEEKEDkaleikkqewkLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1165 KTELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE----------------EIS 1222
Cdd:TIGR02169 482 EKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1223 EQLEQAKRVKG-------------------------------------------------------NLEKNKQ------- 1240
Cdd:TIGR02169 562 EAIELLKRRKAgratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvveDIEAARRlmgkyrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1241 -TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1319
Cdd:TIGR02169 642 vTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1320 TKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDD--- 1396
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrip 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1397 --VGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1474
Cdd:TIGR02169 795 eiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1475 TISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTlEQQV 1554
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSL 953
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1555 EEMRTQLEELEDELQATEDaklrleVNMQAMKaQFDRDLQARDEQnEEKKRALV---KQVREMEAELEDERKQ 1624
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEVLKRLDEL-KEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
820-1462 |
1.30e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 820 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRLftkvkpllQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL 898
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 899 LEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshIQDLEEQLDEEEAA 978
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 979 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1058
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1059 EEKTRQELEKAKRKLDAEttdlqdqIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE 1138
Cdd:COG1196 433 LEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1139 DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAL 1218
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1219 EEISEQLEQAKRVKGNLEKNKQTLESDNK----ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADR 1294
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARyyvlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1295 THKIQTEldnvscLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1374
Cdd:COG1196 666 SRRELLA------ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1375 LEKQLATLQAQLVETKKKLEDDVGALEG-LEEVKRKLQK----DMEVtsqkLEEkaiaFDKLEKTKNRLQQELDDLMVDL 1449
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELEReLERLEREIEAlgpvNLLA----IEE----YEELEERYDFLSEQREDLEEAR 811
|
650
....*....|...
gi 528481571 1450 DHQRQIVSNLEKK 1462
Cdd:COG1196 812 ETLEEAIEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1207-1818 |
3.83e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1207 IQEMRQRHGTaLEEISEQLEQAKRVKGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGE 1285
Cdd:COG1196 195 LGELERQLEP-LERQAEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1286 KVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQD-TQELLQEEtrqklnlsSRIRQLEEEKNNLLEQ 1364
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEElEEELAELE--------EELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1365 QEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1444
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1445 LMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalsmARALDEALEAKEEFERLNKQLRA 1524
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1525 EMEDLISSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmqamkaqfDRDLQARDEQNEEKK 1604
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1605 RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARTSRDEI 1684
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1685 FTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSN 1764
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1765 MELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1818
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1143-1701 |
5.60e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 100.52 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1143 EKAARNKAEKLKrdlseELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID---DETRNHESQIQEMRQRHGTaLE 1219
Cdd:PRK03918 161 ENAYKNLGEVIK-----EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisSELPELREELEKLEKEVKE-LE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1220 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQ 1299
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1300 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLLEQQ------------ 1365
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekel 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1366 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdmEVTSQKLEEkaiafDKLEKTKNRLQQELDDL 1445
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE-----EHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1446 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRA- 1524
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSl 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1525 -----EMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR-TQLEELEDELQATE----------DAKLRLEVNMQAMKAQ 1588
Cdd:PRK03918 545 kkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1589 FDRDLQARDEQNEEKKRA--LVKQVREMEAELEDERKQRAlaVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1666
Cdd:PRK03918 625 EEELDKAFEELAETEKRLeeLRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
570 580 590
....*....|....*....|....*....|....*...
gi 528481571 1667 ---MKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAE 1701
Cdd:PRK03918 703 leeREKAKKELEKLEKALERV-EELREKVKKYKALLKE 739
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1012-1886 |
8.70e-21 |
|
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: 100.43 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1012 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQE--------------LEKAKRKLDAET 1077
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqlkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1078 TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDL 1157
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1158 SEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHgtaLEEISEQLEQAKRVKGNLEK 1237
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1238 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQlqevMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI 1317
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL----KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1318 KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDV 1397
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1398 GALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD--------------HQRQIVSNLEKKQ 1463
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIavleidpilnlaqlDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1464 KKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHEL 1543
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1544 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERK 1623
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1624 QRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQaqmKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1703
Cdd:pfam02463 782 KTEKLKVEEEKEE-KLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1704 QLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1783
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1784 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1863
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
890 900
....*....|....*....|...
gi 528481571 1864 LKEVFMQVEDERRHADQYKEQME 1886
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYL 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
885-1256 |
5.58e-20 |
|
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: 97.82 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 885 ENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSH 964
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 965 IQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1044
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1045 QEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK 1124
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1125 QLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR----SKREQEVAELKKAIDDET 1200
Cdd:TIGR02168 909 KRSELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1201 RNHESQIQEmrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSL 1256
Cdd:TIGR02168 986 PVNLAAIEE--------YEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1012-1734 |
6.11e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.90 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1012 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQElEKAKRKLDAETTDLQDQIAELQAQI 1091
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA-EDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1092 DELKIQLAKKEEEL-QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnKAEKLKRDLSE---------EL 1161
Cdd:PTZ00121 1174 DAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEakkaeeernNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1162 EALKTELEDTLDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQT 1241
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1242 LESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA--RFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1319
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1320 TKdvSSLESQLQDTQELLQEETRQKLNLSSRI---RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDd 1396
Cdd:PTZ00121 1411 KK--AAAAKKKADEAKKKAEEKKKADEAKKKAeeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE- 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1397 vgALEGLEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQI--VSNLEKKQKKFDQMLAEEk 1474
Cdd:PTZ00121 1488 --AKKKAEEAKKK--------ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEE- 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1475 tisARYAEERDRAEAEAREKDTKALSMARAlDEALEAKEEfeRLNKQLRAEMEDLISSKDDVGKnvHELEKSKRTLEQQV 1554
Cdd:PTZ00121 1557 ---LKKAEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1555 EEMRTQLEELEDELQatEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAlaVAAKKK 1634
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEA--EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1635 LEMDLKDVEA--QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE---IFTQSKENEKKLKSLEAEILQLQEDL 1709
Cdd:PTZ00121 1705 EELKKKEAEEkkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
730 740
....*....|....*....|....*
gi 528481571 1710 ASSERARRHAEQERdELADEISNSA 1734
Cdd:PTZ00121 1785 LDEEDEKRRMEVDK-KIKDIFDNFA 1808
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1012-1596 |
1.09e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 96.26 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1012 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKakrkLDAETTDLQDQIAE----- 1086
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1087 --LQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLE----SEKAARNKAEKLKRD---- 1156
Cdd:PRK02224 275 eeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddl 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1157 ------LSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIddetrnhesqiqemrqrhgtalEEISEQLEQAKR 1230
Cdd:PRK02224 355 eeraeeLREEAAELESELEEA-------REAVEDRREEIEELEEEI----------------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1231 VKGNLEKNKQTLESDNKELTNEVKSlqqaksesehkrkkLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLE 1310
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAE--------------LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1311 DAEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETK 1390
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEER--------------REDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1391 KKLE---DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFD-KLEKTKNRLQQ--ELDDLMVDLDHQRQIVSNLEKKQK 1464
Cdd:PRK02224 537 ERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESleRIRTLLAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1465 KFDQMLAEEKTisaRYAEERDRAEAEAREKDtkalsmARALDEALEAKEEFERLNKQLRAEMEDLISSKDDvgknvheLE 1544
Cdd:PRK02224 617 ALAELNDERRE---RLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQ 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1545 KSKRTLEQQVEEmrtqLEELEDELQATEDAKLRLEV------NMQAMKAQFDRDLQAR 1596
Cdd:PRK02224 681 AEIGAVENELEE----LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
882-1470 |
2.85e-19 |
|
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: 94.70 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 882 VKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKM 961
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 962 QSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1037
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1038 LGKVKNKQEMMMVDLEERLKKEEKTRqELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVA 1117
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1118 QKNNALKQLRELQAQLAELQEDL-----ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL 1192
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1193 KKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA 1272
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1273 QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIR 1352
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1353 QLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE--DDVGALEGLEEVKRKLQKDMEVTSQ-------KLEE 1423
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQtqkslkkKQEE 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 528481571 1424 KAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1470
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1219-1930 |
2.89e-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: 95.13 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1219 EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEH----KRKKLEAQLQEVMARFSEGEKVKGELADR 1294
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1295 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKL-NLSSRIRQLEEEKNNLLEQQEEEEESRK 1373
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1374 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQR 1453
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1454 QIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK 1533
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1534 DDVGKNVHELEKSKRTLEQQVEEMRTQLEEL--------------------------------------EDELQATEDAK 1575
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1576 LRLEVN-----------MQAMKA------------------QFDRDLQA------RDE---QNEEKKRALVKQVR--EME 1615
Cdd:TIGR02169 566 LLKRRKagratflplnkMRDERRdlsilsedgvigfavdlvEFDPKYEPafkyvfGDTlvvEDIEAARRLMGKYRmvTLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1616 AELEDE--------RKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1687
Cdd:TIGR02169 646 GELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1688 SKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQsnMEL 1767
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1768 LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSV------KSKFKASIAALEAKILQLEE 1841
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1842 QLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRqLEEAEEEATRANASRRKLQRELD 1921
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKGEDEEIPEEELSLEDVQAELQ 961
|
....*....
gi 528481571 1922 DATEASEGL 1930
Cdd:TIGR02169 962 RVEEEIRAL 970
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1132-1751 |
3.38e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1132 QLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqelrskrEQEVAELKKAIDDetrnHESQIQEMR 1211
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIE----------------EKEEKDLHERLNG----LESELAELD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1212 qrhgTALEEISEQLEQAKRVKGN----LEKNKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKV 1287
Cdd:PRK02224 220 ----EEIERYEEQREQARETRDEadevLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1288 KGELADRTHKIQTELDNVSCLLEDaekkgikLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqee 1367
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA--------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1368 eeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMV 1447
Cdd:PRK02224 359 -----EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1448 DLdhqrqivSNLEKKQKKFDQMLAEEKTISAryaeerdraeaearEKDTKALSMARALDEALEAKEEferlnkqLRAEME 1527
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKCPEC--------------GQPVEGSPHVETIEEDRERVEE-------LEAELE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1528 DLISSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqfdrDLQARDEQNEEKKRAL 1607
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIA----------------------ERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1608 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1687
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1688 SKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKR-RLEARI 1751
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEI 683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
860-1747 |
1.28e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.11 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 860 VTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlVAKKQELEEILHD 939
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 940 LESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1019
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1020 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLdaettdLQDQIAELQAQiDELKIQLA 1099
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------EKLQEKLEQLE-EELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1100 KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTtaaqQ 1179
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1180 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR---VKGNLEKNKQTLESDNKELTNEVKSL 1256
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglkVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1257 QQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ--TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1334
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKlrLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1335 ELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1414
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1415 EVTSQKLEEKAIAfdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREK 1494
Cdd:pfam02463 697 RQLEIKKKEQREK--EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1495 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDA 1574
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1575 KLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARD 1654
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1655 EAIKQLRKLQAQMKDYQRELEEartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSA 1734
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKE---------EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 528481571 1735 SGKAALLDEKRRL 1747
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
866-1557 |
2.93e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 866 EMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVE 945
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 946 EEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEdillledqNSKFLKEKKLLEDRVGEM 1024
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEE--------KKKADEAKKAEEKKKADE 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1025 TSQLAEEEEKAKNLGK----VKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAettdlqdqiAELQAQIDELKIQLAK 1100
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---------AEEKAEAAEKKKEEAK 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1101 KEEElqaVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRdlseeLEALKTELEDTLDTTAA 1177
Cdd:PTZ00121 1378 KKAD---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEA 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1178 QQELRSKREQEvaELKKAIDDETRNHESQIQEMRQRHGTAL----EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1253
Cdd:PTZ00121 1450 KKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1254 KSLQQAKS-----ESEHKRKKLEAQLQEVMARFSEGEKVkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1328
Cdd:PTZ00121 1528 KKAEEAKKadeakKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1329 QLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLVETKKKLEDDVGALEGLEE 1405
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEelkKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1406 VKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisARYAEE 1483
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEE 1754
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1484 RDRAEAEAREKDTKALSMARALDEALeAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1557
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM 1827
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
907-1285 |
4.11e-18 |
|
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: 91.67 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 907 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEK 986
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 987 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEmtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQEL 1066
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1067 EKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA 1146
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1147 RNKAEKLKRDLSEELEALKTELedtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtALEEIS---- 1222
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-----ALEPVNmlai 978
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1223 EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKR-KKLEAQLQEVMARFSEGE 1285
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAfEAINENFNEIFAELSGGT 1042
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
855-1704 |
1.04e-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: 90.03 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 855 KPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL-LEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL 933
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLeLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 934 EEILHDLESRVEEEEERNQSLQN-EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1012
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1013 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1092
Cdd:pfam02463 336 EIEELE--------KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1093 ELKIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK---AEKLKRDLSEELEALKTELE 1169
Cdd:pfam02463 408 QLLLELARQLEDLLKEEK--KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdelELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1170 DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE- 1248
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQk 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1249 LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1328
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1329 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKR 1408
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1409 KLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1488
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1489 AEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1568
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1569 QATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElEDERKQRALAVAAKKKLEMDLKDVEAQIEA 1648
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE-EEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1649 ANKARDEAIKQLRKLQAQMKdyqrELEEARTSRDEIFTQSKENEKKLKSLEAEILQ 1704
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFE----EKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1297-1943 |
1.10e-17 |
|
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: 90.23 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1297 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1376
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1377 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1456
Cdd:pfam01576 96 NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1457 SNLEKKQKKFDQMLAEektisaryAEERDRAEAEAREkdtkalsmaraldealeakeEFERLNKQLRAEMEDLISSKDDv 1536
Cdd:pfam01576 176 KSLSKLKNKHEAMISD--------LEERLKKEEKGRQ--------------------ELEKAKRKLEGESTDLQEQIAE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1537 gknvhelekskrtLEQQVEEMRTQLEELEDELQAtedAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEA 1616
Cdd:pfam01576 227 -------------LQAQIAELRAQLAKKEEELQA---ALARLE------------EETAQKNNALKKIRELEAQISELQE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1617 ELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARTSRDEIFTQSKENEKKL 1695
Cdd:pfam01576 279 DLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1696 KSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1775
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1776 TMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQElEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANK 1855
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1856 IVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVN 1935
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 528481571 1936 TLKNRLRR 1943
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
848-1444 |
6.48e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 848 WRLFTKVKPLLQVTRQEEEMQAKDEEliKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLV 927
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 928 AKKQELEEilhdLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlEKVTAEAKIKKMEEDILLLEDQN 1007
Cdd:PRK03918 242 ELEKELES----LEGSKRKLEEKIRELEERIEELKKEIEELE---------------EKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1008 SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDaETTDLQDQIAEL 1087
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1088 QAQIDELKIQlaKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE-----LE 1162
Cdd:PRK03918 378 KKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1163 ALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDE---TRNHE--SQIQEMRQR-HGTALEEISEQLEQAKRVKGNLE 1236
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKElaEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1237 KNKQTLESDNKELtNEVKSLQQAKSESEHKRKKLEAQLQEVMAR-----FSEGEKVKG-------------ELADRTHKI 1298
Cdd:PRK03918 536 KLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEErlkelepfyneylELKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1299 QTELDNVSCL---LEDAEKKGIKLTKDVSSLESQLQDTQELLQEET-----RQKLNLSSRIRQLEEEKNNLLEQQEEEEE 1370
Cdd:PRK03918 615 EREEKELKKLeeeLDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1371 SRKNLEKQLATLQaqlvETKKKLEDDVGALEGLEEVKRKLQKdmevtsQKLEEKAIAFDKLEKTKNRLQQELDD 1444
Cdd:PRK03918 695 TLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKK------YKALLKERALSKVGEIASEIFEELTE 758
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
912-1750 |
2.85e-16 |
|
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: 85.66 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 912 ETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKkmqshiQDLEEQLDEEEAARQKLQLEKVTAEA 991
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 992 KIKKMEEDILLLEDQNSKFLKEkklledrvgemtsqlaeeeekakNLGKVKNKQEMmmvdleerlkkEEKTRQELEKAKR 1071
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1072 KLDAETTDLQDQIAELQAQIdelkiqlAKKEEELQAVLARGDEEVAqknnalKQLRELQAQLAELQEDLES-EKAARNKA 1150
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRR-------SKIKEQNNRDIAGIKDKLA------KIREARDRQLAVAEDDLQAlESELREQL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1151 EKLKRDLSEELEALKTELEDT---LDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQ-LE 1226
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGELklrLNQATATPELLLQLENFDERIERA--REEQEAANAEVERLQSELRQARKRRDQaSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1227 QAKRVKGNLEKNKQTLEsdnkeltnEVKSLQQAKSESEHKRKKLEAQLQevmarfsegEKVKGELADRTHKIQTELDNVS 1306
Cdd:pfam12128 507 ALRQASRRLEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDW---------EQSIGKVISPELLHRTDLDPEV 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1307 clleDAEKKGIKLTKDVSSLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQL 1386
Cdd:pfam12128 570 ----WDGSVGGELNLYGVKLDLKRIDVPEWAASE-----------EELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1387 VETKKKLEDDVGALEGLEEVKRKLqkdmevTSQKLEEKaiafDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKF 1466
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRL------FDEKQSEK----DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAW 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1467 DQMLAEEKTiSARYAEERDRAEAEAREKDTKAlsmarALDEALEAKEE-FERLNKQLRAEMEDLISSKDDVGKNVHELEK 1545
Cdd:pfam12128 702 LEEQKEQKR-EARTEKQAYWQVVEGALDAQLA-----LLKAAIAARRSgAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1546 SKRTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFDRDLQardEQNEEKKRALVKQVREMEAELEDERKQR 1625
Cdd:pfam12128 776 EIRTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1626 ALAVAAKKkleMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARTSRDEIFTQSKENEKKLKSLEA 1700
Cdd:pfam12128 831 ARLIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSE 907
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1701 EILQLQEDLASSERARRHAEQER--DELADEISNSASGKAALLDEKRRLEAR 1750
Cdd:pfam12128 908 SVKKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1053-1628 |
3.62e-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: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1053 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLA----KKEEELQAVLARGDEEVAQKNNALKQLR- 1127
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEa 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1128 --------------ELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1193
Cdd:COG4913 367 llaalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1194 KAIDDETRNHESQIQ------EMRQR------------HGTALEEISEQlEQAKRVKGNLEKNKQTLESDNKELTNEVKS 1255
Cdd:COG4913 447 DALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFALTLLVPP-EHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1256 LQQAKSESEHKRKKLEAQ-------LQEVMARF-------SEGE------------KVKGELADRTHKIQTELDNVSCLL 1309
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKphpfrawLEAELGRRfdyvcvdSPEElrrhpraitragQVKGNGTRHEKDDRRRIRSRYVLG 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1310 EDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeknnLLEQQEEEEESRKNLEKQLATLQAQLvet 1389
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAEL--- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1390 kKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkFDQM 1469
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1470 LAE------EKTISARYAEERDRAEAEAREKDTKALSMARA-----------LDEALEAKEEFERLNKQLRAemEDLISS 1532
Cdd:COG4913 755 FAAalgdavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLESLPEYLALLDRLEE--DGLPEY 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1533 KDDVGKNVHELEKSKRT-----LEQQVEEMRTQLEELEDELQATE---DAKLRLEVNMQ--AMKAQFDRDLQA------- 1595
Cdd:COG4913 833 EERFKELLNENSIEFVAdllskLRRAIREIKERIDPLNDSLKRIPfgpGRYLRLEARPRpdPEVREFRQELRAvtsgasl 912
|
650 660 670
....*....|....*....|....*....|...
gi 528481571 1596 RDEQNEEKKRALVKQVREMEAELEDERKQRALA 1628
Cdd:COG4913 913 FDEELSEARFAALKRLIERLRSEEEESDRRWRA 945
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
863-1702 |
1.04e-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: 83.56 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 863 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLES 942
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 943 RVEEEEERNQSLQ----------NEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1012
Cdd:TIGR00606 277 RKKQMEKDNSELElkmekvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1013 E-------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIA 1085
Cdd:TIGR00606 357 DrhqehirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1086 ELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAEL--------------------QEDLESEKA 1145
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaeknsltetlkkevkslqNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1146 ARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL---------KKAIDDETRNHESQIQEMRQRHGT 1216
Cdd:TIGR00606 517 LRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1217 ALEEIsEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE---------AQLQEVMARFSEGEKV 1287
Cdd:TIGR00606 596 LNKEL-ASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1288 KGE----LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLL 1362
Cdd:TIGR00606 675 ENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEkRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1363 EQQEEEEESRKNL---EKQLATLQAQLvETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLE--EKAIAFDKLEKTKNR 1437
Cdd:TIGR00606 755 KVNRDIQRLKNDIeeqETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQE 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1438 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA---EAREKDTKALSMARALDEALEAKEE 1514
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQDSP 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1515 FERLNKQLRAEMEDLISSKDDVGKNVH-ELEKSKRTLEQQVEEMRTQLEELEDelqATEDAKLRLEVNMQAMKAQFdrdl 1593
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL---- 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1594 qardEQNEEKKRALVKQVREMEAELEDERKQRALAV--AAKKKLEMDLKDVEAQIeaanKARDEAIKQLRKLQaQMKDYQ 1671
Cdd:TIGR00606 987 ----EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEEL----KQHLKEMGQMQVLQ-MKQEHQ 1057
|
890 900 910
....*....|....*....|....*....|....
gi 528481571 1672 RELEEARTSRDE---IFTQSKENEKKLKSLEAEI 1702
Cdd:TIGR00606 1058 KLEENIDLIKRNhvlALGRQKGYEKEIKHFKKEL 1091
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1462 |
1.11e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 862 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLE 941
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 942 SRVEEEEERNQSLQN--EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEdillledqnSKFLKEKKLLED 1019
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---------KKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1020 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaETTDLQDQIAELQAQIDELKIQ-- 1097
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEev 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1098 --LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRdlSEELEALKTELEdtldtt 1175
Cdd:PTZ00121 1598 mkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE------ 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1176 aAQQELRSKREQEvaELKKAIDDETRNHESQIQEmrqrhgtalEEISEQLEQAKrvKGNLEKNKQTLESDNKELTNEVKS 1255
Cdd:PTZ00121 1667 -AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE---------AEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKA 1732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1256 LQQAKSESEHKRKKLEAQLQE------VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1329
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1330 --------LQDTQELLQEETRQKLNLSSriRQLEEEKNNLLEQQEEEEESRKNLEKqlatlQAQLVETKKKLEDDVGALE 1401
Cdd:PTZ00121 1813 ggkegnlvINDSKEMEDSAIKEVADSKN--MQLEEADAFEKHKFNKNNENGEDGNK-----EADFNKEKDLKEDDEEEIE 1885
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1402 GLEEVKRKLQKDMEV----TSQKLEEKAIAFDKLEKTKNRLQqelddlmvDLDHQRQIVSNLEKK 1462
Cdd:PTZ00121 1886 EADEIEKIDKDDIEReipnNNMAGKNNDIIDDKLDKDEYIKR--------DAEETREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
865-1580 |
1.26e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 83.24 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 865 EEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRARLVAKK---QELEEILHDLE 941
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 942 srveeeeernqslQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQNSKFLKEKK-----L 1016
Cdd:pfam15921 198 -------------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1017 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK-EEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELK 1095
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1096 IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTT 1175
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1176 AAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISE---QLEQAK----RVKGNLEKNKQTLESDNKE 1248
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKemlrKVVEELTAKKMTLESSERT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1249 LTNEVKSLQQAK-------SESEHKRKKLEAQLQEVMARFSEG----------EKVKGELADRTHKIQ---TELDNVSCL 1308
Cdd:pfam15921 498 VSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKDKVIEilrQQIENMTQL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1309 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeESRKNLEK-QLATLQAQLV 1387
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR------------VSDLELEKvKLVNAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1388 ETKKKLEDDVGALegLEEVK------RKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1461
Cdd:pfam15921 646 RAVKDIKQERDQL--LNEVKtsrnelNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1462 KQ-KKFDQMLAEEKTISARyaeerdRAEAEAREKDTKAL--SMARALDEALEAKEEFERLNKqlraEMEDLISSKDDVGK 1538
Cdd:pfam15921 721 SDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLeeAMTNANKEKHFLKEEKNKLSQ----ELSTVATEKNKMAG 790
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 528481571 1539 NVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1580
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1539 |
1.60e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 841 KLRHWQWWRLFTKVKPLLQVTRQ---EEEMQAKDEELIKVKERQVKVENELVEMERKhqqlLEEKNILAEQLQAETELFA 917
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 918 EAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQ-NEKKKMQSHIQDLEEQLDEEEAARQ-----KLQLEKVTAEA 991
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKaeekkKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 992 KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQELEKAKR 1071
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1072 KLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAE 1151
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1152 KLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAlEEISEQLEQAKRV 1231
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1232 ----KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRthkiqteldnvsc 1307
Cdd:PTZ00121 1636 eqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKK------------- 1696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1308 llEDAEKKGIKLTKdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLLEQQEEEEESRKNLEKQLATLQAQLV 1387
Cdd:PTZ00121 1697 --EAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK--KKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1388 ETKKKLEDDVgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ-KKF 1466
Cdd:PTZ00121 1771 EEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAF 1849
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1467 DQMLAEEKTISaryAEERDRAEAEAREKDTKalsmaRALDEALEAKEEFERLNKQlraEMEDLISSKDDVGKN 1539
Cdd:PTZ00121 1850 EKHKFNKNNEN---GEDGNKEADFNKEKDLK-----EDDEEEIEEADEIEKIDKD---DIEREIPNNNMAGKN 1911
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1219-1938 |
1.74e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1219 EEISEQLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmARFSEGEKVKGELADRT 1295
Cdd:PTZ00121 1053 DGNHEGKAEAKAHVGQDEGLKPSYkdfDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1296 HKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL 1375
Cdd:PTZ00121 1131 EEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1376 EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKlqkdmevtsqklEEKAiafDKLEKTKNRLQ-QELDDLMVDLDHQRQ 1454
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAE----AVKKAEEAKKD------------AEEA---KKAEEERNNEEiRKFEEARMAHFARRQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1455 IVSNLEKKQKKFDQMLAEE--KTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISS 1532
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEkkKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1533 KDDVGKNVHELEKSKR---TLEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKaQFDRDLQARDEQNEEKKRA 1606
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEkaeAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1607 L-VKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIF 1685
Cdd:PTZ00121 1428 EeKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1686 TQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE---LADEISNSASGKAAllDEKRRLEARIAQLEEELEEEQ 1762
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1763 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLE--RQNKDLKSKLQEL----EGSVKSKFKASIAALEAKI 1836
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLkkkeAEEKKKAEELKKAEEENKI 1661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1837 LQLEEQLEQEAKERAAAN-KIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeAEEEATRANASRRK 1915
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKE 1738
|
730 740
....*....|....*....|....*
gi 528481571 1916 LQRELDDATEA--SEGLSREVNTLK 1938
Cdd:PTZ00121 1739 AEEDKKKAEEAkkDEEEKKKIAHLK 1763
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1304-1823 |
1.81e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1304 NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNNLLEQQEEEEEsrknLEKQLATLQ 1383
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELE-------KLEKEVKELEELKEEIEELEKELES----LEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1384 AQLVETKKKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1463
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1464 KKFDQMLAEEKTISARYAEERDRAEAeaREKDTKALSMARALdealeaKEEFERLNKQLRAEmedlisSKDDVGKNVHEL 1543
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAK------KEELERLKKRLTGL------TPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1544 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFDRDLQARDEQNEEKKRALvkqvREMEAELEDERK 1623
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL----EEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1624 QRALAVAAKKKLEMDLKDVEAQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARTSRDEIFTQSKENEKKLKSLEA 1700
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1701 EILQLQE---DLASSERARRHAEQERDELADEISNSASGKAALLDEK---------------------RRLEARIAQLEE 1756
Cdd:PRK03918 547 ELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelEREEKELKKLEE 626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1757 ELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSaaQKSENARQQLERQNKDLKSKLQELEGSVKS 1823
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
878-1706 |
5.03e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.32 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 878 KERQVKVENELVEMERKHQQLLEEKNILAEQlqaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNE 957
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEK---------QKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 958 KKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDilLLEDQNSKFLKEKKLL---EDRVGEMTSQLAEEEEK 1034
Cdd:pfam15921 144 RNQLQNTVH----------------ELEAA------KCLKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1035 AKNlgKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI-DELKIQLAKKEEELQAVLARGD 1113
Cdd:pfam15921 200 SGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1114 EEVA----QKNNALKQLRELQAQLAELQEDlesekaARNKAEKLKRDLSE----------ELEALKTELEDTLDTTAAQQ 1179
Cdd:pfam15921 278 VEITglteKASSARSQANSIQSQLEIIQEQ------ARNQNSMYMRQLSDlestvsqlrsELREAKRMYEDKIEELEKQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1180 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA 1259
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1260 KSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL---TKDVSSLESQLQDTQEL 1336
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLessERTVSDLTASLQEKERA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1337 LQEETRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEV 1416
Cdd:pfam15921 512 IEATNAEITKLRSRV----DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1417 TSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfDQMLAEEKTISAryAEERDRAEAEAREKDT 1496
Cdd:pfam15921 585 AGAMQVEKA----QLEKEINDRRLELQEFKILKDKKDAKIRELEARVS--DLELEKVKLVNA--GSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1497 KALSMARALDEALEA-KEEFERLNKQLRAEMEdlisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1575
Cdd:pfam15921 657 QLLNEVKTSRNELNSlSEDYEVLKRNFRNKSE--------------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1576 ---LRLEVNMQamkaqfdRDLQARDEQNEekkrALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQieaanka 1652
Cdd:pfam15921 723 ghaMKVAMGMQ-------KQITAKRGQID----ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE------- 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1653 RDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQ 1706
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1376-1943 |
5.79e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1376 EKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafdklEKtknrlQQELDDLMVDLDHQRQI 1455
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1456 VSNLEKKQKKFDQMLAEEKTISARYAEERD--RAEAEAREKDTKALSMARaldEALEAKEEferlnkQLRAEMEDLISSK 1533
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARR---EELEDRDE------ELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1534 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdRDLQARDEQNEEKKRALVKQVRE 1613
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---------------EDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1614 MEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAikqlRKLQAQMK--DYQRELEEArtsrdEIFTQSKEN 1691
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA----EALLEAGKcpECGQPVEGS-----PHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1692 EKKLKSLEAEILQLQEDLASSErarrhaeqERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDR 1771
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1772 frkttmqVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfkASIAALEAKILqleeqleqeakerA 1851
Cdd:PRK02224 546 -------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIA-------------D 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1852 AANKIVRRTEKKlkEVFMQVEDERRhadqykEQMEKANSRMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEA 1926
Cdd:PRK02224 604 AEDEIERLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
570
....*....|....*..
