|
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 ... |
883-1963 |
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: 1478.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 883 TRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDL 962
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 963 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1042
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1043 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAK 1122
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1123 KEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1202
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1203 LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAK 1282
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1283 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE 1362
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1363 TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQK 1442
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1443 LEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALS 1522
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1523 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1602
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1603 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQL 1682
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1683 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAL 1762
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1763 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGS 1842
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1843 VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLE 1922
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 688558686 1923 EAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1963
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-806 |
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: 1422.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14920 231 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14920 311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14920 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespgeVDRIV 661
Cdd:cd14920 471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD----------------------VDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 GLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd14920 529 GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14920 609 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
102-806 |
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: 1307.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKE---------SGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYR-FLSNGNIPIPGQQDKDNFQ 340
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd01377 312 VTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH-GKFQKP 579
Cdd:cd01377 391 NHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKsKNFKKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 580 RQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQnfqrasfydvsslhespgevdr 659
Cdd:cd01377 469 KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE---------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 660 ivgldqvagmnETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 739
Cdd:cd01377 527 -----------SGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGV 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 740 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd01377 596 LEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-806 |
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: 1232.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14932 235 TMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14932 315 QKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14932 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespgeVDRIV 661
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD----------------------VDRIV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 GLDQVAGMNETAFGaAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd14932 533 GLDKVAGMGESLHG-AFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLE 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14932 612 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-806 |
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: 1187.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14919 228 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14919 308 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14919 388 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespgeVDRIV 661
Cdd:cd14919 468 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD----------------------VDRII 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 GLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd14919 526 GLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLE 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14919 606 GIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
102-806 |
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: 1173.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14921 231 TLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14921 311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14921 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespgeVDRIV 661
Cdd:cd14921 471 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD----------------------VDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 GLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd14921 529 GLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLE 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14921 609 GIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-806 |
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: 1168.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd15896 155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd15896 235 TMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd15896 315 QKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd15896 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespgeVDRIV 661
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD----------------------VDRIV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 GLDQVAGMNEtaFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd15896 533 GLDKVSGMSE--MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLE 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd15896 611 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
102-806 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1159.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKpRQ 581
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvsslhespgevdRIV 661
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA-----------------------EIV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 GLDQVAgMNETAFGAayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd14911 533 GMAQQA-LTDTQFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLE 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14911 610 GIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-806 |
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: 1130.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQdKDNFQE 341
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQ 581
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespgeVDRIV 661
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD----------------------VEGIV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 GLDQVAGMNETAFGAayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd14930 528 GLEQVSSLGDGPPGG--RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14930 606 GIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
90-806 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1095.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 90 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 169
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 170 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkavklQGELERQLLQANPILESFGNAKTVKN 249
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------VGRLEEQILQSNPILEAFGNAKTVRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 250 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-I 328
Cdd:pfam00063 147 NNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 329 PIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRA 408
Cdd:pfam00063 227 TIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 409 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLC 488
Cdd:pfam00063 307 LCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 489 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQ 568
Cdd:pfam00063 387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 569 EQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvs 648
Cdd:pfam00063 464 TFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 649 slhespgevdrivGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 728
Cdd:pfam00063 530 -------------ETAESAAANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNS 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 729 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:pfam00063 597 LVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
83-818 |
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: 1002.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 83 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 162
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 163 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklQGELERQLLQANPILESFG 242
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------------VGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 243 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRF 322
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 323 LSNGN-IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENT-AAQKLCHLLGM 400
Cdd:smart00242 225 LNQGGcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 401 NVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQ 480
Cdd:smart00242 305 DPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 481 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDK 560
Cdd:smart00242 384 VNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 561 TFVDKLVQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNfq 640
Cdd:smart00242 461 TFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN-- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 641 rasfydvsslhespgevdrivgldqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 720
Cdd:smart00242 538 --------------------------------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEK 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 721 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQ 800
Cdd:smart00242 580 KPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGK 659
|
730
....*....|....*...
gi 688558686 801 SKIFFRTGVLAHLEEERD 818
Cdd:smart00242 660 TKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
39-1379 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 905.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 39 VWVPSERHGFEAASIREERGEEVLVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 113
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 114 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 193
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 194 VIQYLAHVASSHkgrkdhniPPESpkavklqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGAN 273
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI-------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 274 IETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQETMEAMHIMSFN 352
Cdd:COG5022 237 IETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 353 HEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADF 432
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 