gi 528481571 1927 SEGLSREVNTLKNRLRR 1943
Cdd:PRK02224 676 RDDLQAEIGAVENELEE 692
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1261-1942 |
6.11e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1261 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV----SCLLEDAEKKGIKLTKDVSSLESQLQDTQEL 1336
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1337 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL-EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKLQKDME 1415
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIA----SLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1416 VTSQKLEEKaiaFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKD 1495
Cdd:TIGR02169 322 ERLAKLEAE---IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1496 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1575
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1576 LRLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELE------------DERKQRALAVAAKKKLEMDLKDVE 1643
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1644 AQIEaankardEAIKQLRKLQA---------QMKDYQRELEEARTS------------------------RDEIFTQSKE 1690
Cdd:TIGR02169 558 AVAK-------EAIELLKRRKAgratflplnKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfGDTLVVEDIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1691 NEKKLK------SLEAEILQLQEDLASSERARRHAE-------QERDELADEISNSASGKAALLDEKRRLEARIAQLEEE 1757
Cdd:TIGR02169 631 AARRLMgkyrmvTLEGELFEKSGAMTGGSRAPRGGIlfsrsepAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1758 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEA--- 1834
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEArls 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1835 --KILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS 1912
Cdd:TIGR02169 790 hsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750
....*....|....*....|....*....|
gi 528481571 1913 RRKLQRELDDATEASEGLSREVNTLKNRLR 1942
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1138-1868 |
1.44e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1138 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQrhgta 1217
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1218 lEEISEQLEQAKRVkgnlEKNKQTLESDNKEltnEVKSLQQAKSESEHKRKKLEAQLQEVmaRFSEGEKvKGELADRTHK 1297
Cdd:PTZ00121 1166 -AEEARKAEDAKKA----EAARKAEEVRKAE---ELRKAEDARKAEAARKAEEERKAEEA--RKAEDAK-KAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1298 IQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEK 1377
Cdd:PTZ00121 1235 AKKDAEEAK--KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1378 QlATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQElddlmvdldhqrQIVS 1457
Cdd:PTZ00121 1310 K-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAA------------EKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1458 NLEKKQKKFDQMLAEEKtisaRYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVG 1537
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1538 KNVHELEKSKRTLEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFDRDLQARDEQNEEKKRALVKQVREME 1615
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1616 AELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1695
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1696 KSLEA----EILQLQEDLASSERARRHAEQERDELADEISNS---------ASGKAALLDEKRRLEARIAQLEEELEEEQ 1762
Cdd:PTZ00121 1608 KAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1763 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQ---KSENAR----QQLERQNKDLKSKLQEL--EGSVKSKFKASIAALE 1833
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENkikaEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEE 1767
|
730 740 750
....*....|....*....|....*....|....*..
gi 528481571 1834 AKILQLEEQLEQEAKERAAANKIVRR--TEKKLKEVF 1868
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDIF 1804
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1127-1836 |
1.62e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1127 RELQAQLAELQEDLESEKAARNKAEKLKR--DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaiDDETRNHE 1204
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR---LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1205 SQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE-LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1283
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1284 GEKvkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlle 1363
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL--------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1364 qqeeeeesRKNLEKQLATLQAQ------LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNR 1437
Cdd:COG4913 446 --------RDALAEALGLDEAElpfvgeLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1438 LQqelddlmVDLDHqrqivsnLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFE 1516
Cdd:COG4913 512 GR-------LVYER-------VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1517 RLNKQLRAEmeDLISSkddvGKNVHELEKSKRTLEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQ 1594
Cdd:COG4913 572 RHPRAITRA--GQVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEA--------LE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1595 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAvaakkklemdlkDVEAQIEAANKARDEaikqLRKLQAQMKDYQREL 1674
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIA------------ELEAELERLDASSDD----LAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1675 EEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQL 1754
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1755 EEELEEEQSNMELLNDRFRKT-TMQVDTLNTELAGERSAAQKsenaRQQLERQnkDLKSKLQELEGSVKSKFKASIAALE 1833
Cdd:COG4913 779 RARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEED--GLPEYEERFKELLNENSIEFVADLL 852
|
...
gi 528481571 1834 AKI 1836
Cdd:COG4913 853 SKL 855
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
857-1442 |
2.54e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 857 LLQVTRQEEEMQAKDeelikVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLvakkQELEEI 936
Cdd:PRK02224 189 LDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 937 LHDLESRVEEEEERNQSLQNEkkkmqshIQDLEeqldeeeAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1016
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE-------VRDLR-------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1017 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1096
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDAD-------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1097 QLAKKEEELQAVLARGDEEVAQKNnalkqlrELQAQLAELQEDLESEKAARNKAEKLKR-----------------DLSE 1159
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1160 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID--DETRNHESQIQEMRQRHGTALEEISEQLEQakrvkgnLEK 1237
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEE-------LRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1238 NKQTLEsdnkeltnevkslqqakSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTeLDNVSCLLEDAEKKGi 1317
Cdd:PRK02224 545 RAAELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1318 kltKDVSSLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEknNLLEQQEEEEESRKNLEKQLATLQ---AQLVETKKKL 1393
Cdd:PRK02224 606 ---DEIERLREKREALAE-LNDERRERLaEKRERKRELEAE--FDEARIEEAREDKERAEEYLEQVEeklDELREERDDL 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1394 EDDVGALEG----LEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQQEL 1442
Cdd:PRK02224 680 QAEIGAVENeleeLEELRERR-EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
872-1547 |
2.61e-14 |
|
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: 78.61 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 872 EELIKVKERQVKVENELVEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHD----------LE 941
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 942 SRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIK-KMEEDILLLEDQNSKFLKEKKLLEDR 1020
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1021 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTD----LQDQIAELQAQIDELKI 1096
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1097 ------QLAKKEE----ELQAVLARGDEEVAQKNNALKQLREL-----------QAQLAELQEDLESEKAARNKAEKLKR 1155
Cdd:pfam05483 322 atkticQLTEEKEaqmeELNKAKAAHSFVVTEFEATTCSLEELlrteqqrleknEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1156 DLSEELEALKT---ELEDTLDTTAAQQELRSK---REQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISEQLE 1226
Cdd:pfam05483 402 NKEVELEELKKilaEDEKLLDEKKQFEKIAEElkgKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1227 QAKRVKGNLEKNKQTLESDNKELTNE----VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1302
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1303 DNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1382
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1383 QAQLVETKKKLEDDVGALEGLEEVKRklqkdmeVTSQKLEEKAIAFDKLEKTKNRLQQELDdlmVDLDHQ-RQIVSNLEK 1461
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKK-------ISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKiAEMVALMEK 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1462 KQKKFDQMLaeektisaryaEERDRAEAEAREKDTKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNV 1540
Cdd:pfam05483 712 HKHQYDKII-----------EERDSELGLYKNKEQEQSSAKAALEIELSnIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
....*..
gi 528481571 1541 HELEKSK 1547
Cdd:pfam05483 781 AILKDKK 787
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
857-1605 |
6.20e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.70 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 857 LLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQqlleeknilaEQLQAETELFAEAEEMRARLVAKKQELEEI 936
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE----------KELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 937 LHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1016
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1017 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1096
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1097 QLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA 1176
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1177 AQQELRSKREQEVAELKKAIDDETRNHES---QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1253
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEgilKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1254 KSLQQAKSESE----HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1329
Cdd:pfam02463 678 IQELQEKAESElakeEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1330 LQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLvETKKKLEDDVGALEGLEEVKRK 1409
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEELE 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1410 LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA 1489
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELL-----LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1490 EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQ 1569
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-------EEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
730 740 750
....*....|....*....|....*....|....*.
gi 528481571 1570 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1605
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1219-1887 |
7.71e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.98 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1219 EEISEQLEQAKRVKGNLEKNKQ---TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegEKVKGELADRT 1295
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDkinKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKEN-------KKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1296 HKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLS---SRIRQLEEEKNNLLEQQEEEEESR 1372
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1373 KNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL--MVDLD 1450
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1451 HQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEME 1527
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1528 DLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaKLRLEVNmqamkaqfdrDLQARDEQNEEKKRAL 1607
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE-----RLKETII----------KNNSEIKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1608 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1687
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1688 SKENEKKLKSLEAEILQLQEDLASSErarrhAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1767
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1768 -------LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkSKFKASIAALE--AKILQ 1838
Cdd:TIGR04523 608 kekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII----KKIKESKTKIDdiIELMK 683
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481571 1839 LEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEK 1887
Cdd:TIGR04523 684 DWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
820-1472 |
7.77e-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: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 820 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELiKVKERQVKVENELVEMERKHQQLL 899
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 900 EEKNILAEQLQaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAAR 979
Cdd:TIGR00618 297 AHIKAVTQIEQ-------QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 980 QKLQleKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKE 1059
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1060 EKTRQ-------ELEKAKRKLDAETTDLQDQ-----------------IAELQAQIDELKIQLAKKEEELQAV------- 1108
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1109 --LARGDEEVAQKNNALK----QLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1182
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1183 SK-----REQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQL------EQAKRVKGNLEKNKQTLESDNKELTN 1251
Cdd:TIGR00618 608 DMlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1252 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvSSLESQLQ 1331
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA-RTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1332 DTQELLQEETRQKL-----NLSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLvetKKKLEDDVGALEGLEEv 1406
Cdd:TIGR00618 767 NEEVTAALQTGAELshlaaEIQFFNRLREE------------------DTHLLKTLEAEI---GQEIPSDEDILNLQCE- 824
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1407 krKLQKDMEVTSQKLEEkaiafdklektKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1472
Cdd:TIGR00618 825 --TLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
894-1643 |
1.23e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.93 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 894 KHQQLLEEKNILAEQLQAETELfaeAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQshiqdleeqld 973
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLC---TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 974 eeeaARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFlkekklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLE 1053
Cdd:TIGR00618 254 ----EQLKKQQLLKQLRARIEELRAQEAVLEETQERI------------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1054 ERLKKEEKTRQELEKAKrKLDAETTDLQDQIAELQAQIDELKIQ-----LAKKEEELQAVLARGDEEVAQKNNALKQLRE 1128
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQEIHIRDAhevatSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1129 LQAQLAELQEDLESEKAARNKAEklkRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQ 1208
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1209 EMRQrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1288
Cdd:TIGR00618 474 QLQT-----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1289 GELADRTHKIQTELDNVSCLLEDAEKKGIK---LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQ 1365
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1366 EEEEESRkNLEKQLATLQAQLVETKKKLEDdvgaleglEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1445
Cdd:TIGR00618 629 DVRLHLQ-QCSQELALKLTALHALQLTLTQ--------ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1446 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAE 1525
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1526 MEDLISskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLqardeqneEKKR 1605
Cdd:TIGR00618 780 LSHLAA----------EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKS 841
|
730 740 750
....*....|....*....|....*....|....*...
gi 528481571 1606 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVE 1643
Cdd:TIGR00618 842 ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1390-1753 |
3.33e-13 |
|
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: 75.49 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1390 KKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqivsnlekkqkkfdqm 1469
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----------------------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1470 laeektisaRYAEERDRAEaearekDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1549
Cdd:TIGR02169 212 ---------RYQALLKEKR------EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1550 LEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1621
Cdd:TIGR02169 277 LNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1622 RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN-------EKK 1694
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlNAA 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1695 LKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQ 1753
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1076-1735 |
7.58e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1076 ETTDLQDQIAELQAQIDELkiqlakkeEELQAVLargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK-----A 1150
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1151 EKLKRDLSEELEALKTELEDTldttaaqqelrskrEQEVAELKKAIdDETRNHESQIQEMRQRHGTaleeisEQLEQAKR 1230
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARL-DALREELDELEAQIRGNGG------DRLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1231 vkgnleknkqtlesdnkeltnEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvkgELADRTHKIQTELDNVSCLLE 1310
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1311 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlleqqeeeeesRKNLEKQLATLQAQ----- 1385
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-----------------RDALAEALGLDEAElpfvg 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1386 -LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNRLQqelddlmVDLDHqrqivsnLEKKQK 1464
Cdd:COG4913 465 eLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLRGR-------LVYER-------VRTGLP 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1465 KFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFERLNKQLRAemEDLISSKDDVG-KNVHE 1542
Cdd:COG4913 525 DPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELRRHPRAITR--AGQVKGNGTRHeKDDRR 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1543 LEKSKRTL----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQNEEKKRalVKQVREMEAEL 1618
Cdd:COG4913 597 RIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDEID--VASAEREIAEL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1619 EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftQSKENEKKLKSL 1698
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALL 751
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481571 1699 EAEILQLQEDlASSERARRHAEQERDELADEISNSAS 1735
Cdd:COG4913 752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEE 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1218-1872 |
1.59e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.75 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1218 LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA---RFSEGEKVKGELadr 1294
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlsKINSEIKNDKEQ--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1295 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1374
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1375 LEKQLATLQAqLVETKKKLEDDvgaLEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDlmvdldhQRQ 1454
Cdd:TIGR04523 199 LELLLSNLKK-KIQKNKSLESQ---ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1455 IVSNLEKKQKKFDQmlAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRaEMEDLISSKD 1534
Cdd:TIGR04523 265 IKKQLSEKQKELEQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1535 DVgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREM 1614
Cdd:TIGR04523 342 EQ---ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1615 EAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKK 1694
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1695 LKSLEAEILQLqedlasserarrhaEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEeleeeqsnmELLNDRFRK 1774
Cdd:TIGR04523 498 LKKLNEEKKEL--------------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---------ELNKDDFEL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1775 TTmqvDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAAN 1854
Cdd:TIGR04523 555 KK---ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
650
....*....|....*...
gi 528481571 1855 KIVRRTEKKLKEVFMQVE 1872
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVK 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1375-1922 |
2.16e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1375 LEKQLATLQaQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIafDKLEKTKNRLQQELDDLMVDLDHQRQ 1454
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1455 IVSNLEKkqkkfdQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLI 1530
Cdd:COG4913 324 ELDELEA------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1531 SSKDDVGKNVHELEKSKRTLEQQveemrtqLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQneekkralVK- 1609
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE--------LPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1610 -----QVREMEAE-----------------LEDERKQRALAVAAKKKLEMDL-------KDVEAQIEAA----------- 1649
Cdd:COG4913 463 vgeliEVRPEEERwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRLvyervrtGLPDPERPRLdpdslagkldf 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1650 --NKARDEAIKQLRKL--------QAQMKDYQREL---------EEARTSRDEIFTQSK-----ENEKKLKSLEAEILQL 1705
Cdd:COG4913 543 kpHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAItragqvkgnGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1706 QEDLASSERARRHAEQERDELAD---------EISNSASGKAALLDEKRRLEARIAQleeeleeeqsnMELLNDRFRKTT 1776
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELER-----------LDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1777 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKI 1856
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-----------DRLEAAEDLARLELRALLEERFAAALG 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1857 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKAnsrMKQLKRQLEEAEEEATRANASRRKLQRELDD 1922
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1027-1753 |
2.70e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.68 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1027 QLAEEEEK----AKNLGKVKNKQEMMMVDLE---ERL----------KKEEKTRQELEKAKRKLDAET---TDLQDQIAE 1086
Cdd:COG3096 300 QLAEEQYRlvemARELEELSARESDLEQDYQaasDHLnlvqtalrqqEKIERYQEDLEELTERLEEQEevvEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1087 LQAQ-------IDELKIQLAKKEEEL-----------QAVLARGDEEVAQKNNAL--KQLRELQAQL-AELQEDLESEKA 1145
Cdd:COG3096 380 AEARleaaeeeVDSLKSQLADYQQALdvqqtraiqyqQAVQALEKARALCGLPDLtpENAEDYLAAFrAKEQQATEEVLE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1146 ARNK---AEKLKRDLSEELEALK-----TELEDTLDTtaAQQELRSKREQE-----VAELKKAIDDETRNHESQIQEMRQ 1212
Cdd:COG3096 460 LEQKlsvADAARRQFEKAYELVCkiageVERSQAWQT--ARELLRRYRSQQalaqrLQQLRAQLAELEQRLRQQQNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1213 rhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfsegEKVKGELA 1292
Cdd:COG3096 538 -----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR----APAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1293 DRTHKIQTEldnVSCLLEDAekkgikltkdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR 1372
Cdd:COG3096 609 DALERLREQ---SGEALADS-----------QEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRL 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1373 KNLEKQL-ATLQAQLVEtKKKLEDD--VGALEG----------LEEVKRKLQkDMEVTSQKL---EEKAIAFDKlektKN 1436
Cdd:COG3096 675 LALAERLgGVLLSEIYD-DVTLEDApyFSALYGparhaivvpdLSAVKEQLA-GLEDCPEDLyliEGDPDSFDD----SV 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1437 RLQQELDDLMVDLDHQRQI-VSNLEK--------KQKKFDQMLAEEKTISARYAEER------DRAEAEAREKDTKALSM 1501
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASfdvqklQRLHQAFSQFVGGHLAV 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1502 ARALDEALEAKE------EFERLNKQLRAEMEDLISSKDDVGKNVHELEK--------SKRTLEQQVEEMRTQLEELED- 1566
Cdd:COG3096 829 AFAPDPEAELAAlrqrrsELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREELDAAQEa 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1567 --ELQATEDAKLRLEVNMQAMK---AQFDRdLQARDEQNEEKKRALVKQVREMEaeledERKQRALAVAAKKKLEM---- 1637
Cdd:COG3096 909 qaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVVQRRPHFSYEDAVGLlgen 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1638 -DLKD-VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEaeilqLQEDLASSERA 1715
Cdd:COG3096 983 sDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG-----VQADAEAEERA 1057
|
810 820 830
....*....|....*....|....*....|....*...
gi 528481571 1716 RrhaeQERDELADEISNSASGKAALLDEKRRLEARIAQ 1753
Cdd:COG3096 1058 R----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1082-1729 |
3.19e-12 |
|
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: 72.31 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1082 DQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS--- 1158
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlr 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1159 ---EELEALKTELEDT-------------LDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1222
Cdd:TIGR00618 267 ariEELRAQEAVLEETqerinrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1223 EQLEQAKRVKGNLEKNKQTL----ESDNKELTNEVKSLQQAKSESEHKRK-------KLEAQLQEVMARFSEGEKVKGEL 1291
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSireiSCQQHTLTQHIHTLQQQKTTLTQKLQslckeldILQREQATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1292 ADRTHKIQTELD----------NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1361
Cdd:TIGR00618 427 AHAKKQQELQQRyaelcaaaitCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1362 LEQQEEEEESRKNLEKQLAT--LQAQLVETKKKLEDDVGALEGLEEVKRK----LQKDMEVTSQKLEEKAIAFDKLEKTK 1435
Cdd:TIGR00618 507 CGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKqrasLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1436 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlsmARALDEALEAKEEF 1515
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH---ALQLTLTQERVREH 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1516 ERLNKQLRAEMEDLISSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELEdelqatEDAKLRLEVNMQAMKAQfdRDLQ 1594
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIE------EYDREFNEIENASSSLG--SDLA 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1595 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL 1674
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1675 EEARTSRDEIFTQSKENEK----KLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1729
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1374-1942 |
1.51e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1374 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLmvdlDHQR 1453
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1454 QIVSNLEKKQKKFDQmlaEEKTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKqlraEMEDLISSK 1533
Cdd:PRK03918 238 EEIEELEKELESLEG---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1534 DDVGKNVHELEKSKRTLEQQV---EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFDRDLQARDEQNEEKKRALVKQ 1610
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1611 VREMEAELEDERKqralavaAKKKLEMDLKDVEAQI---EAANKARDEAIKQLRKLQAQMKDYQRELEEARtsRDEIFtq 1687
Cdd:PRK03918 386 PEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGRELTEEH--RKELL-- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1688 sKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsgkaaLLDEKRRLEARIAQLEEELEEEQSN-ME 1766
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEeYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1767 LLNDRFRKTTMQVDTLNTELagerSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLeqe 1846
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY--- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1847 aKERAAANKIVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEAT-----RANASRRKLQRELD 1921
Cdd:PRK03918 602 -NEYLELKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELA 676
|
570 580
....*....|....*....|.
gi 528481571 1922 DATEASEGLSREVNTLKNRLR 1942
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLE 697
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
988-1781 |
1.59e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.08 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 988 TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM------MVDLEERLKKEEK 1061
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1062 TRQELEKAKRKLDAETTDLQDQIAElqaQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLaELQEDLE 1141
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDE---QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL-LVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1142 SEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQevaeLKKAIDDETRNHESQIQEMRQRHGTALEEI 1221
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL----VIERQEDEAKTAAQLCADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1222 SEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEhKRKKLEAQLQEVMARFSegekvkgeLADRTHKIQTE 1301
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAERELS--------KAEKNSLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1302 LDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQL 1379
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmlTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1380 ATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDME-VTSQKLEEKAIAFDKLekTKNRLQQELDDLMVDLDHQRQIVSN 1458
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVC--GSQDEESDLERLKEEIEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1459 LEKKQKKFDQMLAEEKTISARYAEERDR---AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK-- 1533
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRqs 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1534 --DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQaTEDAKLRLEVNMQAMKAQFDRdLQARDEQNEekkralvKQV 1611
Cdd:TIGR00606 738 iiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1612 REMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIKQLRKLQA---QMKDYQRELEEARTSRDEIFT 1686
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQheLDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1687 QSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADeiSNSASGKAALL------------------------- 1741
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS--SKETSNKKAQDkvndikekvknihgymkdienkiqd 966
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 528481571 1742 ---DEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1781
Cdd:TIGR00606 967 gkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1023-1751 |
1.64e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.99 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1023 EMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL--QDQIAELQAQIDELKIQLak 1100
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERL-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1101 keEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESE----------KAARNKAEKLKRD-------LSE 1159
Cdd:PRK04863 365 --EEQNEVVEEADEQQeeneARAEAAEEEVDELKSQLADYQQALDVQqtraiqyqqaVQALERAKQLCGLpdltadnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1160 ELEALKTELED-TLDTTAAQQELRS-----KREQEVAELKKAIDDET-------------------RNHESQIQEMRQRH 1214
Cdd:PRK04863 443 WLEEFQAKEQEaTEELLSLEQKLSVaqaahSQFEQAYQLVRKIAGEVsrseawdvarellrrlreqRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1215 GTALEEISEQ------LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvk 1288
Cdd:PRK04863 523 SELEQRLRQQqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1289 geLADRTHKIQTELDNVSclledaEKKGIKLTkDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNnlleqqeee 1368
Cdd:PRK04863 601 --RAPAWLAAQDALARLR------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE--------- 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1369 eesrknlekQLATLQAQLVETKKKLEDDVGAL---EGLEEVkrKLQkDMEVTSQKLEE--KAIAFDKLEKTKNRLQQE-- 1441
Cdd:PRK04863 663 ---------RLSQPGGSEDPRLNALAERFGGVllsEIYDDV--SLE-DAPYFSALYGParHAIVVPDLSDAAEQLAGLed 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1442 -LDDLMV---DLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErDRAEAEAREKDTKALSMARALDEALEAKEEF-- 1515
Cdd:PRK04863 731 cPEDLYLiegDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEV-PLFGRAAREKRIEQLRAEREELAERYATLSFdv 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1516 ---ERLNKQLR----------------AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL--------------- 1561
Cdd:PRK04863 810 qklQRLHQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnllad 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1562 -------EELEDELQATEDAKL-------------RLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMeaeleDE 1621
Cdd:PRK04863 890 etladrvEEIREQLDEAEEAKRfvqqhgnalaqlePIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TE 963
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1622 RKQRALAVAAKKKLEMDLKDVE------AQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1695
Cdd:PRK04863 964 VVQRRAHFSYEDAAEMLAKNSDlneklrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1696 KSleaeiLQLQEDLASSERARRHaeqeRDELADEISNSASGKAALLDEKRRLEARI 1751
Cdd:PRK04863 1044 QD-----LGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
819-1170 |
2.04e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 819 FAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPL-LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQ 897
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 898 LLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeea 977
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-------- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 978 arqklqlekvtaeAKIKKMEEDILLLEDQnskflkekklledrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1057
Cdd:TIGR02168 845 -------------EQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1058 KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQK-NNALKQLRELQAQLAEL 1136
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRL 977
|
330 340 350
....*....|....*....|....*....|....
gi 528481571 1137 QEDLESEKAARNKAEKLKRDLSEELEALKTELED 1170
Cdd:TIGR02168 978 ENKIKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1053-1946 |
2.84e-11 |
|
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: 69.21 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1053 EERLKKEEKT---RQELEKAKRKLDAEttdlQDQIAELQAQIDELKIQLAKKEEELQAvlarGDEEVAQKNNALKQLREL 1129
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQA----ASDHLNLVQTALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1130 ---QAQLAELQEDLESEKAARnkaeklkrdlsEELEALKTELEDTLdtTAAQQELRSKREQeVAELKKAID-DETRNheS 1205
Cdd:COG3096 350 eryQEDLEELTERLEEQEEVV-----------EEAAEQLAEAEARL--EAAEEEVDSLKSQ-LADYQQALDvQQTRA--I 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1206 QIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegE 1285
Cdd:COG3096 414 QYQQAVQ----ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV-------C 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1286 KVKGELaDRthkiqteldnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEknnLLE 1363
Cdd:COG3096 483 KIAGEV-ER---------------SQAWQTARELLRRYRSQQALAQRLQQLRAQlaELEQRLRQQQNAERLLEE---FCQ 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1364 QQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVgalEGLEEVKRKLQkDMEVTSQKLEEKA----IAFDKLEKTKNRLQ 1439
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAV---EQRSELRQQLE-QLRARIKELAARApawlAAQDALERLREQSG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1440 QELDDLmVDLDHQRQIVSNLEKKQKKFDQMLAEEKtisARYAEERDRAEAEAREKDTKALSMARAL----------DEAL 1509
Cdd:COG3096 620 EALADS-QEVTAAMQQLLEREREATVERDELAARK---QALESQIERLSQPGGAEDPRLLALAERLggvllseiydDVTL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1510 EAKEEFERLNKQLR---------------AEMED------LIS----SKDDVGKNVHELEK------SKRTL-------- 1550
Cdd:COG3096 696 EDAPYFSALYGPARhaivvpdlsavkeqlAGLEDcpedlyLIEgdpdSFDDSVFDAEELEDavvvklSDRQWrysrfpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1551 --------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDL-----QARDEQNEEKKRALVKQVREMEA 1616
Cdd:COG3096 776 plfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1617 ELED----ERKQRALAVAAKKKLEMdlkdVEAQIEAANKARDEAikqlrkLQAQMKDYQRELEEARTSRDEIFTQSK--- 1689
Cdd:COG3096 851 ELAQhraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIQQHGKala 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1690 ENEKKLKSLEAEILQ---LQEDLASSERARRHAEQERDELADEISNSA----SGKAALLDEKRRLEARIAQLEEELEEEQ 1762
Cdd:COG3096 921 QLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1763 SNmelLNDRFRKTTMQVDTLNTELAGERSAAQkseNARQQLerqnKDLKSKLQELEGSVKSkfkasiaaleakilqleeq 1842
Cdd:COG3096 1001 RE---AREQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQADA------------------- 1051
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1843 leqEAKERAAANKivrrtekklkevfmqvederrhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDD 1922
Cdd:COG3096 1052 ---EAEERARIRR-----------------------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQ 1105
|
970 980 990
....*....|....*....|....*....|....
gi 528481571 1923 ATEASEG----------LSREvNTLKNRLRRGGP 1946
Cdd:COG3096 1106 EREQVVQakagwcavlrLARD-NDVERRLHRREL 1138
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1052-1834 |
3.24e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1052 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRE--- 1128
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSele 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1129 -LQAQL-AELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhesq 1206
Cdd:pfam12128 326 aLEDQHgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAK---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1207 IQEMRQRHGTALEEISEQLEQAKRvkgnleknkQTLESDNKELTNEVKSLQQAKSEsehkrkkleAQLQEVMARFSEGEK 1286
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESELR---------EQLEAGKLEFNEEEYRLKSRLGE---------LKLRLNQATATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1287 VKGELAD-RTHKIQTELdnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqq 1365
Cdd:pfam12128 464 LQLENFDeRIERAREEQ-------EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ-------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1366 eeeeesrknLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLektknRLQQelddl 1445
Cdd:pfam12128 529 ---------LFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL-----DLKR----- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1446 mvdLDHQRQIVSNlekkqkkfDQMLAEEKTISARYAEERDRAEAEarekdTKALSMARALDEALEAKEEFERlnkqlrae 1525
Cdd:pfam12128 590 ---IDVPEWAASE--------EELRERLDKAEEALQSAREKQAAA-----EEQLVQANGELEKASREETFAR-------- 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1526 mEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEledELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1605
Cdd:pfam12128 646 -TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE---RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1606 ALVKQVREMEAELEDERKQRALAVAAKkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIf 1685
Cdd:pfam12128 722 VVEGALDAQLALLKAAIAARRSGAKAE------LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV- 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1686 TQSKENEKKLKSLEAEILQLQedlasSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNM 1765
Cdd:pfam12128 795 LRYFDWYQETWLQRRPRLATQ-----LSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1766 ELLNdrfrktTMQVDTLNTELAGERSaaqksenarqQLERQNKDLKSKLQELEGSVKSK---FKASIAALEA 1834
Cdd:pfam12128 870 SKLA------TLKEDANSEQAQGSIG----------ERLAQLEDLKLKRDYLSESVKKYvehFKNVIADHSG 925
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
34-79 |
3.94e-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: 59.37 E-value: 3.94e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528481571 34 TAKKLVWVPSERHGFEAASIREERGEEVLVELaENGKKAMVNKDDI 79
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1012-1230 |
5.03e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1012 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1091
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1092 DELKIQLAKKEEELQAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDT 1171
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLD---AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1172 LDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKR 1230
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1051-1292 |
9.03e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1051 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvlargdeevaqknnALKQLRELQ 1130
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------------LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1131 AQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhESQIQEM 1210
Cdd:COG4942 97 AELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1211 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG--EKVK 1288
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgfAALK 252
|
....
gi 528481571 1289 GELA 1292
Cdd:COG4942 253 GKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1081-1302 |
9.27e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1081 QDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1160
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1161 LEALKTELEDTLDTTAAQ--QELRSKREQEVAELKKAID-DETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEK 1237
Cdd:COG4942 92 IAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1238 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1302
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1054-1725 |
1.25e-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: 66.67 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1054 ERLKK-EEKTRQELEKAKRKLDAETTDLQDQ---IAELQAQIDELKIQLakkEEELQAvlargDEEVAQKNNALKQ---- 1125
Cdd:pfam05483 88 EKIKKwKVSIEAELKQKENKLQENRKIIEAQrkaIQELQFENEKVSLKL---EEEIQE-----NKDLIKENNATRHlcnl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1126 LRELQAQLAELQEDLESEkaaRNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKREQE---VAELKKAIDDETR 1201
Cdd:pfam05483 160 LKETCARSAEKTKKYEYE---REETRQVYMDLNNNIEKMILAFEElRVQAENARLEMHFKLKEDhekIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1202 NHESQI---------QEMRQRHGT-ALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE 1271
Cdd:pfam05483 237 DKEKQVsllliqiteKENKMKDLTfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1272 AQLQ---EVMARFSEGEKVKGELADRTHK----IQTELDNVSCLLED---AEKKGIKLTKD-VSSLESQLQDTQELLQEE 1340
Cdd:pfam05483 317 EDLQiatKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEEllrTEQQRLEKNEDqLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1341 TRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQ------LVETKKK----LEDDVGALEGLEEVKRKL 1410
Cdd:pfam05483 397 TKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKeqelifLLQAREKeihdLEIQLTAIKTSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1411 QKDMEVTSQKLEEKAIAF----DKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKfdqMLAEEKTISARYAEERDR 1486
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1487 AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1566
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1567 ELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQI 1646
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM 709
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1647 EAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRdeiftqskenEKKLKSLEAEILQLQEDLASSERARRHAEQERDE 1725
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
866-1283 |
1.26e-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: 66.67 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 866 EMQAKDEELikvKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLESRVE 945
Cdd:pfam05483 385 ELQKKSSEL---EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 946 EEEERNQSLQNEKKKMqshiqdleeqldeeeaarqKLQLEKvtaeAKIKKMEedillLEDQNSKFLKEKKLLEDRVGEMT 1025
Cdd:pfam05483 461 AIKTSEEHYLKEVEDL-------------------KTELEK----EKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1026 SQLAEEEEKAKNlgkVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL 1105
Cdd:pfam05483 513 LELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1106 QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1185
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1186 EQ--------------EVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKN----KQTLESDNK 1247
Cdd:pfam05483 670 EEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEqssaKAALEIELS 749
|
410 420 430
....*....|....*....|....*....|....*.
gi 528481571 1248 ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1283
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
913-1644 |
1.27e-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: 66.67 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 913 TELFAEAEEMR-------ARLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQshiqdleeqldeeeaarqkLQLE 985
Cdd:pfam05483 81 SKLYKEAEKIKkwkvsieAELKQKENKLQENRKIIEAQRKAI----QELQFENEKVS-------------------LKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 986 KVTAEAKikkmeeDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNL-GKVKNKQEMMMVDLEERLKKEEKTRQ 1064
Cdd:pfam05483 138 EEIQENK------DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVyMDLNNNIEKMILAFEELRVQAENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1065 E----LEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQAQlaELQEDL 1140
Cdd:pfam05483 212 EmhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD-LTFLLEESRDKANQLEEKTKLQDE--NLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1141 ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAiddetRNHESQIQEMRQRHGTALEE 1220
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1221 ISEQLEQakrvkgNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQT 1300
Cdd:pfam05483 364 LLRTEQQ------RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1301 ELDNVSCLLEDAEKK----GIKLTKDVSSLESQLQDTQELLQEETRQKLnlssRIRQLEEEKNNLLEQQEEEEESRKNLE 1376
Cdd:pfam05483 437 KEQELIFLLQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKL----KNIELTAHCDKLLLENKELTQEASDMT 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1377 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTS----QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQ 1452
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVReefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1453 RQIVSNLEK----KQKKFDQMLAEEKTIsaryaeeRDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1528
Cdd:pfam05483 593 ENKCNNLKKqienKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1529 LISSKDDVgknVHELEKSKRTLEQQVeemrtqleELEDELQATEDAKLRLEVN-MQAMKAQFDRDLQARDEQ-----NEE 1602
Cdd:pfam05483 666 KKISEEKL---LEEVEKAKAIADEAV--------KLQKEIDKRCQHKIAEMVAlMEKHKHQYDKIIEERDSElglykNKE 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 528481571 1603 KKRALVKQVREME-----AELEDERKQRALAVAAKKKLEMDLKDVEA 1644
Cdd:pfam05483 735 QEQSSAKAALEIElsnikAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
932-1286 |
1.34e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.58 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 932 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1011
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1012 KEKKLLEDRVgemtsqlaeeeekaKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1091
Cdd:TIGR04523 419 QEKELLEKEI--------------ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1092 DELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRDLSEELEALKTELedt 1171
Cdd:TIGR04523 485 EQKQKELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLESEK---KEKESKISDLEDELNKDDFEL--- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1172 ldTTAAQQELRSKREQEVAELKKAIDDETRNHEsQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTN 1251
Cdd:TIGR04523 555 --KKENLEKEIDEKNKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
330 340 350
....*....|....*....|....*....|....*
gi 528481571 1252 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEK 1286
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
782-1304 |
1.47e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 782 FFRTGVLahleEERDL--KITDIIIYFQSVCRgylARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWW 848
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 849 RLFTKVKpLLQ--VTRQEEEMQAKDEELIKVKERQVKVENELVEMerkHQQLLEEKNILAEQLQAETElfaEAEEMRARL 926
Cdd:COG4913 285 FAQRRLE-LLEaeLEELRAELARLEAELERLEARLDALREELDEL---EAQIRGNGGDRLEQLEREIE---RLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 927 VAKKQELEEILHDLESRVEEEEernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1006
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1007 NS----KFLKEKKLLEDRVGEMTS---------QLAEEEEK-------------------AKNLGKV-----KNKQEMMM 1049
Cdd:COG4913 435 KSnipaRLLALRDALAEALGLDEAelpfvgeliEVRPEEERwrgaiervlggfaltllvpPEHYAAAlrwvnRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1050 VDLEERLKKEEKTRQELEKAK--RKLDAETTDLQDQI-AELQAQIDELKIQlakKEEELQ--------AVLARGDEEVAQ 1118
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitrAGQVKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1119 KN-------------NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELE---DTLDTTAAQQELR 1182
Cdd:COG4913 592 KDdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1183 SKrEQEVAELKKAiDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAksE 1262
Cdd:COG4913 672 EL-EAELERLDAS-SDDLAALEEQLEELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--A 743
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 528481571 1263 SEHKRKKLEAQLQEVMARFSEGEKVKgELADRTHKIQTELDN 1304
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNR 784
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
857-1445 |
1.48e-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: 66.79 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 857 LLQVTRQEE--EMQAKDEELIKVKERQVK-----VENELVEMERKHQQLLEEKNILAEQ----LQAETELFAEAEEMRAR 925
Cdd:pfam12128 272 TLIASRQEErqETSAELNQLLRTLDDQWKekrdeLNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 926 LVAKKQELEEILHDLESRVEEEEERNQSLqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDI-LLLE 1004
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1005 DQNSKFLKEKKLLEDRVGEMTSQLAE---EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1081
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1082 D---QIAELQAQIDELKIQLAKK---------------EEELQAVLARG------------DEEVAQKNNA------LKQ 1125
Cdd:pfam12128 510 QasrRLEERQSALDELELQLFPQagtllhflrkeapdwEQSIGKVISPEllhrtdldpevwDGSVGGELNLygvkldLKR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1126 L---------RELQAQLAELQEDLESEKA-----------ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1185
Cdd:pfam12128 590 IdvpewaaseEELRERLDKAEEALQSAREkqaaaeeqlvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1186 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKgnlEKNKQTLESDnkeLTNEVKSLQQAKSESEH 1265
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK---QAYWQVVEGA---LDAQLALLKAAIAARRS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1266 KRKKLEAQLQEVMARFSEGEKVKGelaDRTHKIQTELDNVSCLLEDAEKKGikltKDVSSLESQLQDTqeLLQEETRQKL 1345
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDP---DVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLAT 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1346 NLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVK-----RKLQKDMEVTSQK 1420
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERLAQ 894
|
650 660
....*....|....*....|....*
gi 528481571 1421 LEEkaiAFDKLEKTKNRLQQELDDL 1445
Cdd:pfam12128 895 LED---LKLKRDYLSESVKKYVEHF 916
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1547-1753 |
2.28e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1547 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFDR--DLQARDEQNEEKKRALVKQVREMEAELEDERKQ 1624
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1625 RALAvaAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ-AQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1703
Cdd:COG4913 299 ELRA--ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1704 QLQEDLAS-SERARRHAE---QERDELADEISNSASGKAALLDEKRRLEARIAQ 1753
Cdd:COG4913 377 ASAEEFAAlRAEAAALLEaleEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1504-1738 |
2.46e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1504 ALDEALEAKEEFERLNKQL---RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1580
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1581 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQL 1660
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1661 RKLQAQMKDYQRELEEARTSRDEIFTQSkenEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1738
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1032-1432 |
2.81e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1032 EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQA--VL 1109
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1110 ARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEV 1189
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1190 AELKKAIDDETRNHESQIQEMRQRHgtALEEISEQLEQAKR-------------------------------VKGNLEKN 1238
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLllliaaallallglggsllsliltiagvlflVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1239 KQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIK 1318
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1319 LTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEE--EKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1394
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 528481571 1395 DDVGALEGLEEVKRKLQKDMEVtSQKLEEKAIAFDKLE 1432
Cdd:COG4717 450 ELREELAELEAELEQLEEDGEL-AELLQELEELKAELR 486
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1253-1723 |
4.61e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1253 VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ- 1331
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1332 -DTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEddvgalEGLEEVKRKL 1410
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEER-----------LEELRELEEELEELEAELAELQEELE------ELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1411 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH--QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1488
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1489 AEAREKDTKALSMA----------RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR 1558
Cdd:COG4717 271 LILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1559 TQLEELEDELQ--ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVREMEAELEDERK--QRALAVAAKKK 1634
Cdd:COG4717 351 ELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGelEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1635 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY--QRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLASS 1712
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL-------KAELRELAEEWAALKLALELL 502
|
490
....*....|.
gi 528481571 1713 ERARRHAEQER 1723
Cdd:COG4717 503 EEAREEYREER 513
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
979-1750 |
4.98e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 979 RQKLQLEKVTAEAKIKKMEEDILLLEDQnskfLKEKKLLedrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKk 1058
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEER----LEEQNEV---VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1059 EEKTR--------QELEKAKRKLDA---ETTDLQDQIAELQAQIDEL---------KIQLAKK-----EEELQAVLARGD 1113
Cdd:PRK04863 408 VQQTRaiqyqqavQALERAKQLCGLpdlTADNAEDWLEEFQAKEQEAteellsleqKLSVAQAahsqfEQAYQLVRKIAG 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1114 E---EVAQKN--NALKQLRE----------LQAQLAELQEDLESEKAAR------NKAEKLKRDLSEELEALKTELEDTL 1172
Cdd:PRK04863 488 EvsrSEAWDVarELLRRLREqrhlaeqlqqLRMRLSELEQRLRQQQRAErllaefCKRLGKNLDDEDELEQLQEELEARL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1173 DTTAAQQElrskreqEVAELKKAIDDETRNHESQIQEMRQRhGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNE 1252
Cdd:PRK04863 568 ESLSESVS-------EARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1253 VKSLQQAKSESEHKRKKLEAQLQEVMAR-FSEGEKVKGeLADRTHKIQ-TEL-DNVSclLEDA----------------- 1312
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNA-LAERFGGVLlSEIyDDVS--LEDApyfsalygparhaivvp 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1313 EKKGIK---------------LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlleqqeeeeeSRKNLEK 1377
Cdd:PRK04863 717 DLSDAAeqlagledcpedlylIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLF----------GRAAREK 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1378 QLATLQAQ---LVETKKKLEDDVgalegleevkRKLQKDMEVTSQKL-EEKAIAFD-----KLEKTKNRLQQ---ELDDL 1445
Cdd:PRK04863 787 RIEQLRAEreeLAERYATLSFDV----------QKLQRLHQAFSRFIgSHLAVAFEadpeaELRQLNRRRVElerALADH 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1446 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTIsaryAEER--DRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1523
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNLL----ADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1524 AEMEDLisskDDVGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFDRDLQARDEQNEEK 1603
Cdd:PRK04863 932 SDPEQF----EQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQE 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1604 KRALVKQVREMEAELEDerkqralavaaKKKLEMDLKdveAQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARTSRD 1682
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQ-----------YNQVLASLK---SSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRD 1063
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1683 EIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL------DEKRRLEAR 1750
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1626-1860 |
6.28e-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: 63.24 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1626 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1705
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1706 QEDLasserarrhaEQERDELADEIS----NSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLnDRFRKTTMQVDT 1781
Cdd:COG4942 96 RAEL----------EAQKEELAELLRalyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1782 LNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1860
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
994-1502 |
6.41e-10 |
|
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: 64.46 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 994 KKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEE--EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELE 1067
Cdd:pfam10174 137 KTLEEMELRIETQkqtlGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELH 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1068 KAKRKLD--AETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQlaelqedlesEKA 1145
Cdd:pfam10174 217 RRNQLQPdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSH----------SKF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1146 ARNKAEKLKRDLSE---ELEALKTELE-------------DTLDTTAAQQELRSKREQ-EVAELKKAIDDETR---NHES 1205
Cdd:pfam10174 287 MKNKIDQLKQELSKkesELLALQTKLEtltnqnsdckqhiEVLKESLTAKEQRAAILQtEVDALRLRLEEKESflnKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1206 QIQEMRQRHGTALEEIS------------------------EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKS 1261
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlqkkienlqEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1262 ESE-------HKRKKLEAQLQEVMARFSEGEKV--------KGELADRTHKIQTELDNVSCLLEDAEKKGIKL------- 1319
Cdd:pfam10174 447 EKEriierlkEQREREDRERLEELESLKKENKDlkekvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLksleiav 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1320 ---TKDVSSLESQLQDTQElLQEETRQKLNLSSRIRQLEEEknnLLEQQEEEEESRKNLEKQLATLQAqlVETKKKLEDD 1396
Cdd:pfam10174 527 eqkKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE---VARYKEESGKAQAEVERLLGILRE--VENEKNDKDK 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1397 -VGALEGLEEVKRKLQ--KDMEVTSQKLEEKAIAFDKLEK--------TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1465
Cdd:pfam10174 601 kIAELESLTLRQMKEQnkKVANIKHGQQEMKKKGAQLLEEarrrednlADNSQQLQLEELMGALEKTRQELDATKARLSS 680
|
570 580 590
....*....|....*....|....*....|....*..
gi 528481571 1466 FDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1502
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1371-1634 |
9.59e-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: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1371 SRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1450
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1451 HQRQivsNLEKKQKKFDQMLAEektisaryaeerdrAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLI 1530
Cdd:COG4942 94 ELRA---ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1531 SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQARDEQNEEKKRALVKQ 1610
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 528481571 1611 VREMEAELEDERKQRALAVAAKKK 1634
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1297-1941 |
1.08e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1297 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1376
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1377 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1456
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1457 SNLEKKQKKFDQMLAEektisaryaeerdraeAEAREKDTKALSmaralDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1536
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQ----------------ISELKKQNNQLK-----DNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1537 GKNVHELEKSkrtlEQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA 1616
Cdd:TIGR04523 263 NKIKKQLSEK----QKELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1617 ELEDERKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLK 1696
Cdd:TIGR04523 336 IISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1697 SLEAEILQLQEDLASSERARRHAEQERDELADEISNsasgkaaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1776
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-------LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1777 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKsKFKASIAALEAKILQleeqleqeaKERAAANKI 1856
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISD---------LEDELNKDD 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1857 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNT 1936
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
....*
gi 528481571 1937 LKNRL 1941
Cdd:TIGR04523 632 IIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1487-1712 |
1.86e-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: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1487 AEAEAREKDTKALSMARA-LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1565
Cdd:COG4942 17 AQADAAAEAEAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1566 DELQATEDAKLRLEVNMQAMK--------------AQFDRDLQARDEQNeekkRALVKQVREMEAELEDERKQRALAVAA 1631
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLA----PARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1632 KKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLAS 1711
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPA 245
|
.
gi 528481571 1712 S 1712
Cdd:COG4942 246 A 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1498-1739 |
1.91e-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: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1498 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1577
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1578 LEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAI 1657
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1658 KQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGK 1737
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 528481571 1738 AA 1739
Cdd:COG4942 244 PA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
858-1232 |
2.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 858 LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL---- 933
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 934 EEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKE 1013
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1014 KK------------LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1081
Cdd:COG4717 271 LIltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1082 DQIAELQAQIDELKIQLAKKEEE--LQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKlkrdlSE 1159
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----AL 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1160 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHEsqIQEMRQRHGTALEEISEQLEQAKRVK 1232
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALK 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
907-1295 |
2.62e-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: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 907 EQLQAETELFAEAEEMRA-------RLVAKKQELEEILHDLESRVEEEEERNQSLQNEK--KKMQSHIQDLEEQLDEEEA 977
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 978 ARQKLQLEKVTAEAKIKKmeEDILLLEDQNSKFLKEKKL----LEDRVGEMtsQLAEEEEKAKNLGKVKNKQEMMMvdle 1053
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKREL--ERIRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1054 ERLKKEEKTRQELEKAkRKLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLR-ELQAQ 1132
Cdd:pfam17380 386 ERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEERAREMERVRLEEqERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1133 LAELQEDLESEKAARNKAEKLKRDLSEelealkteledtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQ 1212
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKR-----------------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1213 RHGTALEEiseqleqAKRVKGNLEKNKQtlesdnKELtNEVKSLQQAKSESEHKRKKLEA--QLQEVMARFSEGEKVKGE 1290
Cdd:pfam17380 525 RQKAIYEE-------ERRREAEEERRKQ------QEM-EERRRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAE 590
|
....*
gi 528481571 1291 LADRT 1295
Cdd:pfam17380 591 YEATT 595
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1086-1919 |
2.68e-09 |
|
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: 62.76 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1086 ELQAQIDEL--KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1163
Cdd:TIGR00606 170 ALKQKFDEIfsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1164 LKT---ELEDTL-------DTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKG 1233
Cdd:TIGR00606 250 LKNrlkEIEHNLskimkldNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1234 NLEKNKQTLESDNKELTNEVKSLQ-QAKSESEHKRKKlEAQLQEVMARFSEGEKVKGELADRthkiqtELDNVSCL-LED 1311
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLATRLELDGFERGPFSER------QIKNFHTLvIER 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1312 AEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrknLEKQlatlQAQLVETKK 1391
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI----------------LEKK----QEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1392 KLEDDVGALEGLEEVKRKLQKDMEVTSqKLEEKAIAFDKLEKTKNRLQQELDdlmvdldhqrqivsnLEKKQKKFDQMLA 1471
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNEKAD---------------LDRKLRKLDQEME 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1472 EEKtisaRYAEERDRAEAEAREKDTKalsmaraldealeakeeFERLNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLE 1551
Cdd:TIGR00606 526 QLN----HHTTTRTQMEMLTKDKMDK-----------------DEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHSKS 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1552 QQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQneekkralvkqvremEAELEDerkqRALAVAA 1631
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ---------------LSSYED----KLFDVCG 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1632 KKKLEMDLKDVEAQIEAANKardeaikQLRKLQAQMKDYQRELEEARTSR-------DEIFTQSKENEKKLKSLEAEILQ 1704
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRL 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1705 LQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMElLNDRFRKTTMQVDTLNT 1784
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAK 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1785 ELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVK----SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1860
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1861 EKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRE 1919
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1080-1824 |
2.87e-09 |
|
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: 62.43 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1080 LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLREL-QAQLAELQE-DLESEKAARNKAEKLK--R 1155
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEEIQenK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1156 DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqemrqrhgTALEEISEQLEQAK-----R 1230
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlemhfK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1231 VKGNLEKNKQTLESDNKELTN---EVKSLQQAKSESEHKRKKLEAQLQEVMARFSE-GEKVK------GELADRTHKIQT 1300
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDkekQVSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKlqdenlKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1301 ELDNVSCLLEDAEKKGIKLTKDV---SSLESQLQDTQELLQEET-RQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1376
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLqiaTKTICQLTEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1377 KQLATLQAQLVETKKKLEDdVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqiv 1456
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLL---------- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1457 SNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLISS 1532
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1533 KddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDEL-QATEDAKLRLEVNMQAMKAQFDRDLQARDEQN--EEKKRALVK 1609
Cdd:pfam05483 526 K----KQEERMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1610 QVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFtqsk 1689
Cdd:pfam05483 602 QIENKNKNIEELHQENK---ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL---- 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1690 ENEKKLKSLEAEILQLQEdlasserarrhaeqerdELADEISNSASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLN 1769
Cdd:pfam05483 675 EEVEKAKAIADEAVKLQK-----------------EIDKRCQHKIAEMVALMEKHKHQYDKIIEER------DSELGLYK 731
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1770 DRFRKTTMQVDTLNTELAGERsAAQKSENARQQLERQNKD-LKSKLQELEGSVKSK 1824
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIK-AELLSLKKQLEIEKEEKEkLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
952-1178 |
3.67e-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: 60.93 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 952 QSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEE 1031
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1032 EEKaknLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLAR 1111
Cdd:COG4942 103 KEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1112 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ 1178
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1052-1528 |
4.31e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1052 LEERLKKEektRQELEKAKRKLDaetTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQA 1131
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1132 QLAELQEDLEsekaARNKAEKLKRDLSEELEALKtELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR 1211
Cdd:COG4717 120 KLEKLLQLLP----LYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1212 QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAksesehKRKKLEAQLQEVMARFSEGEKVKGEL 1291
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE------ERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1292 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEES 1371
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1372 RKNLEKQLATLQAQLvetkkkleddvgALEGLEEVKRKLQKDMEVTS-QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1450
Cdd:COG4717 349 LQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1451 HQRQIVSNLEKKQKKfdQMLAEEKTISARYAEERDRAEAEAREKDTKaLSMARALDEALEAKEEFERLNKQLRAEMED 1528
Cdd:COG4717 417 ELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAE-LEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1412-1807 |
7.64e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1412 KDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQmLAEEKTISARYAEERDRAEA-E 1490
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1491 AREKDTKAL--SMARALDEALEAKEEFERLNKQL----RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEL 1564
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1565 EDELQATEDAK-----------------------------------LRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVK 1609
Cdd:COG4717 233 ENELEAAALEErlkearlllliaaallallglggsllsliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1610 QVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRkLQAQMKDYQRELEEARTSRDEIFTQSK 1689
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1690 ENEKKLKSLEAEILQLQEDLASSERARRH--AEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1767
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 528481571 1768 --LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQN 1807
Cdd:COG4717 472 aeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
897-1278 |
9.87e-09 |
|
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: 59.91 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 897 QLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEE 976
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 977 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERL 1056
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1057 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAvlargdeevaqknnALKQLRELQAQLAel 1136
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEA--------------LLEELRSLQERLN-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1137 qedlesekAARNKAEKLKRDLSE---------------ELEALKTELEdTLDTTAAQQELRSKREQEVAELKKAIDDETR 1201
Cdd:pfam07888 248 --------ASERKVEGLGEELSSmaaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1202 NHESQIQEMRQRHGTALEEISEQleQAKRVKGNLEK--NKQTLESDNKELTNEVKSLQQAKSESEHkrkkLEAQLQEVM 1278
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMER--EKLEVELGREKdcNRVQLSESRRELQELKASLRVAQKEKEQ----LQAEKQELL 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
979-1285 |
1.29e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 979 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--VGEMTSQLAEEEEKAKNLgkvknKQEMMMVD-LEER 1055
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERL-----DASSDDLAaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1056 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1135
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1136 LQEDLESEKA-ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQE-----VAELKKAIDDETRNHESQIQ- 1208
Cdd:COG4913 774 RIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFVADLLs 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1209 EMRQrhgtALEEISEQLEQAKRVKGNLEKNKQT---LESDNKELTnEVKSLQQ--------AKSESEHKRKKLEAQLQEV 1277
Cdd:COG4913 854 KLRR----AIREIKERIDPLNDSLKRIPFGPGRylrLEARPRPDP-EVREFRQelravtsgASLFDEELSEARFAALKRL 928
|
....*...
gi 528481571 1278 MARFSEGE 1285
Cdd:COG4913 929 IERLRSEE 936
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1081-1306 |
1.32e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1081 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEE 1160
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1161 LEALK---------------TELEDTLDTTAAQQELRSKREQEVAELKKAIdDETRNHESQIQEMRQRHGTALEEISEQL 1225
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1226 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1305
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
.
gi 528481571 1306 S 1306
Cdd:COG3883 251 A 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1060-1282 |
1.35e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1060 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ--LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1137
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1138 EDLES--EKAARNKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRH 1214
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQ-IAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1215 GTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFS 1282
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
894-1275 |
1.62e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 894 KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEIlhdlESRVEEEEERNQSLQNEKKKMqshiqdleeqld 973
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAIYAEQERM------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 974 eeeAARQKLQLEKVTAEAKIKKMEEdillledqnskflkekklledrvgemtsqlAEEEEKAKNLGKVKNKQEMMMvdle 1053
Cdd:pfam17380 343 ---AMERERELERIRQEERKRELER------------------------------IRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1054 ERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDELK--------IQLAKKEEELQAVLARGDEEVAQKNNALKQ 1125
Cdd:pfam17380 386 ERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1126 LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEElealktELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHES 1205
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1206 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQtlesdNKELTNEVKslqqaksESEHKRKKLEAQLQ 1275
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----EREMMRQIV-------ESEKARAEYEATTP 596
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1551-1763 |
1.79e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1551 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVA 1630
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1631 AKKKLEMDLKDVEAQIEAANKArdEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLA 1710
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1711 SSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQS 1763
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1473-1943 |
2.03e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1473 EKTISARYAEERDRAEAEArekdtkALSMARALDEALEAKEEFERLNkqlraemeDLISSKDDVGKNVHELEKSKRTLEQ 1552
Cdd:PRK02224 169 ERASDARLGVERVLSDQRG------SLDQLKAQIEEKEEKDLHERLN--------GLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1553 QVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1632
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIE------------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1633 KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlqedLASS 1712
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE-------LEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1713 ERARRHAEQERDELADEIsnsasgkaalldekRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELageRSA 1792
Cdd:PRK02224 376 REAVEDRREEIEELEEEI--------------EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL---RTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1793 AQKSENARQQLERQNkdLKSKLQELEGS----VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVrRTEKKLKEVF 1868
Cdd:PRK02224 439 RERVEEAEALLEAGK--CPECGQPVEGSphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLE 515
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1869 MQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1943
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1234-1833 |
2.60e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1234 NLEKNKQTLESDNKELTNEVKSLQQAK---SESEHKRKKLEAQLQEVMarfsegekvkgelaDRTHKIQTELDNVSCLLE 1310
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEkshSITLKEIERLSIEYNNAM--------------DDYNNLKSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1311 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIrqleeeknnlleqqeeeeESRKNLEKQLATLQAQLVETK 1390
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPV------------------YKNRNYINDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1391 KKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1470
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV--------LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1471 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEAleaKEEFERLNKQLRAemedLISSKDDVGKNVHEL------- 1543
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSKVSSLNQRIRA----LRENLDELSRNMEMLngqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1544 --------EKSKRTLEQQVEE---MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVR 1612
Cdd:PRK01156 457 vcgttlgeEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1613 EMEAELEDERKQRALAVAAKKklEMDLKDVEAQ---------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1677
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYK--SLKLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1678 RTSRDEIFtqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELAdeisnsasGKAALLDEKRRLEARIAQleee 1757
Cdd:PRK01156 614 KSYIDKSI---REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND---- 678
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1758 leeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvksKFKASIAALE 1833
Cdd:PRK01156 679 ----------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK-----KIKKAIGDLK 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
859-1279 |
2.82e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 859 QVTRQEEEMQAKDEELIKVKERQVKVENELVEME---RKHQQLLEEKNILAEQLQAETELFAEAEEMRaRLVAKKQELEE 935
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELReelEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 936 ILHDLESRVEEEEERNQSLQNEKKK----MQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1011
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1012 KEKKLLEDR-----VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1086
Cdd:COG4717 241 LEERLKEARlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1087 LQAQIDELKIQLAKKEEELQAVLARgdeevaqknnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKT 1166
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDR-----------IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1167 ELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1246
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
410 420 430
....*....|....*....|....*....|...
gi 528481571 1247 keltnevkSLQQAKSESEHKRKKLEAQLQEVMA 1279
Cdd:COG4717 470 --------ELAELLQELEELKAELRELAEEWAA 494
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1584-1751 |
3.52e-08 |
|
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: 56.47 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1584 AMKAQFDR--DLQARD---EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIK 1658
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1659 QLRKLQA--QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsg 1736
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-- 158
|
170
....*....|....*
gi 528481571 1737 kAALLDEKRRLEARI 1751
Cdd:COG1579 159 -EELEAEREELAAKI 172
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
822-1422 |
3.60e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.90 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 822 KQQQLSALKVLQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK---HQQL 898
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 899 LEEKNILAEQLQAETELFAEAEEMRAR------------LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQ 966
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 967 DLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKE------KKLLEDRVGEMTSQLAEEEEKAKNLGK 1040
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1041 VKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKN 1120
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1121 NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRS---KREQEVAELKKAID 1197
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKIAQQAAKLQGSDL 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1198 DETRnheSQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEV 1277
Cdd:TIGR00606 821 DRTV---QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1278 MARFSE--------------GEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQE--LLQEET 1341
Cdd:TIGR00606 898 QSLIREikdakeqdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdyLKQKET 977
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1342 rqklNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLveTKKKLEDDVGALEGLEEVKRKLQKDMEVTS 1418
Cdd:TIGR00606 978 ----ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNL--TLRKRENELKEVEEELKQHLKEMGQMQVLQ 1051
|
....
gi 528481571 1419 QKLE 1422
Cdd:TIGR00606 1052 MKQE 1055
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1030-1206 |
3.82e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1030 EEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVL 1109
Cdd:COG3883 17 QIQAKQKELSELQAELE----AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1110 A-----------------------------RGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1160
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528481571 1161 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQ 1206
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
872-1827 |
4.21e-08 |
|
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: 58.91 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 872 EELIKVKERQVKVENELVEMERKHQQLLEEKniLAEQLQAETELFAEAEEMRARLVAK-KQELEEILHDLESRVEEEEER 950
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETATVELH--LSNIENKKNELLDIIVEIKKHIHGEiNKDLNKILEDFKNKEKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 951 NQSLQNEK---KKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQ 1027
Cdd:TIGR01612 771 INDYAKEKdelNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1028 LAEEEEKAKNlgKVKNKQEMMmVDLEERLKKEEKTRQeLEKAKRKLDaettDLQDQIAELQAQIDE--LKIQLAKKEEEL 1105
Cdd:TIGR01612 851 FINFENNCKE--KIDSEHEQF-AELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLKKVDEY 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1106 QAVLARGDEEVAQKNNALKQLRE-LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTlDTTAAQQEL--- 1181
Cdd:TIGR01612 923 IKICENTKESIEKFHNKQNILKEiLNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLN-DYEAKNNELiky 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1182 ------------RSKREQEVAELKKAIDD---ETRNHESQIQEMRQRHGTALEEISEQLEqaKRVKGNLEK-NKQTLESD 1245
Cdd:TIGR01612 1002 fndlkanlgknkENMLYHQFDEKEKATNDieqKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlNKEILEEA 1079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1246 NKELTNEVKSLQQAK----------------SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNvsclL 1309
Cdd:TIGR01612 1080 EINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIND----L 1155
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1310 EDAEKKGIKlTKDVSSLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLLEQQEEEEESRKNLEKqlaTLQ 1383
Cdd:TIGR01612 1156 EDVADKAIS-NDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGK---LFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1384 AQLVETKKKLEDDVGALEG----LEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDD----LMVDLDHQRQI 1455
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAyiedLDEIKEK--------SPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1456 vSNLEKKQKKFDQMLAEEKTISARYAE-ERDRAEAEAREKDT--------------KALSMARALDEALEAKEEFERLNK 1520
Cdd:TIGR01612 1301 -SDIREKSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDInlylneianiynilKLNKIKKIIDEVKEYTKEIEENNK 1379
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1521 QLRAEM---EDLISS-KDDVgknvhELEKSKRTLEQQVEEmrTQLEELEDELQATEDAKLRLEVNMqamkaqfDRDLQAR 1596
Cdd:TIGR01612 1380 NIKDELdksEKLIKKiKDDI-----NLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNI-------DTYFKNA 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1597 DEQNEEKKrALVKQVremeaELEDERKQRALAVA---AKKKLEMDLKDVEAQIEAANKARDEA---IKQLRKLQAQMKDY 1670
Cdd:TIGR01612 1446 DENNENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQY 1519
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1671 QRELEE------ARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1744
Cdd:TIGR01612 1520 KKDVTEllnkysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQ 1599
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1745 RRLEA------RIAQLEEELEEEQSNMELLNDRFrkTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1818
Cdd:TIGR01612 1600 LSLENfenkflKISDIKKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD 1677
|
....*....
gi 528481571 1819 gSVKSKFKA 1827
Cdd:TIGR01612 1678 -ELDSEIEK 1685
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1559-1943 |
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 528481571 1559 TQLEELEDELQATEDAKLRLevnmqamkaqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAL--AVAAKKKLE 1636
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1637 MDLKDVEAQIEAAnkarDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ-SKENEKKLKSLEAEILQLQEDLASSERA 1715
Cdd:COG4717 139 AELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1716 RRHAEQERDELADEISNSASGKAALLDEKRRLEARI------------AQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1783
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1784 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1863
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1864 --LKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEASEGLSREVNTLKN 1939
Cdd:COG4717 374 alLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
....
gi 528481571 1940 RLRR 1943
Cdd:COG4717 454 ELAE 457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1278 |
4.74e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 853 KVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRarlvaKKQE 932
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 933 leeilhdlesrveeeeernqslqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1012
Cdd:PTZ00121 1631 ------------------------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1013 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAElqaQID 1092
Cdd:PTZ00121 1687 EKKAAE--------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEE 1755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1093 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRDLSEELEAlkTELE 1169
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiieGGKEGNLVINDSKEMED--SAIK 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1170 DTLDTTAAQQElRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1249
Cdd:PTZ00121 1834 EVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDL----KEDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
410 420
....*....|....*....|....*....
gi 528481571 1250 TNEVKSLQQAKSESEHKRKKLEAQLQEVM 1278
Cdd:PTZ00121 1909 GKNNDIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1072-1225 |
5.40e-08 |
|
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: 55.70 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1072 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAV---LARGDEEVAQKNNALKQLRELQA-------------QLAE 1135
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteLEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1136 LQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHG 1215
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
170
....*....|
gi 528481571 1216 TALEEISEQL 1225
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1079-1675 |
5.44e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1079 DLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS 1158
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1159 EELEALK--TELEDTLDTTAAQQELRSKRE-QEVAELKKAIDDETR---NHESQIQEMRQRHGTA--LEEISEQLEQAKR 1230
Cdd:PRK01156 267 MELEKNNyyKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKKQilsNIDAEINKYHAIIKKLsvLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1231 VKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSclle 1310
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS---- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1311 daekkgikltKDVSSLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNLLEQQEEEEESRknlekqlatlqa 1384
Cdd:PRK01156 423 ----------SKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSNHIINHYNEKKSR------------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1385 qLVETKKKLEDDVGAlegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1464
Cdd:PRK01156 481 -LEEKIREIEIEVKD---IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1465 KFDQMLAEEKTISARYAEER----------------DRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1528
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1529 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEqneekKR 1605
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQiaeIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LE 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1606 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIkqLRK-----LQAQMKDYQRELE 1675
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAM--IRKsasqaMTSLTRKYLFEFN 774
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1471-1734 |
6.74e-08 |
|
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: 57.73 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1471 AEEKTISARYAEERDRaeaeaREKDTKALS-MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1549
Cdd:pfam05667 226 WNSQGLASRLTPEEYR-----KRKRTKLLKrIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1550 L----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQ---NEEKKRALVKQVREMEAELEDER 1622
Cdd:pfam05667 301 ThtekLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQElekEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1623 KQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-EEARTSRDEIFTQSKENEKKL---KSL 1698
Cdd:pfam05667 380 EELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLeeiKEL 459
|
250 260 270
....*....|....*....|....*....|....*.
gi 528481571 1699 EAEILQLQEDLASSERARRHAEQERDELADEISNSA 1734
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSA 495
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1326-1878 |
7.97e-08 |
|
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: 57.44 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1326 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEE 1405
Cdd:pfam05557 32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLAD-------ARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1406 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERD 1485
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1486 RAEaearekdtkalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELE 1565
Cdd:pfam05557 185 DSE------------IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-EKYREEAATLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1566 DELQATEdAKLRLEVNMQAMKAQFDR---DLQARDEQNEEKKRALVKQVREMEAELEDERKQRalavaakKKLEMDLKDV 1642
Cdd:pfam05557 252 LEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR-------RELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1643 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEART---SRDEIFTQSKENEKKLKSLE--AEILQLQEDLASSERARR 1717
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1718 HAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELL--NDRFR--KTTMQVDTLNTELAGERSAA 1793
Cdd:pfam05557 404 SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEleRQRLReqKNELEMELERRCLQGDYDPK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1794 -----QKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK---LK 1865
Cdd:pfam05557 484 ktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKnqrLK 563
|
570
....*....|...
gi 528481571 1866 EVFMQVEDERRHA 1878
Cdd:pfam05557 564 EVFQAKIQEFRDV 576
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1265-1938 |
8.98e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1265 HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSslesqlQDTQELLQEETRQK 1344
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1345 LNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE--------VKRKLQKDMEV 1416
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1417 TSQKLE--------EKAIAFDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKTISARyaEERDRA 1487
Cdd:pfam12128 395 IKDKLAkireardrQLAVAEDDLQALESELREQLEAGKLEFnEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1488 EAEAREKDTKAL-SMARALDEALEAKEEFERLNKQLRAEmedlisskddvgknvhelekskrtlEQQVEEMRTQLEELED 1566
Cdd:pfam12128 473 IERAREEQEAANaEVERLQSELRQARKRRDQASEALRQA-------------------------SRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1567 ELQA---TEDAKLRLEVNM--QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA-ELEDERKQRALAVAAKKKLEMDLK 1640
Cdd:pfam12128 528 QLFPqagTLLHFLRKEAPDweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1641 DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSrdeiFTQSKENEKKLKS-LEAEILQLQEdlaSSERARRHA 1719
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1720 EQERDELADEISNSASGKAALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTMQVDTLNTELAGERSAAQKSE 1797
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1798 NArqqLERQNK-DLKSKlqELEGSVKSKFKASIAALEAKIlqleeqleqeakERAAankiVRRTEKKLKEVFMQvEDERR 1876
Cdd:pfam12128 750 KA---LETWYKrDLASL--GVDPDVIAKLKREIRTLERKI------------ERIA----VRRQEVLRYFDWYQ-ETWLQ 807
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1877 HADQYKEQMEKANSRMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLS---REVNTLK 1938
Cdd:pfam12128 808 RRPRLATQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRcemSKLATLK 876
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
979-1193 |
1.22e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 979 RQKLQlekvTAEAKIK--KMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEErL 1056
Cdd:COG3206 188 RKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-S 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1057 KKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAkkeEELQAVLARGDEEVAQknnALKQLRELQAQL 1133
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1134 AELQEDLESEKAARNKAEKLKRDlseeLEALKTELEDTLdttAAQQELRSKREQEVAELK 1193
Cdd:COG3206 337 AQLEARLAELPELEAELRRLERE----VEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1334-1577 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1334 QELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1412
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1413 DMEVTSQKLEEKAIAFDKLEktknrlQQELDDLMVDLDHQRQIVSNLEkkqkKFDQMLAEEKTISARYAEERDRAEAEAR 1492
Cdd:COG4942 98 ELEAQKEELAELLRALYRLG------RQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1493 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1572
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 528481571 1573 DAKLR 1577
Cdd:COG4942 248 FAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
900-1122 |
1.42e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 900 EEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDE--EEA 977
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 978 ARQKLQLEKVTAEA-KIKKMEEDILLLEDQN-SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEER 1055
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1056 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAVLARGDEEVAQKNNA 1122
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1591-1802 |
1.48e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1591 RDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1670
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1671 QRELEEA-RTSRDEIFTQSKENEKKLKSLE----------AEILQLQEDLASSERARRHAEQERDELADEISNSASGKAA 1739
Cdd:COG4942 110 LRALYRLgRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1740 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQ 1802
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1149-1866 |
1.70e-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: 56.65 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1149 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR-QRHGTAL--EEISEQL 1225
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNaTRHLCNLlkETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1226 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRTHKIQTELDNV 1305
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE------DHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1306 SCLLEDAEKKgikltkdvsslESQLQDTQELLqEETRQKLNlssrirQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQ 1385
Cdd:pfam05483 243 SLLLIQITEK-----------ENKMKDLTFLL-EESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1386 L---VETKKKLEDDVG-ALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQ----ELDDLMVDLDHQRQIVS 1457
Cdd:pfam05483 305 LqrsMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1458 NLEKKQKKFDQMlaeektisaryAEERDRAEAEAREKDTKALSMARALDEaleaKEEFERLNKQLRAEMEDLISSKDDVG 1537
Cdd:pfam05483 385 ELQKKSSELEEM-----------TKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1538 KNVHELE-------KSKRTLEQQVEEMRTQLE-ELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ--------NE 1601
Cdd:pfam05483 450 KEIHDLEiqltaikTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQediinckkQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1602 EKKRALVKQVREMEAELEDE--------RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE 1673
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDElesvreefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1674 LEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASserARRHAEQERDELADEISNSASGKAALLDEKRRLEARIaq 1753
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA-- 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1754 leeeleeeqsnmellnDRFRKTTMQVDTLNTELAGERSAAQKSENAR--QQLERQNKDL---KSKLQElEGSVKSKFKAS 1828
Cdd:pfam05483 685 ----------------DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIE 747
|
730 740 750
....*....|....*....|....*....|....*...
gi 528481571 1829 IAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1866
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1053-1263 |
1.85e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1053 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRE-LQA 1131
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREeLGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1132 QLAELQED----------LESE----------------KAARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQELRSKR 1185
Cdd:COG3883 91 RARALYRSggsvsyldvlLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1186 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1263
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1292-1528 |
1.88e-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: 55.54 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1292 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeees 1371
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1372 rKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH 1451
Cdd:COG4942 86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1452 QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1528
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
991-1413 |
1.88e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 991 AKIKKMEEDILLLEDQNSKF---LKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM---------MVDLEERLKK 1058
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1059 EEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQL-AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1137
Cdd:COG4717 151 LEERLEELRELEEELEE----LEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1138 EDLESEKAARNKAEKLKRDLSEE-----------LEALKTELEDTLDTTAA------------QQELRSKREQEVAELKK 1194
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1195 AIDDETRN--HESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELtnEVKSLQQAKSESEHKRK-KLE 1271
Cdd:COG4717 307 LQALPALEelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGvEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1272 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLNLSSRI 1351
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1352 RQLEEEKNNLleqqeeeeesrkNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1413
Cdd:COG4717 463 EQLEEDGELA------------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1424 |
2.01e-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: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 859 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELE 934
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 935 EILHDLESRVEEEEernQSLQNEKKKMQSHiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1014
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKN--------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1015 KLLedrvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERlkkeektrqelEKAKRKLDAETTDLQDQIAELQAQIDEL 1094
Cdd:pfam05483 412 KIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR-----------EKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1095 KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldt 1174
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE----- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1175 tAAQQELRSKREqevaELKKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVK 1254
Cdd:pfam05483 552 -SVREEFIQKGD----EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1255 SLQQAKSESEHKRKKLEAQLQEVMARFsegekvkGELADRTHK-IQTELDNVSCLLEDAEK------KGIKLTKDVsSLE 1327
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKF-------EEIIDNYQKeIEDKKISEEKLLEEVEKakaiadEAVKLQKEI-DKR 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1328 SQlQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDvgaleglEEVK 1407
Cdd:pfam05483 698 CQ-HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIE-------KEEK 769
|
570
....*....|....*..
gi 528481571 1408 RKLQKDMEVTSQKLEEK 1424
Cdd:pfam05483 770 EKLKMEAKENTAILKDK 786
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1517-1943 |
2.10e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1517 RLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnmqamkAQFDRDLQAR 1596
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1597 DEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV----EAQIEAANKARDEAIKQLRKLQAQMKDYQR 1672
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1673 ELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL-----DEKRRL 1747
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLflllaREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1748 EARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKskLQELEGSVKSKFKA 1827
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1828 SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVfmqvedERRHADQYKEQMEKansRMKQLKRQLEEAEEEAT 1907
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL------EELLEALDEEELEE---ELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 528481571 1908 RANASRRKLQRELDDATEASE--GLSREVNTLKNRLRR 1943
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
955-1708 |
3.03e-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: 56.21 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 955 QNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQ-NSKFLKEKKLLEDRVGEMTSQLaEEEE 1033
Cdd:TIGR01612 532 QNIKAKLYKEIEAGLKESYELAKNWKKLIHE---IKKELEEENEDSIHLEKEiKDLFDKYLEIDDEIIYINKLKL-ELKE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1034 KAKNLGKvKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI-AELQAQIDEL-KIQLAKKEEELQAVLAR 1111
Cdd:TIGR01612 608 KIKNISD-KNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIySTIKSELSKIyEDDIDALYNELSSIVKE 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1112 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELEDTLDTTAaqQELRSKR 1185
Cdd:TIGR01612 687 NAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsniENKKNELLDIIVEIKKHIHGEINKDLNKIL--EDFKNKE 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1186 EQEVAELK--KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRvkgNLEKNKQTL------ESDNKELTNEVKSLQ 1257
Cdd:TIGR01612 765 KELSNKINdyAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQ---NYDKSKEYIktisikEDEIFKIINEMKFMK 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1258 QAKSESEHKRKKLEAQLQEVM----ARFSE-GEKVKGELADR-------------------THKIQTELDNVSCLLEDAE 1313
Cdd:TIGR01612 842 DDFLNKVDKFINFENNCKEKIdsehEQFAElTNKIKAEISDDklndyekkfndskslineiNKSIEEEYQNINTLKKVDE 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1314 KkgIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKl 1393
Cdd:TIGR01612 922 Y--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIE--KSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNN- 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1394 eddvGALEGLEEVKRKLQKDMEVTSQKleekaiAFDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEE 1473
Cdd:TIGR01612 997 ----ELIKYFNDLKANLGKNKENMLYH------QFDEKEKATNDIEQKIEDA-------NKNIPNIEIAIHTSIYNIIDE 1059
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1474 ktISARYAEERDRAEAEAREKDTKALSMARALDEALE-------AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKS 1546
Cdd:TIGR01612 1060 --IEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1547 KRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQARDEQNEekkraLVKQVREMEAELEDERK 1623
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEE 1211
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1624 QRALAVA---------------AKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMkDYQRELEEARTSRDEI---F 1685
Cdd:TIGR01612 1212 VKGINLSygknlgklflekideEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETFNISHDDDkdhH 1290
|
810 820
....*....|....*....|...
gi 528481571 1686 TQSKENEKKLKSLEAEILQLQED 1708
Cdd:TIGR01612 1291 IISKKHDENISDIREKSLKIIED 1313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1533-1753 |
3.50e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1533 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVR 1612
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAK-LLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1613 EMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIK-------QLRKLQAQMKDYQREL-EEARTSRD 1682
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1683 EIFTQSKENEKKLKSLEAEILQLQEDLAS-SERARRHAEQERD-ELADEISNSasgkaaLLdeKRRLEARIAQ 1753
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1104-1276 |
3.72e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1104 ELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtlDTTAAQQELRS 1183
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1184 KREQEvaelkkAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1263
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 528481571 1264 EHKRKKLEAQLQE 1276
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1383-1601 |
4.09e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1383 QAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1462
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1463 QKKFDQMLAEEKTI--SARYAEERDRAEAEAREKDtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknv 1540
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEALKA------ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528481571 1541 hELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNE 1601
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1195-1437 |
4.70e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1195 AIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQL 1274
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1275 QEVMARFsegEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1354
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1355 EEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKT 1434
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 528481571 1435 KNR 1437
Cdd:COG4942 250 ALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1460-1943 |
5.03e-07 |
|
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: 55.07 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1460 EKKQKKFDQMLAEEKTISARYAEERDRAEA----EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDD 1535
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1536 VGKNVHELEKSKRTLEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRAL 1607
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1608 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1687
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1688 SKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1760
Cdd:TIGR02169 415 LQRLseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1761 EQSNMELLNDRFRKTTMQVDTLNTEL------------------------AGERSAAQKSEN------ARQQLERQN--- 1807
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgeryataievaAGNRLNNVVVEDdavakeAIELLKRRKagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1808 ------KDLKSKLQELE--------------------------------------------------------------- 1818
Cdd:TIGR02169 575 atflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtlegelfeksga 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1819 ---GSVKSKFKASIAA-LEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQ 1894
Cdd:TIGR02169 655 mtgGSRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1895 LKRQLEEAEEE-------ATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1943
Cdd:TIGR02169 735 LKERLEELEEDlssleqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
864-1390 |
5.08e-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: 55.05 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 864 EEEMQAKDEELIKVKERQVKVENELVEMER-KHQQLLEEKNILAEQLQAETELFAeaeemrarlVAKKQELEEILHDLES 942
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQnKNHINNELESKEEQLSSYEDKLFD---------VCGSQDEESDLERLKE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 943 RVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVG 1022
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1023 EMTS----QLAEEEEKAKNLGKVKNKQEMMMVD-------LEERLKKEEKTRQELEKAK---------RKLDAETTDLQD 1082
Cdd:TIGR00606 727 EMLGlapgRQSIIDLKEKEIPELRNKLQKVNRDiqrlkndIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDVER 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1083 QIAELQAQID---------ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQedleSEKAARNKAEKL 1153
Cdd:TIGR00606 807 KIAQQAAKLQgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK----SEKLQIGTNLQR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1154 KRDLSEELEALKTELEDTLdttaaqQELRSKREQEVAELKKAIDDETRNHE--SQIQEMRQRHGTALEEISEQLEQAKRV 1231
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLI------REIKDAKEQDSPLETFLEKDQQEKEEliSSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1232 KGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSegekvkgeladrTHKIQTELDNVSCLLE 1310
Cdd:TIGR00606 957 MKDIENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID------------TQKIQERWLQDNLTLR 1024
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1311 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETK 1390
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL--EENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1049-1926 |
5.25e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1049 MVDLEERLKKEEKT---RQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlakkEEELQAVLARgdeeVAQKNNAL-- 1123
Cdd:PRK04863 275 MRHANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAASDH----LNLVQTALrq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1124 -KQLRELQAQLAELQEDLESEKAARNKAeklkRDLSEELEALKTELEDTLDTTAAQqelrskreqeVAELKKAID-DETR 1201
Cdd:PRK04863 347 qEKIERYQADLEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDELKSQ----------LADYQQALDvQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1202 NheSQIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarf 1281
Cdd:PRK04863 413 A--IQYQQAVQ----ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1282 segekvkgeladrtHKIQTELDNvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEKN 1359
Cdd:PRK04863 483 --------------RKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLQQLRMRlsELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1360 NLLEQQEeeeesrkNLEKQLATLQAQLVEtkkkleddvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK---- 1435
Cdd:PRK04863 544 KRLGKNL-------DDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawl 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1436 ------NRLQ----------QELDDLMVD-LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKA 1498
Cdd:PRK04863 607 aaqdalARLReqsgeefedsQDVTEYMQQlLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1499 LSMARAlDEALEAKEEFERLNKQLR---------------AEMEDL----------ISSKDDVGKNVHELEK------SK 1547
Cdd:PRK04863 687 LSEIYD-DVSLEDAPYFSALYGPARhaivvpdlsdaaeqlAGLEDCpedlyliegdPDSFDDSVFSVEELEKavvvkiAD 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1548 RTL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDLQ-----ARDEQNEEKKR 1605
Cdd:PRK04863 766 RQWrysrfpevplfgraarEKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1606 ALVKQVREMEAELED----ERKQRALAVAAKKKL--------EMDLKDVEAQIEAANKARDEaIKQLRKLQAQMKDYQRE 1673
Cdd:PRK04863 841 QLNRRRVELERALADhesqEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQ-LDEAEEAKRFVQQHGNA 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1674 LEeartsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAllDEKRRLEARIAq 1753
Cdd:PRK04863 920 LA-----------QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD- 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1754 leeeleeeqsnmelLNDRFRkttmqvdtlntelagersaaQKSENARQQLERQNKDLKSKLQELegsvkSKFKASIAALE 1833
Cdd:PRK04863 986 --------------LNEKLR--------------------QRLEQAEQERTRAREQLRQAQAQL-----AQYNQVLASLK 1026
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1834 AkilqleeqleqeakERAAANKIVRRTEKKLKEVFMQVEDE-----RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR 1908
Cdd:PRK04863 1027 S--------------SYDAKRQMLQELKQELQDLGVPADSGaeeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDN 1092
|
970
....*....|....*...
gi 528481571 1909 ANASRRKLQRELDDATEA 1926
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1324-1748 |
5.85e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1324 SSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEkQLATLQAQLVETKKKLEDDVGALEG 1402
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1403 LEEVKRKLQKDMEVTSQ---------KLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkfDQMLAEE 1473
Cdd:COG4717 124 LLQLLPLYQELEALEAElaelperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1474 KTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR-----AEMEDLISSKDDVGKNVHE------ 1542
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaAALLALLGLGGSLLSLILTiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1543 ------------LEKSKRTLEQQVEEMR--TQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDL-----QARDEQNEEK 1603
Cdd:COG4717 281 lvlgllallfllLAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1604 KRALVKQVREMEAEL--------EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRK--LQAQMKDYQRE 1673
Cdd:COG4717 361 EELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1674 LEEARTSRDEIftqskenEKKLKSLEAEILQLQED--LASSERARRHAEQERDELADEISNSASGKAALLDEKRRLE 1748
Cdd:COG4717 441 LEELEEELEEL-------REELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
941-1152 |
6.00e-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: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 941 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIlllEDQNSKFLKEKKLLEDR 1020
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1021 VGEM-----TSQLAEEEEKAKNLGKVKNKQEMMMVDLE---ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1092
Cdd:COG3883 92 ARALyrsggSVSYLDVLLGSESFSDFLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1093 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1152
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1033-1165 |
6.89e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.45 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1033 EKAK-NLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLakkEEELQAVLAR 1111
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1112 GDEEVAQknnALKQLRELQAQLA------ELQEDLESEKAARNKAEKLKRDLSEELEALK 1165
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYasvkahELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1352-1941 |
7.79e-07 |
|
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: 54.35 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1352 RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKL 1431
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV---HEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1432 EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDR-AEAEAREKDTKALSMARALD---- 1506
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDteis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1507 -------------EAL--EAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTleqQVEEMRTQLEELEDELQAT 1571
Cdd:pfam15921 235 ylkgrifpvedqlEALksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1572 EDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELE----------------DERKQRALAVAAKKKL 1635
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdqfsqesgnlDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1636 EMDLKDVEAQ------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAE-- 1701
Cdd:pfam15921 392 ELSLEKEQNKrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQle 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1702 -----ILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNmellNDRFRKTT 1776
Cdd:pfam15921 472 stkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQ 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1777 MQVDTLNTELAGERSAA----QKSENARQ-----------------QLERQNKDLKSKLQELEgSVKSKFKASIAALEAK 1835
Cdd:pfam15921 548 TECEALKLQMAEKDKVIeilrQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQEFK-ILKDKKDAKIRELEAR 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1836 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQME--KANSRMK---------QLKRQLEEAEE 1904
Cdd:pfam15921 627 VSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKseemetttnKLKMQLKSAQS 706
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481571 1905 EATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1941
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1377-1943 |
8.40e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1377 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEekaiafDKLEKTKNRLQQELDDLMVDLDHQRQIV 1456
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1457 SNLEKKQKKFDQMLAEEKtisARYAEERD--RAEAEAREKDTKALsmaraLDEALEAKEEFERLnKQLRAEmedliSSKD 1534
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKAL-----TGKHQDVTAKYNRR-RSKIKE-----QNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1535 DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlEVNMQamkaqfdrdlQARDEQNEEKKRALVKQVREM 1614
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-EFNEE----------EYRLKSRLGELKLRLNQATAT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1615 EAELEDERKQRALAVAAKKKLEMDLKDVE-AQIE--AANKARDEAIKQLRKLQAQMKDYQRELEEARTsrdEIFTQSKEN 1691
Cdd:pfam12128 460 PELLLQLENFDERIERAREEQEAANAEVErLQSElrQARKRRDQASEALRQASRRLEERQSALDELEL---QLFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1692 EKKLKSLEAEILQLQEDLASSE---RARRHAEQERDELADEISNSASGkaalLDEKR-----------RLEARIAQLEEE 1757
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPEllhRTDLDPEVWDGSVGGELNLYGVK----LDLKRidvpewaaseeELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1758 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKiL 1837
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ-L 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1838 QLEEQLEQEAKERAAANKIVRRTEK--KLKEVfmqVEDERRHADQYKEQMEKANSrmkQLKRQLEEAEEEATRANASRrk 1915
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASL-- 763
|
570 580
....*....|....*....|....*...
gi 528481571 1916 lqrelDDATEASEGLSREVNTLKNRLRR 1943
Cdd:pfam12128 764 -----GVDPDVIAKLKREIRTLERKIER 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
979-1135 |
1.10e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 979 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknLGKVKNKQEMmmvdleERLKK 1058
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEY------EALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1059 EEKTrqeLEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1135
Cdd:COG1579 97 EIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1520-1736 |
1.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1520 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdlQARDEQ 1599
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1600 NEEKKR-------------ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1666
Cdd:COG3883 97 RSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1667 MKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1736
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1643-1866 |
1.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1643 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLasserarrhaEQE 1722
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1723 RDELADEI------SNSASGKAALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAqks 1796
Cdd:COG3883 85 REELGERAralyrsGGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1797 ENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1866
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1256-1921 |
1.57e-06 |
|
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: 53.19 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1256 LQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADrthKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQE 1335
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE---EIQENKDLIK--ENNATRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1336 LLQEETRQ-KLNLSSRIrqleeEKNNLLEQQEEEEESRKNLEKQLatlqaqlvetkkKLEDDVGALEGLEEVKRKLQKDm 1414
Cdd:pfam05483 176 YEREETRQvYMDLNNNI-----EKMILAFEELRVQAENARLEMHF------------KLKEDHEKIQHLEEEYKKEIND- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1415 evtsqklEEKAIAFDKLEKTKNrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEARek 1494
Cdd:pfam05483 238 -------KEKQVSLLLIQITEK--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1495 dtKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAted 1573
Cdd:pfam05483 307 --RSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI--- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1574 aklrlevnmqamkaqFDRDLQARDEQNEEkkraLVKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKAR 1653
Cdd:pfam05483 382 ---------------ITMELQKKSSELEE----MTKFKNNKEVELEELKK----ILAEDEKLLDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1654 DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNS 1733
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1734 ASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1813
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1814 LQELEGSVKSKFKasiaaleaKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMK 1893
Cdd:pfam05483 596 CNNLKKQIENKNK--------NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660
....*....|....*....|....*...
gi 528481571 1894 QLKRQLEEAEEEATRANASRRKLQRELD 1921
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
807-1269 |
1.60e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 807 QSVCRGYLARkafAKKQQQLSALKVLQRNCAAY-----LKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVKErq 881
Cdd:TIGR00618 419 FRDLQGQLAH---AKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL-- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 882 vKVENELVEMER---KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEK 958
Cdd:TIGR00618 494 -ARLLELQEEPCplcGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 959 KKMQSHIQDLEEQLDEEEAARQKLQLE-KVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1037
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLtEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1038 LGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAKKEEELQAVLARGDE 1114
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlaQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1115 EVAQKNNALKQ-LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1193
Cdd:TIGR00618 733 DLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1194 KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKK 1269
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
864-1353 |
1.61e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 864 EEEMQAKDEELIKVKErqvkvenELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVA---KKQELEEILHDL 940
Cdd:PRK01156 189 EEKLKSSNLELENIKK-------QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 941 ESRVEEEEERN---QSLQNEKKKMQS--------HIQDLEEQLDEEEAARQKLQ---LEKVTAEAKIKKMEEdillLEDQ 1006
Cdd:PRK01156 262 ESDLSMELEKNnyyKELEERHMKIINdpvyknrnYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1007 NSKFLKEKKLLEDRVGEMT----------SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAE 1076
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1077 TTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG----------------------------DEEVAQKNNALKQLRE 1128
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiinhynekksrlEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1129 LQAQLAELQEDLESEKAARNKAEKLKrdlseeLEALKTELEDTLDTTAAQQELRSKREQEVAELKKA-IDDETRNHESQI 1207
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1208 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN-----------KELTNEVKSLQQAKSESEHKRKKLEA---- 1272
Cdd:PRK01156 572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddksyidksiREIENEANNLNNKYNEIQENKILIEKlrgk 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1273 --QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDA-------EKKGIKLTKDVSSLESQLQDTQELLQ--EET 1341
Cdd:PRK01156 652 idNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTIEILRTRINELSDRINDINETLEsmKKI 731
|
570
....*....|..
gi 528481571 1342 RQKLNLSSRIRQ 1353
Cdd:PRK01156 732 KKAIGDLKRLRE 743
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
992-1200 |
1.65e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 992 KIKKMEEDILL-LEDQNSKFLKE-------------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK--------QEMMM 1049
Cdd:PRK05771 2 APVRMKKVLIVtLKSYKDEVLEAlhelgvvhiedlkEELSNERLRKLRSLLTKLSEALDKLRSYLPKlnplreekKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1050 VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK------------------------IQLAKKEEEL 1105
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1106 QAVLARGDEEVAQKNN---------------ALKQLRELQAQLAELQEDLESEKAARNKAEKLKR------DLSEELEAL 1164
Cdd:PRK05771 162 LESDVENVEYISTDKGyvyvvvvvlkelsdeVEEELKKLGFERLELEEEGTPSELIREIKEELEEiekereSLLEELKEL 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 528481571 1165 KTELEDTLdtTAAQQELRSKREQEVAELKKAIDDET 1200
Cdd:PRK05771 242 AKKYLEEL--LALYEYLEIELERAEALSKFLKTDKT 275
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1252-1631 |
1.65e-06 |
|
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: 52.76 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1252 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ 1331
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1332 DtQELLQEETRQKL-NLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKL 1410
Cdd:pfam19220 101 E-AEAAKEELRIELrDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1411 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERDRAEAE 1490
Cdd:pfam19220 180 QALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQ-----------------AERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1491 ARekdtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1570
Cdd:pfam19220 243 RA-------SLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1571 TEDAKLRLEVNMQAM-KAQFDRD------------LQARDEQ----NEEKKRALVKQVREMEAELEDERKQRALAVAA 1631
Cdd:pfam19220 316 MQRARAELEERAEMLtKALAAKDaaleraeeriasLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1429-1642 |
1.69e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1429 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1492
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1493 EKDTKALSMARALDEALEAKEEFERLNKQLR---------AEMEDLISSKDDVGKnvhelekskrtLEQQVEEMRTQLEE 1563
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITK-----------IKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1564 LEDELQatEDAKLRLEVNMQAMKAqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1642
Cdd:PHA02562 318 LDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1413-1632 |
1.98e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1413 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEA 1491
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1492 REKDT----KALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1567
Cdd:COG3883 97 RSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1568 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1632
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1086 |
2.22e-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: 52.07 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 863 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELEEILH 938
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 939 DLESRVEEEEERNQSLQneKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE--AKIKKMEEDILLLEDQNSKFLKEKKL 1016
Cdd:COG4942 98 ELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1017 LEdrvgemtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1086
Cdd:COG4942 176 LE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1105-1334 |
3.07e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1105 LQAVLARGDEEVAQKNNALKQLRE----LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQE 1180
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1181 LRSKREQevaeLKKaiddetRNHESQIQEMRQRHGTAL---EEISEQLEQAKRVKGNLEKNKQTLE---SDNKELTNEVK 1254
Cdd:COG3883 81 IEERREE----LGE------RARALYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEelkADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1255 SLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1334
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
1051-1164 |
3.55e-06 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 51.10 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1051 DLEERLK--KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL----------------------- 1105
Cdd:pfam14362 107 EIDRELLeiQQEEADAAKAQLAAAYRARLAELEAQIAALDAEIDAAEARLDALQAEArceldgtpgtgtgvpgdgpvakt 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528481571 1106 -QAVLARGDEEVAQ-KNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1164
Cdd:pfam14362 187 kQAQLDAAQAELAAlQAQNDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEAL 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1696-1940 |
3.80e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1696 KSLEAEILQLQEDLASSERARRHAEQERDeladeisnsasgKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1775
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDARE------------QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1776 tmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEeqleqeaKERAAANK 1855
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-------RELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1856 IVRRTEKKLKEVFMQVEDErrhADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDateasegLSREVN 1935
Cdd:COG4913 360 RRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 528481571 1936 TLKNR 1940
Cdd:COG4913 430 SLERR 434
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1052-1620 |
3.89e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1052 LEERLKKEEKTRQELEKAKRKLDAETT-------DLQDQIAELQAQIDELKIQLAKKE--EELQAVLARGDEEVAQKNNA 1122
Cdd:PRK10246 299 IQEQSAALAHTRQQIEEVNTRLQSTMAlrarirhHAAKQSAELQAQQQSLNTWLAEHDrfRQWNNELAGWRAQFSQQTSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1123 LKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE---LEDTLDTTAAQQELRSKREQEVAELKKAIDDE 1199
Cdd:PRK10246 379 REQLRQWQQQLTHAEQKLNALPAI---TLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1200 TRNHESQIQEMRQRHGTALEEISEQ---LEQAKRVKgNLEKNKQTLESDNK-----ELTNEVKSLQQAKSESEHKRKkLE 1271
Cdd:PRK10246 456 QTQRNAALNEMRQRYKEKTQQLADVktiCEQEARIK-DLEAQRAQLQAGQPcplcgSTSHPAVEAYQALEPGVNQSR-LD 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1272 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELL-----QEETRQKLN 1346
Cdd:PRK10246 534 ALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaQEEHERQLR 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1347 LSSRIRQLEEEKNNLleqqeeeeesrknlEKQLATLQAQLVETKKKLEDDVGAL------EGLEEvkrKLQKDMEVTSQK 1420
Cdd:PRK10246 614 LLSQRHELQGQIAAH--------------NQQIIQYQQQIEQRQQQLLTALAGYaltlpqEDEEA---SWLATRQQEAQS 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1421 LEEKAIAFDKLEKTKNRLQQELDDL--MVDLDHQRQIVSnLEKKQKKFDQML---AEEKTISARYAEERDRAeAEAREKD 1495
Cdd:PRK10246 677 WQQRQNELTALQNRIQQLTPLLETLpqSDDLPHSEETVA-LDNWRQVHEQCLslhSQLQTLQQQDVLEAQRL-QKAQAQF 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1496 TKALSMARALDealeaKEEFerlnkqLRAEMEDlisskddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA----- 1570
Cdd:PRK10246 755 DTALQASVFDD-----QQAF------LAALLDE---------ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQhqqhr 814
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1571 ------TEDAKlRLEVNMQAMKAQFdRDLQAR----------DEQNEEKKRALVKQVREMEAELED 1620
Cdd:PRK10246 815 pdgldlTVTVE-QIQQELAQLAQQL-RENTTRqgeirqqlkqDADNRQQQQALMQQIAQATQQVED 878
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1442-1820 |
4.52e-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: 51.66 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1442 LDDLMVDLDHQRQIvsNLEKKQKKFDQMlaeektisaryAEERDRAEaeaREKDTKALSMARALDEALEAKEEFERLNKQ 1521
Cdd:pfam17380 271 LNQLLHIVQHQKAV--SERQQQEKFEKM-----------EQERLRQE---KEEKAREVERRRKLEEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1522 LRAEMEDLisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaQFDRDLQARDEQNE 1601
Cdd:pfam17380 335 IYAEQERM------------AMERERELERIRQEERKRELERIRQEEIAMEISRMR----------ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1602 ekkralvkQVREmeaELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1681
Cdd:pfam17380 393 --------RVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1682 DEIFTQsKENEKKLKSLEAEILQLQEDLASSERaRRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEE 1761
Cdd:pfam17380 462 VERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1762 QSNMELLNDRFRKTTMQVDTLNTElagERSAAQKSENARQQLeRQNKDLKSKLQELEGS 1820
Cdd:pfam17380 540 EERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1542-1718 |
4.75e-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: 49.92 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1542 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQNEEKKralVKQVREMEAELEDE 1621
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN---NKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1622 RKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAqmkdyqrELEEARTSRDEIFTQSKENEKKLKSLEAE 1701
Cdd:COG1579 102 KRRIS-------DLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|....*....
gi 528481571 1702 ILQL--QEDLASSERARRH 1718
Cdd:COG1579 168 LAAKipPELLALYERIRKR 186
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1084-1323 |
4.94e-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: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1084 IAELQAQIDELKIQLAKKEEELQAvlaRGDEEVAQKNNA-LKQlrELQAQLAEL---QEDLES-EKAARNKAEKLKRD-L 1157
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNA---LADKERAEADRQrLEQ--EKQQQLAAIsgsQSQLEStDQNALETNGQAQRDaI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1158 SEELEALKTELE------DTLDTTAAQQELRSK--REQEVAELKKAID---DETRNHES-QIQEMRQRHGTALEEISEQL 1225
Cdd:NF012221 1612 LEESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKISGkQLADAKQRHVDNQQKVKDAV 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1226 EQAKRVKGNLEKNKQTLESDnkeltnevksLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1305
Cdd:NF012221 1692 AKSEAGVAQGEQNQANAEQD----------IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK 1761
|
250
....*....|....*...
gi 528481571 1306 SCLLEdAEKKGIKLTKDV 1323
Cdd:NF012221 1762 ANQAQ-ADAKGAKQDESD 1778
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1048-1429 |
5.08e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1048 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLR 1127
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1128 ELQAQLAELQEDLESekaarnkaeklkrdLSEELEALKTELEDTLDTtaAQQELRSKREQEvaELKKAIDDETRNHESQI 1207
Cdd:pfam07888 126 AHEARIRELEEDIKT--------------LTQRVLERETELERMKER--AKKAGAQRKEEE--AERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1208 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTL------ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1281
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1282 SEGE-----------KVKGELADRTHKIQTELDNVS----CLLEDAEKKGIKLTKdvssLESQLQDTQELLQEETRQKLN 1346
Cdd:pfam07888 268 DRTQaelhqarlqaaQLTLQLADASLALREGRARWAqereTLQQSAEADKDRIEK----LSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1347 LSSrirQLEEEKnnlLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKdmeVTSQKLEEKAI 1426
Cdd:pfam07888 344 LEV---ELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET---VADAKWSEAAL 414
|
...
gi 528481571 1427 AFD 1429
Cdd:pfam07888 415 TST 417
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1706-1944 |
5.09e-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: 50.92 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1706 QEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTE 1785
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1786 LAGERSAAQKSENARQQLERQNKdLKSKLQeleGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLK 1865
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1866 EVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRRG 1944
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
985-1494 |
6.61e-06 |
|
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: 51.28 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 985 EKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQ 1064
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK----------YLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1065 ELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE------ 1138
Cdd:pfam05557 98 QLADAREVISC----LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1139 -----------------DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETR 1201
Cdd:pfam05557 174 elefeiqsqeqdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1202 NH--ESQIQE---MRQRHGTAL---EEISEQLEQakrvkgnLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1273
Cdd:pfam05557 254 KEklEQELQSwvkLAQDTGLNLrspEDLSRRIEQ-------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1274 LQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLED------AEKKGIKLTKDVSSLESQLQDTQ-----------EL 1336
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydkeltMSNYSPQLLERIEEAEDMTQKMQahneemeaqlsVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1337 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR-KNLEKQLATLQAQLvetkKKLEDDVGALEgLEEVKRKLQKDME 1415
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvDSLRRKLETLELER----QRLREQKNELE-MELERRCLQGDYD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1416 VTSQK---LEEKAIAfdkleKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERdRAEAEAR 1492
Cdd:pfam05557 482 PKKTKvlhLSMNPAA-----EAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESA 555
|
..
gi 528481571 1493 EK 1494
Cdd:pfam05557 556 EL 557
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
897-1355 |
7.07e-06 |
|
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: 51.28 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 897 QLLEEKNILaEQLQAETELfAEAEEMRARLvakkqELEEILHDLESRVEEEEERNQSLQNEKKKMQshiQDLEEQLDEEE 976
Cdd:pfam05557 3 ELIESKARL-SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 977 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMmmvdLEERL 1056
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL----LKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1057 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEE-----ELQAVLARGDEEVAQKNNALKQLRELQA 1131
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSElaripELEKELERLREHNKHLNENIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1132 QLAELQEDLESEKAARNKAEKLKRDLS---EELEALKTELEDTLDTTAAQQELRSK------REQEVAELKKAIDDETRN 1202
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEkleQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1203 HESQIQEMRQRHGTALEEISE---QLEQAKRVKGNLEKN-----------KQTLESDNKELTNEVKSLQQAK--SESEHK 1266
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDlnkKLKRHKALVRRLQRRvllltkerdgyRAILESYDKELTMSNYSPQLLEriEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1267 RKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLN 1346
Cdd:pfam05557 389 TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNE 466
|
....*....
gi 528481571 1347 LSSRIRQLE 1355
Cdd:pfam05557 467 LEMELERRC 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1495-1739 |
8.06e-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: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1495 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL------ 1568
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1569 -QATEDAKLRLEV------------NMQAMKAQFDRDLQARDEQNEEKKralvkQVREMEAELEDERKQralAVAAKKKL 1635
Cdd:COG3883 95 lYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1636 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1715
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260
....*....|....*....|....
gi 528481571 1716 RRHAEQERDELADEISNSASGKAA 1739
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1031-1165 |
9.57e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.63 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1031 EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL--KIQLAKKEEELQav 1108
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLerELSEARSEERRE-- 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528481571 1109 lARGDEEVAQKNNALKQLR----ELQAQLAELQEDLESEKAARNKaeklkrDLSEELEALK 1165
Cdd:COG2433 461 -IRKDREISRLDREIERLEreleEERERIEELKRKLERLKELWKL------EHSGELVPVK 514
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1543-1747 |
1.03e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1543 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1621
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1622 RKQRALAVAAKKKLEMDLKDVEAQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARTSRDE-- 1683
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1684 -IFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1747
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
877-1173 |
1.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 877 VKERQVKVEnelvEMERKHQQLLEEKNILAEQLQAETELfAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQN 956
Cdd:PRK02224 470 IEEDRERVE----ELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 957 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIllledqnskflkekklleDRVGEMTSQLAEEEEKAK 1036
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI------------------ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1037 NLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDlqDQIAELQAQIDELKIQLAKKEEELQAVLARGDE-- 1114
Cdd:PRK02224 607 EIERLREKRE----ALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDlq 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1115 -EVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLK---RDLSEEL-----EALKTELEDTLD 1173
Cdd:PRK02224 681 aEIGAVENELEELEELRERREALENRVEALEALYDEAEELEsmyGDLRAELrqrnvETLERMLNETFD 748
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1060-1336 |
1.07e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 50.08 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1060 EKTRQELEKAkRKLDAETTD----LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1135
Cdd:pfam04108 17 TDARSLLEEL-VVLLAKIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1136 LQE-----------DLESEKAARNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKreQEVAELKKAIDDETRNH 1203
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDLKRfDDDLRDLQKELESL--SSPSESISLIPTLLKEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1204 ESQIQEMRQRhgtaLEEIS---EQLEQAKRV-KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA 1279
Cdd:pfam04108 174 ESLEEEMASL----LESLTnhyDQCVTAVKLtEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNS 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1280 RFSEGEKVKGELADrthkIQTELDN-VSCLLEDAEkkgiKLTKDVSSLESQLQDTQEL 1336
Cdd:pfam04108 250 LIDELLSALQLIAE----IQSRLPEyLAALKEFEE----RWEEEKETIEDYLSELEDL 299
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
910-1148 |
1.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 910 QAETELFAEAEEMRArLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTA 989
Cdd:COG3883 13 FADPQIQAKQKELSE-LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 990 EAKIKKMEE-------------------DILLLEDQNSKFLKEKKLLeDRVGEMTSQLAEEEEKAKNlgKVKNKQEmmmv 1050
Cdd:COG3883 78 EAEIEERREelgeraralyrsggsvsylDVLLGSESFSDFLDRLSAL-SKIADADADLLEELKADKA--ELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1051 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1130
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....*...
gi 528481571 1131 AQLAELQEDLESEKAARN 1148
Cdd:COG3883 231 AAAAAAAAAAAAAASAAG 248
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1073-1288 |
1.24e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1073 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1152
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY---DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1153 LKRDLSEELEALKTEL----EDTLDTTAAQQ-----ELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRhgtaLEEISE 1223
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKELQHSLEKL----DTAIDELEEI----MDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1224 QLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1288
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLitlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
670-694 |
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 528481571 670 YKESLTKLMATLRNTNPNFVRCIIP 694
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1052-1227 |
1.35e-05 |
|
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: 47.64 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1052 LEERLKKEEKTRQELEK-----AKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLArgdeevaqknnalKQL 1126
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-------------QNV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1127 RELQAQLAELQEDLesEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ-----QELRSKREQEVAELKKAIDDETR 1201
Cdd:pfam01442 69 EELRQRLEPYTEEL--RKRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*.
gi 528481571 1202 NHESQIQEMRQRHGTALEEISEQLEQ 1227
Cdd:pfam01442 147 EVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1047-1278 |
1.42e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1047 MMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQL 1126
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1127 RELQAQLAELQEDLESEKAARNKAEKLKRD---LSEELEALKTELEDTLDTTAAQQEL--RSKR-EQEVAELKKAID--D 1198
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEknE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1199 ETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE---LTNEVKSLQQAKSESEHKRKKLEAQLQ 1275
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEadeLHKEIVEAQEKADELHEEIIELQKELR 240
|
...
gi 528481571 1276 EVM 1278
Cdd:COG1340 241 ELR 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1010-1356 |
1.44e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.96 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1010 FLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQA 1089
Cdd:COG5185 171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1090 QIDELKIQLAKKEEELQAVLARGDEEVA----QKNNALKQLRELQAQLAELQEDLESEKA------------ARNKAEKL 1153
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKrlneNANNLIKQFENTKEKIAEYTKSIDIKKAtesleeqlaaaeAEQELEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1154 KRDLSEELEALKTELEDTLDT-TAAQQELRSKREQEVAELKKAIDDET-RNHESQIQEMRQRHGTALEEiseQLEQAKRV 1231
Cdd:COG5185 331 KRETETGIQNLTAEIEQGQESlTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQN---QRGYAQEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1232 KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKiqteldnvSCLLED 1311
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN--------RSVRSK 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528481571 1312 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1356
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAE 524
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1066-1222 |
1.58e-05 |
|
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: 49.34 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1066 LEKAKRKLDAETTDLQDQIAELQAQIDelkiQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKA 1145
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1146 ARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQE-LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1222
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1598-1750 |
1.64e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1598 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE--------AANKARD----EAIKQLRKLQA 1665
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1666 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK- 1744
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 528481571 1745 RRLEAR 1750
Cdd:COG1842 175 EEMEAR 180
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
914-1550 |
1.75e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 914 ELFAEAEEMRaRLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKI 993
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 994 KKMEEDILLLED---QNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqemmmvDLEERLKKEEKTRQeleKAK 1070
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYK-----------ELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1071 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ--AVLARGDEEVAQKNnalKQLRELQAQLAELQEDLESEKAARN 1148
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKK---SRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1149 KAEKLK---RDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQL 1225
Cdd:PRK01156 371 SIESLKkkiEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1226 ------------------EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA-QLQEVMARFSEGEK 1286
Cdd:PRK01156 447 emlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1287 VKGELADRTHKIQTeldnvsclLEDAEKKGIKLTKDVSSLEsqlqdtQELLQEETRQKLNLSSRIRQLEEEknnlleqqe 1366
Cdd:PRK01156 527 ARADLEDIKIKINE--------LKDKHDKYEEIKNRYKSLK------LEDLDSKRTSWLNALAVISLIDIE--------- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1367 eeeesrknlekqlaTLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNrlqqELDDLM 1446
Cdd:PRK01156 584 --------------TNRSRSNEIKKQLND---LESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN----EIQENK 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1447 VDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEaearekdtkalSMARALDEALEAKEEFERLNKQLRAEM 1526
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK-----------KSRKALDDAKANRARLESTIEILRTRI 711
|
650 660
....*....|....*....|....
gi 528481571 1527 EDLISSKDDVGKNVHELEKSKRTL 1550
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKKAI 735
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1135-1395 |
1.83e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1135 ELQEDLESEK--AARNKAEKLK-RDLSEELEALKTELEDTLDTTAAQQ----ELRSKREQEVAELKKAIDD---ETRNHE 1204
Cdd:PHA02562 154 KLVEDLLDISvlSEMDKLNKDKiRELNQQIQTLDMKIDHIQQQIKTYNknieEQRKKNGENIARKQNKYDElveEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1205 SQIqemrqrhgtalEEISEQLEqakrvkgNLEKNKQTLESDNKELTNEvkslqQAKSESEHKRKKLEAQLQE-------V 1277
Cdd:PHA02562 234 AEI-----------EELTDELL-------NLVMDIEDPSAALNKLNTA-----AAKIKSKIEQFQKVIKMYEkggvcptC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1278 MARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI---KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1354
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDefnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 528481571 1355 EEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLED 1395
Cdd:PHA02562 371 QAE--------------FVDNAEELAKLQDELDKIVKTKSE 397
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1483-1925 |
1.97e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1483 ERDRAEAEAREKDTKALsmARALDEALEAKEEFERLNKQLRAEMEDLisskdDVGKNVHELEKSKRTLEQQVEEMRTQLE 1562
Cdd:COG4717 77 EEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1563 ELEDELQATEDaklrLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1642
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1643 EAQIEA-ANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEK--------------KLKSLEAEILQLQE 1707
Cdd:COG4717 226 EEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1708 DLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELA 1787
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1788 GERSAAQKSEnARQQLERQNKDLKSKLQELEGSVKSKFKA-SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKe 1866
Cdd:COG4717 386 ELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELE- 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1867 vfmQVEDERRHADQYKEQmekansrmKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1925
Cdd:COG4717 464 ---QLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
932-1572 |
2.11e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 932 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaarQKLQLEKVTAEA-------KIKKMEEDILLLE 1004
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---------QINDLEDVADKAisnddpeEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1005 DQNSKFLKEKKLLEDRVGEM-TSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1083
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1084 IAELQAQIDelkiqlAKKEEELQAVLARGDEE---VAQKNNalkqlrelqaqlaelqedlESEKAARNKAEKLKRDLSEE 1160
Cdd:TIGR01612 1263 ENEMGIEMD------IKAEMETFNISHDDDKDhhiISKKHD-------------------ENISDIREKSLKIIEDFSEE 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1161 --LEALKTELEDTLDTTAAQQELRSKREQEVAELK--------KAIDDETRNHESQIQEMRQRHGTALEEiSEQLEQAKR 1230
Cdd:TIGR01612 1318 sdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYnilklnkiKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLIKKIK 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1231 VKGNLEKNKQTLES--DNKELTNEVKSLQQAKSEsehkrkkleaqlqevmarfsegekvkgeladrthkIQTELDNVSCL 1308
Cdd:TIGR01612 1397 DDINLEECKSKIEStlDDKDIDECIKKIKELKNH-----------------------------------ILSEESNIDTY 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1309 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQlatlqaqlv 1387
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNdHDFNINELKEHIDKSKGCKDEADKNAKAIEKN--------- 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1388 etkkkleddvgaleglEEVKRKLQKDMEVTSQKLEEKAIAfDKLEKTKNRLQQELDDLMvdlDHQRQIVSNLEKKQKKFD 1467
Cdd:TIGR01612 1513 ----------------KELFEQYKKDVTELLNKYSALAIK-NKFAKTKKDSEIIIKEIK---DAHKKFILEAEKSEQKIK 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1468 QMLAEEKTISARYAEERDRAEA------EAREKDTKALSMARALDEALEAKEEFERLNKQLRA----EMEDLISSKDDVG 1537
Cdd:TIGR01612 1573 EIKKEKFRIEDDAAKNDKSNKAaidiqlSLENFENKFLKISDIKKKINDCLKETESIEKKISSfsidSQDTELKENGDNL 1652
|
650 660 670
....*....|....*....|....*....|....*
gi 528481571 1538 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1572
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1484-1749 |
2.85e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1484 RDRAEAEAREKDTKALSMARALDEA---LEAKEEFERLNKQLRAEMEdlISSKDDVGKnvhELEKSKRTLEQQVEEMRTQ 1560
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEAldkLRSYLPKLNPLREEKKKVS--VKSLEELIK---DVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1561 LEELEDELQATEDAKLRLEVnmqaMKAqFDRDLQARDEQ----------NEEKKRALVKQVREMEAELEDERKQRALAVA 1630
Cdd:PRK05771 109 ISELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1631 AKKKlemdlkdveaqieaanKARDEAIKQLRKLqaqmkDYQR-ELEEARTSRDEIftqsKENEKKLKSLEAEILQLQEDL 1709
Cdd:PRK05771 184 VVLK----------------ELSDEVEEELKKL-----GFERlELEEEGTPSELI----REIKEELEEIEKERESLLEEL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528481571 1710 ASSerarrhaeqeRDELADEISNSasgKAALLDEKRRLEA 1749
Cdd:PRK05771 239 KEL----------AKKYLEELLAL---YEYLEIELERAEA 265
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
875-1896 |
2.95e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 875 IKVKERQVKVENELVEMERKHQQLLEEKNILAEQLqAETELFAEAEEMRAR---LVAKKQELEEILHD--------LESR 943
Cdd:TIGR01612 605 LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQVPEHLKNKdkiYSTIKSELSKIYEDdidalyneLSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 944 VEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlekvtaeAKIKKMEEDILLLEDQNSKFLKEKklLEDRVGE 1023
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKIDKEY---------------------DKIQNMETATVELHLSNIENKKNE--LLDIIVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1024 MTSQLAEE--EEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAelqaqIDELKIQLAK- 1100
Cdd:TIGR01612 741 IKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-----IDNIKDEDAKq 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1101 ---KEEELQAVLARGDEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDtldttaa 1177
Cdd:TIGR01612 812 nydKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD------- 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1178 qqELRSKREQEVAELKKAIDDETRNHESQIQEMrqrhgTALEEISEQLEQAKRVKGNLEK--NKQTL--ESDNKEL---- 1249
Cdd:TIGR01612 883 --DKLNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTLKKVDEYIKICENTKESIEKfhNKQNIlkEILNKNIdtik 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1250 -TNEVK---------SLQQAKSESEHKRKKL-----EAQLQEVMARFSEGEKVKGElaDRTHKIQTELDNVSCLLEDAEK 1314
Cdd:TIGR01612 956 eSNLIEksykdkfdnTLIDKINELDKAFKDAslndyEAKNNELIKYFNDLKANLGK--NKENMLYHQFDEKEKATNDIEQ 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1315 KGIKLTKDVSS---------------LESQLQDTQELLQEETRQKLNLS----SRIRQ----------LEEEKNNLLEQQ 1365
Cdd:TIGR01612 1034 KIEDANKNIPNieiaihtsiyniideIEKEIGKNIELLNKEILEEAEINitnfNEIKEklkhynfddfGKEENIKYADEI 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1366 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVgaleglEEVKRKLQKDMEVTsqkleEKAIAFDKLEKTKNRLQqeldDL 1445
Cdd:TIGR01612 1114 NKIKDDIKNLDQKIDHHIKALEEIKKKSENYI------DEIKAQINDLEDVA-----DKAISNDDPEEIEKKIE----NI 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1446 MVDLDHQRQIVSNLEK------KQKKFDQMLAEEKTISARYAE-------ERDRAEAEAREKDTKAL-SMARALDEALEA 1511
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGINLSYGKnlgklflEKIDEEKKKSEHMIKAMeAYIEDLDEIKEK 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1512 KEEFER---LNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNM-QAMKA 1587
Cdd:TIGR01612 1259 SPEIENemgIEMDIKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLlDAQKH 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1588 QFDRDLQARDEQN------EEKKRALVKQVREMEAELEDERKQ------RALAVAAKKKLEMDLKDVEAQIEAA--NKAR 1653
Cdd:TIGR01612 1338 NSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDDINLEECKSKIESTldDKDI 1417
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1654 DEAIKQLRKLQAQMkdyqreLEEaRTSRDEIFTQSKENEKKL----KSLE------AEILQLQEDLASSERARRHAE-QE 1722
Cdd:TIGR01612 1418 DECIKKIKELKNHI------LSE-ESNIDTYFKNADENNENVlllfKNIEmadnksQHILKIKKDNATNDHDFNINElKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1723 RDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN--DRFRKTTMQVD----------TLNTELAGER 1790
Cdd:TIGR01612 1491 HIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNkfAKTKKDSEIIIkeikdahkkfILEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1791 SAAQKSENARQQLERQNKDLKSK----LQELEGSVKSKFkASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK--- 1863
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKNDKSNKaaidIQLSLENFENKF-LKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKeng 1649
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 528481571 1864 -----LKEVFMQVEDERRHADQYKEQMEKANSRMKQLK 1896
Cdd:TIGR01612 1650 dnlnsLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1653-1818 |
2.96e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1653 RDEAIKQLRKLQAQMKDyQRELEEARTSrdeiftqskenekklkSLEAEILQLQEDLASSERARRHAEQERDELADEISn 1732
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1733 SASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS 1812
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
|
170
....*....|....
gi 528481571 1813 KL--------QELE 1818
Cdd:PRK09039 180 RLnvalaqrvQELN 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
987-1191 |
3.44e-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: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 987 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQEL 1066
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL---QAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1067 EKAKRK--------------LDAETTD-----------LQDQIAELQAQIDELKIQLAKKEEELQAVLArgdEEVAQKNN 1121
Cdd:COG3883 89 GERARAlyrsggsvsyldvlLGSESFSdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLA---ELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1122 ALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1191
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1400-1897 |
3.45e-05 |
|
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: 48.98 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1400 LEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK-KQKKFD--QMLAEEKTI 1476
Cdd:pfam07111 75 LRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEgSQRELEeiQRLHQEQLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1477 SARYAEERDRA----EAEAREKDTKALSMARA--LDEALEAKEEFERLNKQLRAEMEDLISS------------------ 1532
Cdd:pfam07111 155 SLTQAHEEALSsltsKAEGLEKSLNSLETKRAgeAKQLAEAQKEAELLRKQLSKTQEELEAQvtlveslrkyvgeqvppe 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1533 ---------KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEK 1603
Cdd:pfam07111 235 vhsqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1604 KRALVKQVREMEAELEDERKQRALAVAAKKK-----------LEMDLKDVEAQIEA--------------ANKAR----- 1653
Cdd:pfam07111 315 VFALMVQLKAQDLEHRDSVKQLRGQVAELQEqvtsqsqeqaiLQRALQDKAAEVEVermsakglqmelsrAQEARrrqqq 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1654 --DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL----------KSLEAEILQLQEDLASSERARRHAEQ 1721
Cdd:pfam07111 395 qtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQESCPPPPPAPP 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1722 ERDELADEISNSASGKAALlDEKRRLEARIAQLEEELEEEQSNMELLndRFRKTTMQVDT---------------LNTEL 1786
Cdd:pfam07111 475 VDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAERQ--QLSEVAQQLEQelqraqeslasvgqqLEVAR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1787 AGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqlEEQLEQEAKERAAANKIVRRT--EKKL 1864
Cdd:pfam07111 552 QGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAtqEKER 628
|
570 580 590
....*....|....*....|....*....|...
gi 528481571 1865 KEVFMQVEDERRhadqyKEQMEKANSRMKQLKR 1897
Cdd:pfam07111 629 NQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
864-1232 |
3.48e-05 |
|
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: 48.98 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 864 EEEMQAKDEELIKVKERQV----KVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRAR--------LVAKKQ 931
Cdd:pfam09731 51 LGEDPPLAPKPKTFRPLQPsvvsAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE--KEATKDAAEakaqlpksEQEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 932 ELEEILHDLESRVEEEEERNQSLQNEKKK-MQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEDILLLEDQNSK 1009
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQaVKAHTDSLKEASDTAEISREKaTDSALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1010 FLKEKKLLEDRVGEMTS----QLAEEEEKAKNLGKVKNKqemmMVDLEErlKKEEKTRQELEK--------AKRKLDAET 1077
Cdd:pfam09731 209 AAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQQELVSifpdiipvLKEDNLLSN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1078 TDLQDQIAELQAQIDELKIQLA--KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLA--ELQEDLESEKAARNKAEKL 1153
Cdd:pfam09731 283 DDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRESY 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1154 KRDLSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNHESQIQEMRQRHG---TALEEISEQLEQAKR 1230
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRK 441
|
..
gi 528481571 1231 VK 1232
Cdd:pfam09731 442 AQ 443
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
862-1282 |
3.71e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 862 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL------LEEKNILAEQLQAETE-LFAEAEEMRARLVAKKQELE 934
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksIESLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 935 EILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDillledqnskFLKEK 1014
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINH----------YNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1015 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVD-LEERLKKEEKTRQELEKAKRKLdAETTDLQDQIAELQAQIDE 1093
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKS 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1094 LKIQL--AKKEEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE 1167
Cdd:PRK01156 558 LKLEDldSKRTSWLNALAVISLIDIetnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1168 LEDTLDTTAAQQELRSKRE---QEVAElKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLES 1244
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDnykKQIAE-IDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRARLESTIEILRT 709
|
410 420 430
....*....|....*....|....*....|....*...
gi 528481571 1245 DNKELTNEVKSLQQaKSESEHKRKKLEAQLQEVMARFS 1282
Cdd:PRK01156 710 RINELSDRINDINE-TLESMKKIKKAIGDLKRLREAFD 746
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
858-1089 |
3.80e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 858 LQVTRQE------EEMQAKDEELIKVKERQVKVENELVEMERkhqqlleeknILAEQLQAETELFAEAEEMRARlvakkq 931
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEMEQ----------IRAEQEEARQREVRRLEEERAR------ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 932 ELEEI-LHDLESRVEEEEERNQSLQNEKKKMQshIQDLEEQLDEEEAARQKLqLEKVTAEAKIKKMEEDillledqnskf 1010
Cdd:pfam17380 447 EMERVrLEEQERQQQVERLRQQEEERKRKKLE--LEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEE----------- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1011 lKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEM---MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAEL 1087
Cdd:pfam17380 513 -RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeerRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
..
gi 528481571 1088 QA 1089
Cdd:pfam17380 592 EA 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1405-1656 |
3.90e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1405 EVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisaryaeER 1484
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1485 DRAEAEAREKDTKALsMARALDEAleakeefERLNKQLRAEMedLISSKDdvgknVHELEKSKRTLEQQVEEMRTQLEEL 1564
Cdd:COG4942 91 EIAELRAELEAQKEE-LAELLRAL-------YRLGRQPPLAL--LLSPED-----FLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1565 E---DELQATEdaklrlevnmQAMKAQFDRDLQARDEQNEEKKR--ALVKQVREMEAELEDERKQRALAVAAKKKLEMDL 1639
Cdd:COG4942 156 RadlAELAALR----------AELEAERAELEALLAELEEERAAleALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*..
gi 528481571 1640 KDVEAQIEAANKARDEA 1656
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1197-1427 |
4.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1197 DDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQE 1276
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1277 VmarFSEGEKVK-----------GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqkl 1345
Cdd:COG3883 95 L---YRSGGSVSyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1346 nLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKA 1425
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
..
gi 528481571 1426 IA 1427
Cdd:COG3883 245 SA 246
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
993-1220 |
4.77e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 993 IKKMEEDILLLE-------DQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQE 1065
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE-EQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1066 LEKA-KRKLDAETTDLQDQIAELQAQIDELKIQLA--KKEEELQAVLargdeevaQKNNAL--KQLRELQAQLAELQEDL 1140
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKL--------EKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1141 esekaarNKAEKLKRD-LSEELEalktELEDTLDTTAAQ-----------QELRSKREQEVAELKKAiddETRNHESQIQ 1208
Cdd:PLN02939 288 -------SKLSPLQYDcWWEKVE----NLQDLLDRATNQvekaalvldqnQDLRDKVDKLEASLKEA---NVSKFSSYKV 353
|
250
....*....|..
gi 528481571 1209 EMRQRHGTALEE 1220
Cdd:PLN02939 354 ELLQQKLKLLEE 365
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
992-1306 |
5.67e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 992 KIKKMEEDILLLEDQNSK--FLKEKKLL----------EDRVGEMTSQLAE----EEEKAKNLGKVKNKQEMMMVD---- 1051
Cdd:PRK04778 80 SLPDIEEQLFEAEELNDKfrFRKAKHEIneieslldliEEDIEQILEELQEllesEEKNREEVEQLKDLYRELRKSllan 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1052 ----------LEERLKKEEKTRQELEKAK------------RKLDAETTDLQDQIA-----------ELQAQIDELKIQL 1098
Cdd:PRK04778 160 rfsfgpaldeLEKQLENLEEEFSQFVELTesgdyveareilDQLEEELAALEQIMEeipellkelqtELPDQLQELKAGY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1099 AKKEEE--------LQAVLARGDEEVAQKNNALKQLR--ELQAQLAELQED-------LESEKAARNKAEKLKRDLSEEL 1161
Cdd:PRK04778 240 RELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDldEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1162 EALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---IDDETRNHE---SQIQEMrqrhgtaLEEISEQL 1225
Cdd:PRK04778 320 EHAKEQNKELKEEIDrvkqsytlNESELESVRqlEKQLESLEKQydeITERIAEQEiaySELQEE-------LEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1226 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKL----------------EAQLQEVMARFSEG----E 1285
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSnlpglpedylemffevSDEIEALAEELEEKpinmE 472
|
410 420
....*....|....*....|.
gi 528481571 1286 KVKGELadrtHKIQTELDNVS 1306
Cdd:PRK04778 473 AVNRLL----EEATEDVETLE 489
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1309-1514 |
6.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1309 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVE 1388
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1389 TKKKLEDDVGAL----------------EGLEEVKRK---LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDL 1449
Cdd:COG3883 84 RREELGERARALyrsggsvsyldvllgsESFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1450 DHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEE 1514
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1090-1258 |
6.93e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.93 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1090 QIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELqaqLAELQEDLESEKAARNKAEKLKrdlSEELEALKTELE 1169
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDCD---PTELDRAKEKLK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1170 DTLDTTAAQQELRSKREQEVAELKKAIDDETrnhesqiqemrqrhgtalEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1249
Cdd:smart00787 215 KLLQEIMIKVKKLEELEEELQELESKIEDLT------------------NKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
|
....*....
gi 528481571 1250 TNEVKSLQQ 1258
Cdd:smart00787 277 KEQLKLLQS 285
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1118-1421 |
7.99e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1118 QKNNALKQLRELQA-QLAELQEDLESEKAarNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEVAELKKAI 1196
Cdd:PRK05771 17 YKDEVLEALHELGVvHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLP------KLNPLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1197 DDetrnhesqiqemrqrhgtaLEEISEQLEqaKRVKGnleknkqtLESDNKELTNEVKSLQQAKSESEhkrkKLEAqLQE 1276
Cdd:PRK05771 89 KD-------------------VEEELEKIE--KEIKE--------LEEEISELENEIKELEQEIERLE----PWGN-FDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1277 VMARFSEGEKVKGELAdRTHKIQTE----LDNVSCLLEDAEKKG------IKLTKDVSSLESQLQDTqELLQEETRQKLN 1346
Cdd:PRK05771 135 DLSLLLGFKYVSVFVG-TVPEDKLEelklESDVENVEYISTDKGyvyvvvVVLKELSDEVEEELKKL-GFERLELEEEGT 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1347 LSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGL--EEVKRKLQKDMEVTSQKL 1421
Cdd:PRK05771 213 PSELIREIKEEL--------------EEIEKERESLLEELKELAKKYLEELLALYEYleIELERAEALSKFLKTDKT 275
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1452-1943 |
8.14e-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: 48.04 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1452 QRQIVSNLEKKQKkFDQMLAEEKTISAryaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIS 1531
Cdd:TIGR00618 165 KKELLMNLFPLDQ-YTQLALMEFAKKK---SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1532 SKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrDLQARDEQNEEKKRALVKQV 1611
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA---AHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1612 REMEAELEDERKQRALAVAAKKKLEmdlkdveaqieaankardEAIKQLRKLQAQMKDYQRELEEArTSRDEIFTQSKEN 1691
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIE------------------EQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1692 EKKLKSLEA--EILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN 1769
Cdd:TIGR00618 378 TQHIHTLQQqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1770 DRFRKTTMQvdtlntELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSvKSKFKASIAALEAKILQLEEQLEQEAKE 1849
Cdd:TIGR00618 458 KIHLQESAQ------SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1850 RAAANKiVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeaeeeATRANASRRKLQRELDDATEASEG 1929
Cdd:TIGR00618 531 QRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....
gi 528481571 1930 LSREVNTLKNRLRR 1943
Cdd:TIGR00618 603 LSEAEDMLACEQHA 616
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1153-1283 |
8.40e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1153 LKRDLSEELEALKTELEDTLDttAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtalEEISEQLEQAKRVK 1232
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR-------NELQKLEKRLLQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 528481571 1233 GNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1283
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1049-1145 |
8.80e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1049 MVDLEERLKKEEKTRQELEKAKRKLDAET-TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNnalkQLR 1127
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG----KIP 488
|
90
....*....|....*...
gi 528481571 1128 ELQAQLAELQEDLESEKA 1145
Cdd:COG0542 489 ELEKELAELEEELAELAP 506
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1123-1467 |
8.81e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1123 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTaaQQELRSKREQEVAELKKAIDDETRN 1202
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1203 HESQIQEMRQRHGtalEEISEQLEQAKRVKgNLEKNKQtlesdnKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfs 1282
Cdd:pfam17380 379 ELERLQMERQQKN---ERVRQELEAARKVK-ILEEERQ------RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1283 EGEKVKGELADRTHKIQTELDnvscllEDAEKKGIKLTKDvsslesqlqdtqellQEETRQKLnlssrirqLEEEKnnll 1362
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQ------QEEERKRKKLELE---------------KEKRDRKR--------AEEQR---- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1363 eqqeeeeesRKNLEKQLATLQAQLVETKKK-------LEDDVGALegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK 1435
Cdd:pfam17380 494 ---------RKILEKELEERKQAMIEEERKrkllekeMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
330 340 350
....*....|....*....|....*....|..
gi 528481571 1436 NRlQQELDDLMVDLDHQRQIVSNlEKKQKKFD 1467
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVES-EKARAEYE 592
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1498-1739 |
9.50e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1498 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtleQQVEEMRTQLEELEDELQATEDAKLR 1577
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1578 LEVNMQAMKAQFDRdlQARDEQNEEKKRALVKQVreMEAELEDERKQRALAV-----AAKKKLEmDLKDVEAQIEAANKA 1652
Cdd:COG3883 77 AEAEIEERREELGE--RARALYRSGGSVSYLDVL--LGSESFSDFLDRLSALskiadADADLLE-ELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1653 RDEAIKQLRKLQAQMKDYQRELEeartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISN 1732
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE----------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
....*..
gi 528481571 1733 SASGKAA 1739
Cdd:COG3883 222 AAAAAAA 228
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1085-1339 |
9.55e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1085 AELQAQIDELKiqlakKEEELQAvlargDEEVAQKNnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1164
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQD--LEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1165 KTELEDTLDTTAAQQELRSkREQEVAELkkaiddetrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEs 1244
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQ-LESRLAQT-----------LDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1245 dnkELTNEVKSLQQAKSESEHKRK-KLEAQLQEVMARFSEGekvkgeladrthkiQTELDNVSCLLEDAEKKGIKLTKDV 1323
Cdd:PRK11281 174 ---QIRNLLKGGKVGGKALRPSQRvLLQAEQALLNAQNDLQ--------------RKSLEGNTQLQDLLQKQRDYLTARI 236
|
250
....*....|....*.
gi 528481571 1324 SSLESQLQDTQELLQE 1339
Cdd:PRK11281 237 QRLEHQLQLLQEAINS 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1482-1709 |
9.55e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1482 EERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL 1561
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1562 EELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDeQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKD 1641
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRA-ELKE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1642 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDL 1709
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1598-1721 |
1.03e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.83 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1598 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE------------AANKARDEAIKQLRKLQA 1665
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaaltkGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1666 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQ 1721
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1080-1727 |
1.16e-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: 47.12 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1080 LQDQIAELQAQIDELKIQLAKKEEELQAVLargdeevaqknNALKQLRElqaqlAELQEDLESEKAARNKAEKLK---RD 1156
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTFWS-----PELKKERALRKEEAARISVLKeqyRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1157 LSEELEALKTELEDTLDTTAAQQELRSKREQEV------AELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQakr 1230
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1231 VKGNLEKNKQTLESDNKELTN-----EVKSLQQAKSESEHKRKK----LEAQLQEVMARFSEGEKVKGELADRTHK---I 1298
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKllemlQSKGLPKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREELHRrnqL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1299 QTELDNVSCLLEDAEKKGIKltkdVSSLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKN-----NLLEQQEEEE 1369
Cdd:pfam10174 222 QPDPAKTKALQTVIEMKDTK----ISSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKShskfmKNKIDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1370 ESRKN-----LEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1444
Cdd:pfam10174 298 LSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1445 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMArALDEALEAKEE-FERLN 1519
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1520 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ------ATEDAKLR-LEVNMQAMKAQFDR- 1591
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSKl 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1592 DLQARDEQNEE----KKRALVKQVREMEAELEDERKQRALAVA-------AKKKLEMDLKDVEAQIEAANKARDEAIKQL 1660
Cdd:pfam10174 537 ENQLKKAHNAEeavrTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMKEQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1661 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKlkslEAEILQLQEDLASSERARRHAEQERDELA 1727
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
991-1271 |
1.17e-04 |
|
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: 47.46 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 991 AKIKKMEEDILLLEDqnskFLKEKKLLEDRVGEMTSQLAEEEEKAkNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKak 1070
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEK-- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1071 rKLDAETTDLQDQIAELQA--QIDELkIQLAKKEEElqavlaRGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARN 1148
Cdd:pfam18971 636 -KLESKSGNKNKMEAKAQAnsQKDEI-FALINKEAN------RDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFD 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1149 KAEKLK-RDLS---EELEALKTELED----------TLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqeMRQRH 1214
Cdd:pfam18971 708 EFKNGKnKDFSkaeETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI--INQKV 785
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1215 GTALEEISEQLEQAKRVkGNLEKNKQTLeSDNKELTNEVKSLQQAKSESEHKRKKLE 1271
Cdd:pfam18971 786 TDKVDNLNQAVSVAKAM-GDFSRVEQVL-ADLKNFSKEQLAQQAQKNEDFNTGKNSE 840
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1009-1445 |
1.32e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.77 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1009 KFLKEKKLLEDRVGEMTSQ-LAEEEEKAKNLGkvknkqemMMVDLEERLKKEEKTRQELEkakrklDAETTDLQDQIAEL 1087
Cdd:pfam06160 7 KIYKEIDELEERKNELMNLpVQEELSKVKKLN--------LTGETQEKFEEWRKKWDDIV------TKSLPDIEELLFEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1088 QAQIDELKIQLAKKE-EELQAVLARGDEEVAQKNNALKQLrelqaqlaelqedLESEKAARNKAEKLK---RDLSEELEA 1163
Cdd:pfam06160 73 EELNDKYRFKKAKKAlDEIEELLDDIEEDIKQILEELDEL-------------LESEEKNREEVEELKdkyRELRKTLLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1164 LKTELEDTLDTTAAQ-QELRSKREQEVaELKKAID-DETRNHESQIQEMrqrhgtaLEEISEQLEqakRVKGNLEKNKQT 1241
Cdd:pfam06160 140 NRFSYGPAIDELEKQlAEIEEEFSQFE-ELTESGDyLEAREVLEKLEEE-------TDALEELME---DIPPLYEELKTE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1242 LESDNKELTNEVKSLQQAKSESEH-----KRKKLEAQLQEVMARFSEGE--KVKGELADrthkIQTELDNVSCLLE---D 1311
Cdd:pfam06160 209 LPDQLEELKEGYREMEEEGYALEHlnvdkEIQQLEEQLEENLALLENLEldEAEEALEE----IEERIDQLYDLLEkevD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1312 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQkLNLSSRIRQLEEEKNnlleqqeeeeesrKNLEKQLATLQAQLVETKK 1391
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELER-VQQSYTLNENELERV-------------RGLEKQLEELEKRYDEIVE 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1392 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1445
Cdd:pfam06160 351 RLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEF 404
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1640-1836 |
1.43e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1640 KDVEAQIEAANKARDeaikqlrkLQAQMKDYQRELEEARTSRDEIFTQSKENE---KKLKSLEAEILQLQEDLASSERAr 1716
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1717 rhaeqerdelADEISNSASGKAALldekRRLEARIAQLEEELEEEQSNMELLNDrfrkttmQVDTLNTelAGERSAAQKS 1796
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQNDLAEYNS-------QLVSLQT--QPERAQAALY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528481571 1797 ENAR--QQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKI 1836
Cdd:PRK11281 167 ANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1419-1943 |
1.47e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1419 QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKD 1495
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1496 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR-----------------TLEQQVEEMR 1558
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1559 TQLEELEDELQATEDAKLRLEVnMQAMKAQFDRDLQARDEQN---------EEKKRALVKQVREMEAELEDERKQR---- 1625
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilelegyEMDYNSYLKSIESLKKKIEEYSKNIerms 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1626 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQS----------------- 1688
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhi 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1689 -KENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1767
Cdd:PRK01156 471 iNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1768 LNDRFRKTTMQ-VDTLNTELAgeRSAAQKS----ENARQQLERQNK---DLKSKLQELEGS---VKSKFKASIAALEAKI 1836
Cdd:PRK01156 551 IKNRYKSLKLEdLDSKRTSWL--NALAVISlidiETNRSRSNEIKKqlnDLESRLQEIEIGfpdDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1837 LQLEEQLEQEAKERAAANKIvRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEeaeeeatRANASRRKL 1916
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-------DAKANRARL 700
|
570 580
....*....|....*....|....*..
gi 528481571 1917 QRELDDATEASEGLSREVNTLKNRLRR 1943
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLES 727
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1478-1797 |
1.49e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1478 ARYAEERDRaEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1557
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1558 RTQLEELEDELQATEDAKLRLEVNMQAMKaqfdrdlqardeqneEKKRALVKQVREMEAElederkqralavaaKKKLEM 1637
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAE--------------RKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1638 DLKDVEAQIEAANKardeAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERArr 1717
Cdd:pfam07888 179 KLQQTEEELRSLSK----EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1718 hAEQERDELADEISNSASGKAALldEKRRLEAR----------------IAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1781
Cdd:pfam07888 253 -VEGLGEELSSMAAQRDRTQAEL--HQARLQAAqltlqladaslalregRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330
....*....|....*.
gi 528481571 1782 LNTELAGERSAAQKSE 1797
Cdd:pfam07888 330 LEERLQEERMEREKLE 345
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1642-1896 |
1.75e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1642 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFT--QSKENEKKLKSLEAEILQLQEDLASSERARRHA 1719
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1720 EQERDELADEISNSASGKAAlldekRRLEARIAQleeeleeeqsnmellndrfrkttmqvdtLNTELAGERSAAQKSENA 1799
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVI-----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1800 RQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqleeqleqeakerAAANKIVRRTEKKLKEvFMQVEDE----R 1875
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQARE--------------ASLQAQLAQLEARLAE-LPELEAElrrlE 357
|
250 260
....*....|....*....|.
gi 528481571 1876 RHADQYKEQMEKANSRMKQLK 1896
Cdd:COG3206 358 REVEVARELYESLLQRLEEAR 378
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1500-1853 |
1.92e-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: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1500 SMARALDEALEAKEEFERLNKQLRAEMEDLISSKddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLe 1579
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELPQAK----SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1580 vnmQAMKAQFDRDLQARDEQNEEKK---RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEA 1656
Cdd:pfam19220 89 ---VARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1657 IKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASS----ERARRHAEQERDELADEISN 1732
Cdd:pfam19220 166 RERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEqaerERAEAQLEEAVEAHRAERAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1733 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQ------ 1806
Cdd:pfam19220 246 LRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraelee 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1807 -----NKDLKSKLQELEGSVKS-------------KFKASIAALEAKILQLEEQLEQEAKERAAA 1853
Cdd:pfam19220 326 raemlTKALAAKDAALERAEERiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
927-1109 |
1.97e-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: 44.92 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 927 VAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1006
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1007 NSKFLKEKklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1086
Cdd:COG1579 82 LGNVRNNK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|...
gi 528481571 1087 LQAQIDELKIQLAKKEEELQAVL 1109
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPEL 176
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1412-1656 |
2.12e-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: 46.75 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1412 KDMEVTSQKLEEKAIAfdklEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKTISAryaeERDRAEAEA 1491
Cdd:NF012221 1552 KQDDAAQNALADKERA----EADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1492 REKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIssKDDVGKnvhELEKSKRTLEQQVEEMRTQLE----ELEDE 1567
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQE---QLDDAKKISGKQLADAKQRHVdnqqKVKDA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1568 LQATEDAKLRLEVNMQAMKAQFDrdlQARDEQNEEKKRALVKQVREMEAElederkQRALAVAAKKKLEMDlKDVEAQIE 1647
Cdd:NF012221 1691 VAKSEAGVAQGEQNQANAEQDID---DAKADAEKRKDDALAKQNEAQQAE------SDANAAANDAQSRGE-QDASAAEN 1760
|
....*....
gi 528481571 1648 AANKARDEA 1656
Cdd:NF012221 1761 KANQAQADA 1769
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1590-1713 |
2.23e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1590 DRDLQARDEQNEEKKRALVKQVREMEAELEDE---RKQRALAVAAKKKLEMDLKDVEAQIEAANK------ARDEAIKQL 1660
Cdd:COG1566 78 PTDLQAALAQAEAQLAAAEAQLARLEAELGAEaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqqELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 528481571 1661 RKLQAQMKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAEILQLQEDLASSE 1713
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREE-EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1073-1227 |
2.31e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1073 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEK 1152
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDL----QDSVANLRASLSAAEAERSRLQALLAELA---GAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1153 LKRDLSEELEALKTELEDTLDTTAA-QQELRSKREQeVAELKKAIDD-ETRNHESQ--IQEMRQRHGTALEEISEQLEQ 1227
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDAsEKRDRESQakIADLGRRLNVALAQRVQELNR 194
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1371-1579 |
2.41e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 45.98 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1371 SRKNLEKQLATLQAQ------LVETKKKLEDDVgalEGLEEVKRK--LQK-DMEVTSQKLEEKaiafdkLEKTKNRLQQE 1441
Cdd:pfam15066 340 SNLYLEKKVKELQMKitkqqvFVDIINKLKENV---EELIEDKYNviLEKnDINKTLQNLQEI------LANTQKHLQES 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1442 lddlmvdldhqrqivsnleKKQKKFDQMlaEEKTISARYAEERDRAEAEAREKDtKALSMARALDEALEAKE-EFERLnK 1520
Cdd:pfam15066 411 -------------------RKEKETLQL--ELKKIKVNYVHLQERYITEMQQKN-KSVSQCLEMDKTLSKKEeEVERL-Q 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1521 QLRAEMEDLISSKDDVgknvheLEKSKRTLEQQVEEMRTQLEELEDE-LQATEDAKLRLE 1579
Cdd:pfam15066 468 QLKGELEKATTSALDL------LKREKETREQEFLSLQEEFQKHEKEnLEERQKLKSRLE 521
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
859-1338 |
2.53e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 859 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLVAKKQELEE 935
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 936 IlHDLESRVeeeeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKL-QLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1014
Cdd:pfam05557 199 I-PELEKEL-------ERLREHNKHLNENIENKLLLKEEVEDLKRKLeREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1015 KLLEDRVGE-MTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDE 1093
Cdd:pfam05557 271 TGLNLRSPEdLSRRIEQLQQREIVLKEENS-------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1094 L--KIQLAKKEEE-LQAVLARGDEEVAQKN---NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTE 1167
Cdd:pfam05557 344 LqrRVLLLTKERDgYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1168 LedTLDTTAAQQELRSKREQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEqakrvkgnLEKNKQTLESDNK 1247
Cdd:pfam05557 424 L--QALRQQESLADPSYSKEEVDSLRRKLET--------LELERQR----LREQKNELE--------MELERRCLQGDYD 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1248 ELTNEVKSLQQ-AKSESEHKRKKLEAQLQEVMARfsegekvkgeLADRTHKIQTELDNVSCL----LEDAEKKGIKLTKD 1322
Cdd:pfam05557 482 PKKTKVLHLSMnPAAEAYQQRKNQLEKLQAEIER----------LKRLLKKLEDDLEQVLRLpettSTMNFKEVLDLRKE 551
|
490
....*....|....*.
gi 528481571 1323 VSSLESQLQDTQELLQ 1338
Cdd:pfam05557 552 LESAELKNQRLKEVFQ 567
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1632-1813 |
2.61e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1632 KKKLEMDLKDVEAqieAANKARDEAIKQL---------RKLQAQ-MKDYQRELEE----ARTSRDEIFTQSKE-----NE 1692
Cdd:PRK10929 25 EKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEprsvpPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1693 KKLKSLEAEILQLQEDLAssERARRhAEQERDElADEISNSASGKAALLDEKRRL----EARI-AQLEEELEEEQSNMEL 1767
Cdd:PRK10929 102 MSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528481571 1768 LNDRFRKTTMQVDTLntELagersaAQKSENARQQLERQNKDLKSK 1813
Cdd:PRK10929 178 LQAESAALKALVDEL--EL------AQLSANNRQELARLRSELAKK 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1064-1292 |
2.77e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1064 QELEKAKRKLD------AETTDLQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQKNNALkQLRELQAQLAELQ 1137
Cdd:PRK11281 63 QDLEQTLALLDkidrqkEETEQLKQQLAQAPAKLRQAQ-------AELEALKDDNDEETRETLSTL-SLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1138 EDLESekaarnkaekLKRDLSE---ELEALKTELEDtldttaAQQEL--RSKREQEVAELKKAIDDETRNHESQIQEMRQ 1212
Cdd:PRK11281 135 DQLQN----------AQNDLAEynsQLVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1213 RHGTALEEISEQLEQakrvkgNLEKNKQTLESDNKELtnEVKSLQQAKSESE---------HKRKKL------EAQLQEV 1277
Cdd:PRK11281 199 AEQALLNAQNDLQRK------SLEGNTQLQDLLQKQR--DYLTARIQRLEHQlqllqeainSKRLTLsektvqEAQSQDE 270
|
250
....*....|....*
gi 528481571 1278 MARFSEGEKVKGELA 1292
Cdd:PRK11281 271 AARIQANPLVAQELE 285
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1072-1753 |
2.79e-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: 45.97 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1072 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNnalkQLRELQAQLAELQEDLESEKAARNKAE 1151
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHL----REELHRRN----QLQPDPAKTKALQTVIEMKDTKISSLE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1152 KLKRDLSEELEALKTELEdtLDTTAAQQELRSkreqevAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEqakrv 1231
Cdd:pfam10174 247 RNIRDLEDEVQMLKTNGL--LHTEDREEEIKQ------MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLE----- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1232 kgnleknkqTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVkgeLADRTHKIQteldnvsclled 1311
Cdd:pfam10174 314 ---------TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESF---LNKKTKQLQ------------ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1312 aekkgiKLTKDVSSLESQLQDTQELLQEETRqKLNLssrirqleeeknnlleqqeeeeesrknLEKQLATLQAQLVETKK 1391
Cdd:pfam10174 370 ------DLTEEKSTLAGEIRDLKDMLDVKER-KINV---------------------------LQKKIENLQEQLRDKDK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1392 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDlmvDLDHQRQIVSNLEKKQKKFDQMLA 1471
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1472 EEKTISARYAEERDRAEAEAREKDTKALSMARALDealEAKEEFERLNKQLraemedlisskddvgKNVHELEKSKRTLE 1551
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE---QKKEECSKLENQL---------------KKAHNAEEAVRTNP 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1552 QQVEemRTQLEELEDELQATEDAKLRLEVnmqamkaqfDRDLQA-RDEQNEekKRALVKQVREMEAELEDERKQRALAVA 1630
Cdd:pfam10174 555 EIND--RIRLLEQEVARYKEESGKAQAEV---------ERLLGIlREVENE--KNDKDKKIAELESLTLRQMKEQNKKVA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1631 AKKKLEMDLK------DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL- 1703
Cdd:pfam10174 622 NIKHGQQEMKkkgaqlLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRk 701
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 528481571 1704 QLQEDLASSERARRHAEQERDELADEISNSASGK-------AALLDEKRRLEARIAQ 1753
Cdd:pfam10174 702 QLEEILEMKQEALLAAISEKDANIALLELSSSKKkktqeevMALKREKDRLVHQLKQ 758
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1563-1835 |
3.87e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1563 ELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElederkqrALAVAAKKKLEMDLKDV 1642
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAEARAAKDKDAVAA--------ALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1643 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskENEKKlKSLEAEIlqlqedlassERAR-RHAEQ 1721
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAA------------ADPKK-AAVAAAI----------ARAKaKKAAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1722 ErDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmqvdtlnTELAGERSAAQKSENARQ 1801
Cdd:PRK05035 565 Q-AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA---------VAAAIARAKAKKAEQQAN 634
|
250 260 270
....*....|....*....|....*....|....
gi 528481571 1802 QLERQNKDLKsklqelegsvKSKFKASIAALEAK 1835
Cdd:PRK05035 635 AEPEEPVDPR----------KAAVAAAIARAKAR 658
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1470-1626 |
3.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1470 LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED----LISSKDDVGKNVHELEK 1545
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1546 SKRTLEQQVEEMRTQLEELE------DELQATEDAKLRLEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELE 1619
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEkkeeelEELIEEQLQELERISGLTAEEAK----EILLEKVEEEARHEAAVLIKEIEEEAK 183
|
....*..
gi 528481571 1620 DERKQRA 1626
Cdd:PRK12704 184 EEADKKA 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
892-1225 |
4.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 892 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQ--SLQNEKKkmqsHIQDLE 969
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELE----RLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 970 EQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknlgkvknkqemmm 1049
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--------------- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1050 vDLEERLKKEEKTRQELEKAKRkldaettdLQDQIAELQAQIDELKIQLAKKEEELQ----AVLARGDEEVAQKNNALKQ 1125
Cdd:COG4913 750 -LLEERFAAALGDAVERELREN--------LEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLAL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1126 LRELQAQ-LAELQEDLESEKAARNKAEK--LKRDLSEELEALKTELE---DTL------DTTAAQQELRSKREQEVAELK 1193
Cdd:COG4913 821 LDRLEEDgLPEYEERFKELLNENSIEFVadLLSKLRRAIREIKERIDplnDSLkripfgPGRYLRLEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|..
gi 528481571 1194 KAIDDETRNHESQIQEMRQRHGTALEEISEQL 1225
Cdd:COG4913 901 QELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
926-1302 |
4.33e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 926 LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK----------LQLEKVTAEA---- 991
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKylllqkqleqLQEENFRLETardd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 992 ---KIKKMEEDILLLEDQNSKFLK---EKKLLED----------RVGEMTSQLAEEEEKAKNLG----KVKNKQEMMM-- 1049
Cdd:pfam05622 85 yriKCEELEKEVLELQHRNEELTSlaeEAQALKDemdilressdKVKKLEATVETYKKKLEDLGdlrrQVKLLEERNAey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1050 ----VDLEERLKKEEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNN---A 1122
Cdd:pfam05622 165 mqrtLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTlreT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1123 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLseeleaLKTELEDTLdttaaqqeLRSKREQEVAELKKAIDDETRn 1202
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI------MPAEIREKL--------IRLQHENKMLRLGQEGSYRER- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1203 hesqiqemrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE-------SEHKRKKLEAQLQ 1275
Cdd:pfam05622 306 ---------------LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLE 370
|
410 420
....*....|....*....|....*..
gi 528481571 1276 EVMARFSEGEKVKGELADRTHKIQTEL 1302
Cdd:pfam05622 371 KLHEAQSELQKKKEQIEELEPKQDSNL 397
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
958-1339 |
4.39e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 958 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVT----------------------AEAKIKKMEEDILLLEDQNSK--FLKE 1013
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLPVNDELEKVKklnltgqseekfeewrqkwdeiVTNSLPDIEEQLFEAEELNDKfrFRKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1014 KKLLedrvGEMTSQLAEEEEKAKNLgkvknKQEMM-MVDLEERLKKE-EKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1091
Cdd:PRK04778 104 KHEI----NEIESLLDLIEEDIEQI-----LEELQeLLESEEKNREEvEQLKDLYRELRKSLLANRFSFGPALDELEKQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1092 DELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDT 1171
Cdd:PRK04778 175 ENLEEEFSQFVELTES----GDYVEAR-----EILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1172 ---LDTTAAQQELRSKREQeVAELKKAID----DETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEKNKQTLES 1244
Cdd:PRK04778 246 gyhLDHLDIEKEIQDLKEQ-IDENLALLEeldlDEAEEKNEEIQE-------RIDQLYDILEREVKARKYVEKNSDTLPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1245 D-------NKELTNEVKSLQQAK--SESE-HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK 1314
Cdd:PRK04778 318 FlehakeqNKELKEEIDRVKQSYtlNESElESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK 397
|
410 420
....*....|....*....|....*
gi 528481571 1315 KGIKLTKDVSSLESQLQDTQELLQE 1339
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREKLER 422
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1089-1199 |
4.71e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1089 AQIDELKIQLAKKEEELQAVLARGDEEVAQKnnalkqLRELQAQLAELQEDLESEKaARNKAEKlkrDLSEELEALKTEL 1168
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALK-ARWEAEK---ELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 528481571 1169 EDTLDTTAAQQELRSKREQEVAELKKAIDDE 1199
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1591-1800 |
5.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1591 RDLQARDEQNEEKKRALVKQVREMEAELEDerkqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1670
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1671 QRELEEARTSRD--EIFTQSKENEKKLKSLEA----------EILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1738
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESFSDFLDRLSAlskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1739 ALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENAR 1800
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
871-1169 |
5.46e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 871 DEELIKVKERQVKVENELVEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLVAKkqELEEILHDLESRVEE 946
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklRSYLPKLNPLREEKKKVSVKSLEELIK--DVEEELEKIEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 947 EEERNQSLQNEKKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDIllledqnsKFLKEKKLLEDRVGEMTS 1026
Cdd:PRK05771 105 LEEEISELENEIKELEQEIE----------------RLEPW------GNFDLDL--------SLLLGFKYVSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1027 QLAEEEEKAKNLGKV----KNKQEMMMV---------DLEERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDE 1093
Cdd:PRK05771 155 DKLEELKLESDVENVeyisTDKGYVYVVvvvlkelsdEVEEELKKLGFERLELE-EEGTPSELIREIKEELEEIEKERES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1094 LK---IQLAKKEEELQAVLARGDEEVAQKNNALKQLRE------LQA-----QLAELQEDLesEKAARNKAEKLKRDLSE 1159
Cdd:PRK05771 234 LLeelKELAKKYLEELLALYEYLEIELERAEALSKFLKtdktfaIEGwvpedRVKKLKELI--DKATGGSAYVEFVEPDE 311
|
330
....*....|
gi 528481571 1160 ELEALKTELE 1169
Cdd:PRK05771 312 EEEEVPTKLK 321
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1053-1273 |
5.76e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1053 EERLKKEEKTRQEleKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQ 1132
Cdd:PRK05035 459 QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1133 LAELQEDLESEKA-----ARNKAEKLKR-----DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRN 1202
Cdd:PRK05035 537 KQAAAAADPKKAAvaaaiARAKAKKAAQqaanaEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1203 HESQIQEMR-QRHGTALEEISEQLEQAK--RVKGNLEKNK-----QTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1273
Cdd:PRK05035 617 VAAAIARAKaKKAEQQANAEPEEPVDPRkaAVAAAIARAKarkaaQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1056-1356 |
5.86e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1056 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAqlae 1135
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTR---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1136 lQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQElrskreqevaelkkaiddetrNHESQIQEMrQRHg 1215
Cdd:pfam15905 137 -VNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE---------------------GMEGKLQVT-QKN- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1216 taLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLeAQLQEVMArfsegekvkgELADRT 1295
Cdd:pfam15905 193 --LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDI-AQLEELLK----------EKNDEI 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1296 HKIQTELDNVSCLLEdaekkgiKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEE 1356
Cdd:pfam15905 260 ESLKQSLEEKEQELS-------KQIKDLNEKCKLLEsEKEELLREYEEKEQTLNAELEELKE 314
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1017-1101 |
6.80e-04 |
|
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467481 [Multi-domain] Cd Length: 103 Bit Score: 40.99 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1017 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqEMMMVDLEERLK----------KEEKTRQELEKAKRKLDAETTDLQDQIAE 1086
Cdd:cd23165 11 LNARLHELKEELKAKKKELENLEDASD--ELELADDDEPVPykigevfvhlSLEEAQERLEKAKEELEEEIEKLEEEIDE 88
|
90
....*....|....*
gi 528481571 1087 LQAQIDELKIQLAKK 1101
Cdd:cd23165 89 IEEEMKELKVQLYAK 103
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1048-1187 |
6.95e-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: 43.98 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1048 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLR 1127
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLA-------TERSARREAEAELE 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1128 ELQAQLAELQEDLESEKAARnkaEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ 1187
Cdd:pfam09787 118 RLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQ 174
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1206-1357 |
7.37e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 44.65 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1206 QIQEMR----QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1281
Cdd:pfam10168 540 ATQVFReeylKKHDLAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1282 -------SEGEKvkgELADRTHKIQTELDNVSCLLEDAEKK------------GIKLTKDVSSLESQLQDTQELLQEETR 1342
Cdd:pfam10168 620 nsqlpvlSDAER---EMKKELETINEQLKHLANAIKQAKKKmnyqryqiaksqSIRKKSSLSLSEKQRKTIKEILKQLGS 696
|
170
....*....|....*
gi 528481571 1343 QKLNLSSRIRQLEEE 1357
Cdd:pfam10168 697 EIDELIKQVKDINKH 711
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1698-1836 |
7.74e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1698 LEAEILQLQEDLASSERARRHAEQERD---ELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1774
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1775 TTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS---KLQELEGSVKSKFKASIAALEAKI 1836
Cdd:pfam00529 136 GGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1046-1180 |
7.78e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 44.07 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1046 EMMMVDLEERLKKE--EKTRQELEKAKRKLDAETTDLQD------------QIAELQAQIDELKIQLAKKEEELQAVLAR 1111
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1112 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLkrdlsEELEALKTEL---EDTLDTTAAQQE 1180
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
980-1180 |
7.78e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.13 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 980 QKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqemmMVDLEERLKKE 1059
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA----------LTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1060 EKTR-QELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARgdEEVAQKNNALKQLR---------EL 1129
Cdd:pfam04012 88 ALAEkKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTSLgslstssatDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 528481571 1130 QAQLAELQEDLESEKAARNKAEKlKRDLSEELEALKTELEDTLDTTAAQQE 1180
Cdd:pfam04012 166 FERIEEKIEEREARADAAAELAS-AVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1542-1727 |
1.02e-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: 43.68 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1542 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDE 1621
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1622 RKQRALAVAAKKKLEmdlkdveaqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARTSRDEIFTQSKENEKKLKSLEAE 1701
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 528481571 1702 ILQLQEDLASSERARRHAEQERDELA 1727
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1656-1943 |
1.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1656 AIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAE---QERDELADEISN 1732
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1733 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttmqvdtlntelAGERSAAQKSENARQQLERQNKDLKS 1812
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1813 KLQELEgSVKSKFKASIAALEAKIlqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANsRM 1892
Cdd:PRK03918 308 ELREIE-KRLSRLEEEINGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-EL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 528481571 1893 KQLKRQLeeaeeeatrANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1943
Cdd:PRK03918 375 ERLKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1026-1164 |
1.07e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1026 SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEEL 1105
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAA 607
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1106 QAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1164
Cdd:COG3096 608 QDALERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1625-1834 |
1.15e-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: 43.13 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1625 RALAVAAKKKLEMDLKD-----VEAQIEAANKARDEA---IKQLRKLQAQMKDYQRELEEARTSRDEIFTQ--SKENEKK 1694
Cdd:cd22656 101 DDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAakvVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1695 LKSLEAEILQLQEDLAsserarRHAEQERDELADEISNsasgkaalLDEKRRLEARIaqleeeleeeQSNMELLNDrfrk 1774
Cdd:cd22656 181 IKDLQKELEKLNEEYA------AKLKAKIDELKALIAD--------DEAKLAAALRL----------IADLTAADT---- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1775 ttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEA 1834
Cdd:cd22656 233 ---DLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1270-1619 |
1.16e-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: 43.73 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1270 LEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKgikLTKDVSSLESQLQDTQELLQEETRQKLNLSS 1349
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE---LESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1350 RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE------DDVGALEGLEEVKRK-LQKDMEVTSQKLE 1422
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkeraKKAGAQRKEEEAERKqLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1423 EKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1502
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1503 RALDEALEAKEEFERLNKQL--------------RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1568
Cdd:pfam07888 269 RTQAELHQARLQAAQLTLQLadaslalregrarwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVEL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1569 QATEDAKL----RLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELE 1619
Cdd:pfam07888 349 GREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
874-1104 |
1.18e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 874 LIKVKERQVKVENELVEMERKH--QQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERN 951
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 952 QSLQNEKKKMQShiqdleeqldeeEAARQKLQLEKVTAEAK--------------IKKMEEDILLLEDQNSKFLKEKKLL 1017
Cdd:PHA02562 251 EDPSAALNKLNT------------AAAKIKSKIEQFQKVIKmyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1018 EDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ 1097
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKIS----TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
....*..
gi 528481571 1098 LAKKEEE 1104
Cdd:PHA02562 395 KSELVKE 401
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
957-1159 |
1.31e-03 |
|
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: 43.69 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 957 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVtaEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAK 1036
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1037 NLgkvknKQEMMMVDLEERLKKEEKTRQElekakrkldaettDLQDQIAELQAQIDELKIQLAKKE---EELQAVLargd 1113
Cdd:pfam06160 309 EL-----KEELERVQQSYTLNENELERVR-------------GLEKQLEELEKRYDEIVERLEEKEvaySELQEEL---- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528481571 1114 eevaqkNNALKQLRELQAQLAELQEDLES----EKAARNKAEKLKRDLSE 1159
Cdd:pfam06160 367 ------EEILEQLEEIEEEQEEFKESLQSlrkdELEAREKLDEFKLELRE 410
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1060-1346 |
1.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1060 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQED 1139
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1140 LESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE 1219
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1220 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHkRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ 1299
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528481571 1300 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN 1346
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1620-1810 |
1.42e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1620 DERKQRALAVAAKKKLEMDLK---DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN----- 1691
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrq 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1692 -EKKLKSLEAEILQLQEDLAS-----------SERARR---HAEQERDELADEISNSASGKAALLDEKR-RLEARIAQle 1755
Cdd:PRK11281 126 lESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQAEQAL-- 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1756 eeleeeqsnMELLNDrFRKTTMQVDTLNTELaGERSAAQKSENArQQLERQNKDL 1810
Cdd:PRK11281 204 ---------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQLQLL 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1011-1682 |
1.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1011 LKEKKLLEDRVGEMTSQLAE----------EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL 1080
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSEleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1081 QDQIAELQAQIDELKiQLAKKEEELQAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1160
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1161 LEALkteledTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISeqleqakRVKGNLEK 1237
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAG 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1238 NKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE--GEKVKGELA--DRTHKIQTELDNVSCLLEdae 1313
Cdd:PRK04863 728 LEDCPE-DLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpEVPLFGRAAreKRIEQLRAEREELAERYA--- 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1314 kkgiKLTKDVSSLESQLQDTQELLQ-----------EETRQKLNlsSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1382
Cdd:PRK04863 804 ----TLSFDVQKLQRLHQAFSRFIGshlavafeadpEAELRQLN--RRRVELERALADHESQEQQQRSQLEQAKEGLSAL 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1383 QAQLVETKKKLEDDVGalEGLEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQ---QELDDLMVDLDHQRQIVSNL 1459
Cdd:PRK04863 878 NRLLPRLNLLADETLA--DRVEEIREQL-DEAEEAKRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDA 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1460 ekKQKKFDqmlaeektisarYAEERDRAEAEAREKDTKALSMARALDEALEAK-EEFERLNKQLRAEMEDLISSKDDVGK 1538
Cdd:PRK04863 955 --KQQAFA------------LTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1539 NVHELEKSKRTLEQQVEEMRTQLEELedELQATEDAklrlevnmqAMKAQFDRD-LQARDEQNEEKKRALVKQVREMEAE 1617
Cdd:PRK04863 1021 VLASLKSSYDAKRQMLQELKQELQDL--GVPADSGA---------EERARARRDeLHARLSANRSRRNQLEKQLTFCEAE 1089
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1618 LEDERKQralavaaKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-----EEARTSRD 1682
Cdd:PRK04863 1090 MDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELaylsaDELRSMSD 1152
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1031-1575 |
1.62e-03 |
|
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: 43.59 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1031 EEEKAKNLGKVKNKQEMMMVDL----EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ 1106
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1107 A-----------VLARGDEEVAQKNNALKQlRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELE 1169
Cdd:pfam07111 215 AqvtlveslrkyVGEQVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQPS 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1170 DTLD---TTAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1246
Cdd:pfam07111 294 DSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1247 ---KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKK--GIK-LT 1320
Cdd:pfam07111 373 msaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKgLM 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1321 KDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeeSRKNLEKQLATLQAQLvETKKKLEDDVGAL 1400
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER------------NRLDAELQLSAHLIQQ-EVGRAREQGEAER 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1401 EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSnlekkqKKFDQMLAEEKTISARY 1480
Cdd:pfam07111 520 QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYG------QALQEKVAEVETRLREQ 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1481 AEERDRAEAEAREKDTKALSMARALDEalEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR----TLEQQVEE 1556
Cdd:pfam07111 594 LSDTKRRLNEARREQAKAVVSLRQIQH--RATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLL 671
|
570
....*....|....*....
gi 528481571 1557 MRTQLEELEDELQATEDAK 1575
Cdd:pfam07111 672 SRYKQQRLLAVLPSGLDKK 690
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1091-1273 |
1.66e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1091 IDELKIQLAKKEEELQAvlargdEEVAQKNNALKQLRELQAQ--LAELQEDLESE-KAARNKAEKLKRDLSEELEALKTE 1167
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1168 LEDTLDTTA---AQQELRSKREQEVAELKKaiddetrnhesQIQEMRQRHGTALEEISE-QLEQAKRVKgnLEKNKQTLE 1243
Cdd:PRK12704 102 LELLEKREEeleKKEKELEQKQQELEKKEE-----------ELEELIEEQLQELERISGlTAEEAKEIL--LEKVEEEAR 168
|
170 180 190
....*....|....*....|....*....|
gi 528481571 1244 SDNKELTNEVKslQQAKSESEHKRKKLEAQ 1273
Cdd:PRK12704 169 HEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1051-1206 |
1.87e-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: 41.90 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1051 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLREL 1129
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAAL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481571 1130 QAQLAELQEDLESeKAARNKAEKLKRDL-SEELEALKTELEdtldttAAQQELRSKREQEVAELKKAIDDETRNHESQ 1206
Cdd:pfam12795 162 KAQIDMLEQELLS-NNNRQDLLKARRDLlTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1601-1874 |
1.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1601 EEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTS 1680
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1681 RDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1760
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1761 EQSNMELLNDRFRKTTMQ-VDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQL 1839
Cdd:COG4372 190 KEANRNAEKEEELAEAEKlIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270
....*....|....*....|....*....|....*
gi 528481571 1840 EEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDE 1874
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1660-1823 |
1.90e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1660 LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEisnsasgKAA 1739
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-------KDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1740 LLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEG 1819
Cdd:pfam07888 120 LLAQRAAHEARIRE--------------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
....
gi 528481571 1820 SVKS 1823
Cdd:pfam07888 186 ELRS 189
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
907-1313 |
1.99e-03 |
|
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: 42.92 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 907 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshiqdleeqldeeeaarqklqlek 986
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT----------------------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 987 vtaeakikkmeedillLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEE--------KAKnlgKVKNKQEMMMVDLEERLkk 1058
Cdd:pfam06160 137 ----------------LLANRFSYGPAIDELEKQLAEIEEEFSQFEEltesgdylEAR---EVLEKLEEETDALEELM-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1059 eEKTRQELEKAKRKLDAETTDLQDQIAELQAQ---IDELKI-----QLAKKEEELQAVLARGDEEVAQKNNalkqlRELQ 1130
Cdd:pfam06160 196 -EDIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVdkeiqQLEEQLEENLALLENLELDEAEEAL-----EEIE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1131 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---ID 1197
Cdd:pfam06160 270 ERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlNENELERVRglEKQLEELEKRydeIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1198 DETRNHE---SQIQEMrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKseSEHKRKKLEAQL 1274
Cdd:pfam06160 350 ERLEEKEvaySELQEE-------LEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL--REIKRLVEKSNL 420
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 528481571 1275 ----QEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1313
Cdd:pfam06160 421 pglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQ 463
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1436-1870 |
2.12e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.97 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1436 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeEKTISARYAEERDRAEAEAREKDTKALsMARALDEALEAKEEF 1515
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRARLLLLALAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1516 ERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQA 1595
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1596 RDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE 1675
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1676 EARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLE 1755
Cdd:COG5278 326 AALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1756 EELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAK 1835
Cdd:COG5278 406 AAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
410 420 430
....*....|....*....|....*....|....*
gi 528481571 1836 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQ 1870
Cdd:COG5278 486 EAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1542-1753 |
2.15e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1542 ELEKSKRTLEQQVEEMRTQLEELED-ELQATEDAKLRLEVNMQAmkaqfdrdlqardeqNEEKKRALVKQVREMeaeL-E 1619
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLS---------------NAEKLREALQEALEA---LsG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1620 DERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE---------EARTSR--------- 1681
Cdd:COG0497 238 GEGGALDLLGQALRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdperleevEERLALlrrlarkyg 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1682 ---DEIFTQSKENEKKLKSLEAeilqLQEDLASSERARRHAEQERDELADEISNsASGKAAlldekRRLEARIAQ 1753
Cdd:COG0497 317 vtvEELLAYAEELRAELAELEN----SDERLEELEAELAEAEAELLEAAEKLSA-ARKKAA-----KKLEKAVTA 381
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1527-1701 |
2.18e-03 |
|
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: 42.44 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1527 EDLISSKDDvGKNVHELEkSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRA 1606
Cdd:pfam09787 24 EKLIASLKE-GSGVEGLD-SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1607 LVKQV---REMEAEL-----------EDERKQRALAVAAKKKLEMDLKDVEAQIEA---ANKARDEAIKQLRKLQAQMKD 1669
Cdd:pfam09787 102 LATERsarREAEAELerlqeelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQ 181
|
170 180 190
....*....|....*....|....*....|..
gi 528481571 1670 YQRELEEARTSRDEIFTQSKENEKKLKSLEAE 1701
Cdd:pfam09787 182 KQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1010-1165 |
2.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1010 FLKEKKLLEDRvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELqa 1089
Cdd:PRK12705 24 LLKKRQRLAKE-AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1090 qiDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQ---LRELQAQ---LAELQEDLESEKAARNKAEKLKRDLSEELEA 1163
Cdd:PRK12705 101 --DNLENQLEEREKALSARELELEELEKQLDNELYRvagLTPEQARkllLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
..
gi 528481571 1164 LK 1165
Cdd:PRK12705 179 QN 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1044 |
2.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 859 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK----HQQLLEEKNILAEQLQA--------------ETELFAEAE 920
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 921 EMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeQLDEEEAARQKLQLEKVTAEAKIKKMEEDI 1000
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 528481571 1001 LLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1044
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1054-1163 |
2.77e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1054 ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEELQAvlARGDEEVAQKNNALKQLRELQAQL 1133
Cdd:COG2268 220 NREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAE--ANAEREVQRQLEIAEREREIELQE 296
|
90 100 110
....*....|....*....|....*....|...
gi 528481571 1134 AELQEDLESEKA---ARNKAEKLKRDLSEELEA 1163
Cdd:COG2268 297 KEAEREEAELEAdvrKPAEAEKQAAEAEAEAEA 329
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1141-1358 |
2.89e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1141 ESEKAARNKAEKLKRdlSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNhESQIQEMRQRHGTALEE 1220
Cdd:TIGR00927 637 EAEHTGERTGEEGER--PTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEG-EGEIEAKEADHKGETEA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1221 ISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGEL-ADRTHKIQ 1299
Cdd:TIGR00927 713 EEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIqAGEDGEMK 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1300 TElDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1358
Cdd:TIGR00927 793 GD-EGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1059-1191 |
2.91e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1059 EEKTRQELEKAKrKLDAE-TTDLQDQIAELQAqidELKIQLAKKEEELQAVLARGDEEvaqknNALKQLRELQAQLAELQ 1137
Cdd:PTZ00491 642 DERTRDSLQKSV-QLAIEiTTKSQEAAARHQA---ELLEQEARGRLERQKMHDKAKAE-----EQRTKLLELQAESAAVE 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1138 ---------------EDLESE---KAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1191
Cdd:PTZ00491 713 ssgqsraealaeaeaRLIEAEaevEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD 784
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1014-1177 |
3.01e-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: 41.97 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1014 KKLLEDRVGEMTSQLAEEEEKAKnlgKVKNKqemmMVDLEERLKKEEKTRQELEKA-KRKLDAETTDL-QDQIAELQAQI 1091
Cdd:cd22656 116 KKTIKALLDDLLKEAKKYQDKAA---KVVDK----LTDFENQTEKDQTALETLEKAlKDLLTDEGGAIaRKEIKDLQKEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1092 DELK----IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLK---RDLSEELEAL 1164
Cdd:cd22656 189 EKLNeeyaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIG---PAIPALEKLQgawQAIATDLDSL 265
|
170
....*....|...
gi 528481571 1165 KTELEDTLDTTAA 1177
Cdd:cd22656 266 KDLLEDDISKIPA 278
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1501-1629 |
3.05e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1501 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVgknVHELEKSKRTLEQQVEEMRTQLEELEDEL---QATEDAKLR 1577
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQ---VERLEAEVEELEAELEEKDERIERLERELseaRSEERREIR 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1578 LEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAV 1629
Cdd:COG2433 463 KDREISRLDREIER-LERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1314-1579 |
3.27e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1314 KKGIKLTKDVSSLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKL 1393
Cdd:pfam15905 63 KKSQKNLKESKDQKELEKEIRALVQERGEQ----DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1394 EDDVGALEGLEEVKRKLQKDMEVTS--QKLEEKA-IAFDKLEKTKNRLQQelddLMVDLDHQRQIVSNLEKKQKKFDQML 1470
Cdd:pfam15905 139 ELLKAKFSEDGTQKKMSSLSMELMKlrNKLEAKMkEVMAKQEGMEGKLQV----TQKNLEHSKGKVAQLEEKLVSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1471 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtl 1550
Cdd:pfam15905 215 IEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK--- 291
|
250 260
....*....|....*....|....*....
gi 528481571 1551 EQQVEEMRTQLEELEDELQATEDaKLRLE 1579
Cdd:pfam15905 292 EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1635-1805 |
3.28e-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: 42.03 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1635 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQ---RELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLAs 1711
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1712 seRARRHAEQE---RDELADEISNSASGKAALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELag 1788
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL-- 200
|
170
....*....|....*..
gi 528481571 1789 ersaaqksENARQQLER 1805
Cdd:pfam00529 201 --------KLAKLDLER 209
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1216-1714 |
3.31e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1216 TALEEISEQLEQAKRVKGNLEKN-------KQTLESDNKELTNEVKSLQQAKSESEHKRKKleaQLQEVMARFSEgEKVK 1288
Cdd:pfam15818 7 TSLLEALEELRMRREAETQYEEQigkiiveTQELKWQKETLQNQKETLAKQHKEAMAVFKK---QLQMKMCALEE-EKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1289 GELADRTHkiQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQdTQELLQEETRQKLNlssrirQLEEEKNNLLEQQEEE 1368
Cdd:pfam15818 83 YQLATEIK--EKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQ-LHLLAKEDHHKQLN------EIEKYYATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1369 EESRKNLEKQLA---TLQAQLVETKKKLEDDVGAL-EGLEEVKRKLQKDmEVTSQ-KLEEKAIAFDKLEKTKNRLQQELD 1443
Cdd:pfam15818 154 KENHGKLEQNVQeaiQLNKRLSALNKKQESEICSLkKELKKVTSDLIKS-KVTCQyKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1444 -DLMVDLDHQRQIVSNLEKKQKKFdqmlaeektISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERlnKQL 1522
Cdd:pfam15818 233 mELELNKKINEEITHIQEEKQDII---------ISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQR--EKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1523 RAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrdlqarDEQNEE 1602
Cdd:pfam15818 302 KENEEKFLNLQN-------EHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQ--------KKFEED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1603 KKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQReLEeaRTSRD 1682
Cdd:pfam15818 367 KKFQNVPEVNNENSEMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQV-LE--KSFKN 443
|
490 500 510
....*....|....*....|....*....|..
gi 528481571 1683 EIFTQSKENEKKLKSLEAEILQLQEDLASSER 1714
Cdd:pfam15818 444 EIDTSVPQDKNQSEISLSKTLCTDKDLISQGQ 475
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1065-1165 |
3.50e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1065 ELEKAKRKLDAETTDLQ---DQIAELQAQIDELKiQLAKK----EEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1137
Cdd:COG0497 276 ELEEAASELRRYLDSLEfdpERLEEVEERLALLR-RLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAE 354
|
90 100 110
....*....|....*....|....*....|....
gi 528481571 1138 EDLEsEKAA------RNKAEKLKRDLSEELEALK 1165
Cdd:COG0497 355 AELL-EAAEklsaarKKAAKKLEKAVTAELADLG 387
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1053-1232 |
3.54e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.34 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1053 EERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKI------QLAKKEEEL---QAVLARGDEEVaqknnal 1123
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIkdkQEKLMRRCKKV------- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1124 kqLRELQAQLAELqedLESEkaarnkaeklkRDLSEELEALKTELEdTLDttAAQQELRSKREQEVAELKKAIDDETRN- 1202
Cdd:pfam10168 616 --LQRLNSQLPVL---SDAE-----------REMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSIRKKSs 676
|
170 180 190
....*....|....*....|....*....|....*.
gi 528481571 1203 ------HESQIQEMRQRHGtalEEISEQLEQAKRVK 1232
Cdd:pfam10168 677 lslsekQRKTIKEILKQLG---SEIDELIKQVKDIN 709
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1323-1543 |
4.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1323 VSSLESQLqDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEG 1402
Cdd:PHA02562 190 IDHIQQQI-KTYNKNIEEQRKK---NGENIARKQNKYDELVEEA------KTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1403 LEEVKRKLQKDME----------------VTSQKLEEKAiafDKLEKTKNR---LQQELDDLMVDLDHQRQIVSNLEKKQ 1463
Cdd:PHA02562 260 LNTAAAKIKSKIEqfqkvikmyekggvcpTCTQQISEGP---DRITKIKDKlkeLQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1464 KKFDQMLAEEKTISARYAEERDRAeaeareKDTKALsMARALDEALEAKEEFERLNKQLraemEDLISSKDDVGKNVHEL 1543
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKA------KKVKAA-IEELQAEFVDNAEELAKLQDEL----DKIVKTKSELVKEKYHR 405
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
958-1354 |
4.35e-03 |
|
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: 41.76 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 958 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVTA----------------------EAKIKKMEEDILLLEDQNSK--FLKE 1013
Cdd:pfam06160 5 RKKIYKEIDELEERKNELMNLPVQEELSKVKKlnltgetqekfeewrkkwddivTKSLPDIEELLFEAEELNDKyrFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1014 KKLLEdrvgEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ-------IAE 1086
Cdd:pfam06160 85 KKALD----EIEELLDDIEEDIKQILE----------ELDELLESEEKNREEVEELKDKYRELRKTLLANrfsygpaIDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1087 LQAQIDELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALK- 1165
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTES----GDYLEAR-----EVLEKLEEETDALEELMEDIPPL---YEELKTELPDQLEELKe 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1166 --TELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEK 1237
Cdd:pfam06160 219 gyREMEeegyalEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1238 NKQTLESD-------NKELTNEVKSLQQ----AKSESEHKR------KKLEAQLQEVMARFSEGEKVKGELADRTHKIQT 1300
Cdd:pfam06160 292 NLPEIEDYlehaeeqNKELKEELERVQQsytlNENELERVRglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILE 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 528481571 1301 ELDNVsclledaEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1354
Cdd:pfam06160 372 QLEEI-------EEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1400-1909 |
4.85e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1400 LEGLEEVKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISAR 1479
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHG----KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1480 YaeerdraeaearekdtkalsmaRALDEALEAKEEFERLNKQLRAEMEDLISSKddvgkNVHELEKSKRTLEQQVEEMRT 1559
Cdd:TIGR00618 245 L----------------------TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1560 QLEELEDELQATEDAKLRLEVNMQAM-KAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKK---L 1635
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1636 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1715
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1716 RRHAEQERDELADEISNSASGKAALLDEKRRLEARIAqleeELEEEQSNMELLNDRFRKTTMQVdTLNTELAGERSAAQK 1795
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1796 SENARQQLERQNKDLKSKLQELE---GSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1872
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510
....*....|....*....|....*....|....*..
gi 528481571 1873 DERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRA 1909
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1014-1165 |
5.36e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1014 KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD----AETTDLQDQIAELQA 1089
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1090 QIDELKIQLAKKEEELQAVlargdEEVAQKNNALKQlrELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALK 1165
Cdd:smart00787 219 EIMIKVKKLEELEEELQEL-----ESKIEDLTNKKS--ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1012-1168 |
5.36e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1012 KEKKL--LEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKakrkLDAEttdLQDQIAELQA 1089
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQA----LLAE---LAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481571 1090 QIDELKIQLAkkeeELQAVLARgdeevaqknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTEL 1168
Cdd:PRK09039 117 RAGELAQELD----SEKQVSAR----------ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1040-1163 |
5.62e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1040 KVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQK 1119
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS---FERLAELRDELAELE-------EELEALKARWEAEKELI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 528481571 1120 NNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1163
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1014-1196 |
5.64e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1014 KKLLEDRVGEMTSQLAE-EEEKAKNLGKVKnKQEMMMVDLEERLKK-EEKTRQELEKA-----------KRKLDAETTDL 1080
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEaRQALAQVIANQK-RLERQLEELEAEAEKwEEKARLALEKGredlarealerKAELEAQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1081 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNAlkqlrELQAQLAELQEDLESEKAAR--NKAEKLKRDLS 1158
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-----KAQEKVNEALSGIDSDDATSalERMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 528481571 1159 EELEALKT-ELEDTLDTTAAQQELRSKREQEVAELKKAI 1196
Cdd:COG1842 179 ARAEAAAElAAGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1533-1696 |
5.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1533 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaKLRLEVNMQAmkaqfdrdlqardEQNEEKKRALVkqvr 1612
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE--KLKEELEEKK-------------EKLQEEEDKLL---- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1613 emeAELEDERKQRalavaakkklemdlkdveaqIEAANKARDEAIKQLRKLQA---------QMKDYQRELEEARTSRDE 1683
Cdd:PRK00409 569 ---EEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKggyasvkahELIEARKRLNKANEKKEK 625
|
170
....*....|...
gi 528481571 1684 IFTQSKENEKKLK 1696
Cdd:PRK00409 626 KKKKQKEKQEELK 638
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1503-1937 |
5.82e-03 |
|
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: 41.38 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1503 RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELqatedaklrlEVNM 1582
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDEL----------EKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1583 QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQ-RALAVAAKKKLEMDLKDVEA---QIEAANKA--RDEA 1656
Cdd:pfam06160 156 AEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyrEMEEEGYAleHLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1657 IKQLRKLQAQMKDYQRELEEARTsrdeiftqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1736
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLEL---------DEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1737 KAALLDEKRRLeariaqleeeleeeQSNMELLND---RFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1813
Cdd:pfam06160 307 NKELKEELERV--------------QQSYTLNENeleRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1814 LQELEGSVKsKFKASIAALEakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKAN 1889
Cdd:pfam06160 373 LEEIEEEQE-EFKESLQSLR--------------KDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVS 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 528481571 1890 SRMKQLKRQLeeaeeeatraNASR---RKLQRELDDATEASEGLSREVNTL 1937
Cdd:pfam06160 436 DEIEDLADEL----------NEVPlnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1063-1165 |
5.88e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.25 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1063 RQELEKAKRKLDAETTDLQDQIAELQAQIDELkIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLES 1142
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAY-AAAQAALATAQKELA--NAQAQALQTAQNNLATAQAALANAEARLAK 336
|
90 100
....*....|....*....|...
gi 528481571 1143 EKAArnkAEKLKRDLSEELEALK 1165
Cdd:TIGR04320 337 AKEA---LANLNADLAKKQAALD 356
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1640-1744 |
5.94e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.96 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1640 KDVEAQIEAANKARDEAIKQLrklqaqmKDYQRELEEARTSRDEIFTQSKENEKKLKslEAEILQLQEDLASS-ERARRH 1718
Cdd:cd06503 33 EKIAESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAE 103
|
90 100
....*....|....*....|....*.
gi 528481571 1719 AEQERDELADEISNSASGKAALLDEK 1744
Cdd:cd06503 104 IEQEKEKALAELRKEVADLAVEAAEK 129
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1591-1726 |
6.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1591 RDLQARDEQNEEKKRALVKQVREMEAELEDERkqralavaakkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1670
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEE----------------IRRLEEQVERLEAEVEELEAELEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1671 QRELEEARTSRDEiftqSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDEL 1726
Cdd:COG2433 447 ERELSEARSEERR----EIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1602-1897 |
6.31e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1602 EKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1681
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1682 DEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKaALLDEKRRLEARIAQLEEELEEE 1761
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1762 QSNMELLNdRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKAsIAALEAKILqlee 1841
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK-ADELHEEII---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481571 1842 qleqeakeraAANKIVRRTEKKLKEVFMQVEDERRHADQyKEQMEKANSRMKQLKR 1897
Cdd:COG1340 234 ----------ELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1512-1664 |
6.52e-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: 40.82 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1512 KEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA--TEDAKLRLEVNMQAMKAQF 1589
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDllTDEGGAIARKEIKDLQKEL 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481571 1590 DrdlQARDEQNEEKKRALvKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeaankarDEAIKQLRKLQ 1664
Cdd:cd22656 189 E---KLNEEYAAKLKAKI-DELKALIADDEAKLAAALRLIADLTAADTDLDNLLALI-------GPAIPALEKLQ 252
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1246-1475 |
6.81e-03 |
|
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: 41.17 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1246 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG-----EKVKGELADRTHKIQTELDNVSC---------LLED 1311
Cdd:pfam05667 249 LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSsttdtGLTKGSRFTHTEKLQFTNEAPAAtsspptkveTEEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1312 AEKKGiklTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQlVETKK 1391
Cdd:pfam05667 329 LQQQR---EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEEL--------------EELKEQNEELEKQ-YKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1392 KLeddVGALEGLEEVKRKLQKDMEVTSQKLEE-------------------KAIAFDKLEKTKNRLQ--QELDDLMvdld 1450
Cdd:pfam05667 391 KT---LDLLPDAEENIAKLQALVDASAQRLVElagqwekhrvplieeyralKEAKSNKEDESQRKLEeiKELREKI---- 463
|
250 260
....*....|....*....|....*
gi 528481571 1451 hqRQIVSNLEKKQKKFDQMLAEEKT 1475
Cdd:pfam05667 464 --KEVAEEAKQKEELYKQLVAEYER 486
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
864-1198 |
7.46e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 864 EEEMQAKDEELIKVKERQVKVENELVE--------MERKHQQLLEEKNILAEQLQAETELFAEAEEMRA-RLVAKKQELE 934
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINksineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 935 EILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarqklqlekvtaeakIKKMEEDILLLEDQNSKFLKEK 1014
Cdd:PRK01156 569 SWLNALAVISLIDIETNRSRSNEIKKQLNDL---------------------------ESRLQEIEIGFPDDKSYIDKSI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1015 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvdleeRLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL 1094
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKID--------NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1095 KIQLAKKEEELQAVLARgdeevaqknnalkqLRELQAQLAELQEDLESEKaarnKAEKLKRDLSEELEALKTELEDTLDT 1174
Cdd:PRK01156 694 KANRARLESTIEILRTR--------------INELSDRINDINETLESMK----KIKKAIGDLKRLREAFDKSGVPAMIR 755
|
330 340
....*....|....*....|....
gi 528481571 1175 TAAQQELRSKREQEVAELKKAIDD 1198
Cdd:PRK01156 756 KSASQAMTSLTRKYLFEFNLDFDD 779
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1483-1726 |
7.75e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1483 ERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEmedlisskdDVGKNVHELEKSKRTLEQQVEEmRTQLE 1562
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKS-ISSLK 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1563 E--LEDELQATEdaklrlevnmqaMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEM-DL 1639
Cdd:COG5022 899 LvnLELESEIIE------------LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVEsKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1640 KDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqsKENEKKLKSLEAEILQLQ--EDLASSERARR 1717
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL----QESTKQLKELPVEVAELQsaSKIISSESTEL 1042
|
....*....
gi 528481571 1718 HAEQERDEL 1726
Cdd:COG5022 1043 SILKPLQKL 1051
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1547-1701 |
7.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1547 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFDRDLQARDEQNEEKKRALVKQVREMEAELED 1620
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1621 ERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEAR-TSRDEIFTQSKENEKKLKs 1697
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEeEARHEAAVLIKEIEEEAK- 183
|
....
gi 528481571 1698 LEAE 1701
Cdd:PRK12704 184 EEAD 187
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1179-1441 |
7.97e-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: 40.56 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1179 QELRSKREQEVAELK--KAIDDETRN--HESQIQEMRQRHGTA-LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTnEV 1253
Cdd:pfam15905 59 LELKKKSQKNLKESKdqKELEKEIRAlvQERGEQDKRLQALEEeLEKVEAKLNAAVREKTSLSASVASLEKQLLELT-RV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1254 KSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDT 1333
Cdd:pfam15905 138 NELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1334 QELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1413
Cdd:pfam15905 218 KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
250 260
....*....|....*....|....*...
gi 528481571 1414 MEVTSQKLEEkaiafdKLEKTKNRLQQE 1441
Cdd:pfam15905 298 YEEKEQTLNA------ELEELKEKLTLE 319
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
1059-1169 |
8.10e-03 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 37.66 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1059 EEKTRQELEKAKRkldaettdlqDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQE 1138
Cdd:pfam16516 1 EELKRKEMEKVYK----------DEIDCLQAQLQAAEEALAAKQREIDEL----KQEIAQKEEDLETISVLKAQAEVYRS 66
|
90 100 110
....*....|....*....|....*....|.
gi 528481571 1139 DLESEKAARNKAEKLKRDLSEELEALKTELE 1169
Cdd:pfam16516 67 DFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1482-1731 |
8.19e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1482 EERDRAEAEAREKDTKalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKskrtLEQQVEEMRTQL 1561
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEE----AEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1562 EELEDELQATEDAKLRLEVNMQAMKAqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKD 1641
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKE--------IAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1642 V-------EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskenEKKLKSLEAEILQLQEDLASSER 1714
Cdd:pfam00261 153 VgnnlkslEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFA--------------ERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|....*..
gi 528481571 1715 ARRHAEQERDELADEIS 1731
Cdd:pfam00261 219 KYKAISEELDQTLAELN 235
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1209-1530 |
8.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1209 EMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1288
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1289 GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknNLLEQQEEE 1368
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1369 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1448
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1449 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1528
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
..
gi 528481571 1529 LI 1530
Cdd:COG4372 335 LL 336
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
859-1160 |
8.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 859 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 938
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 939 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1018
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481571 1019 DRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQL 1098
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481571 1099 AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1160
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| |
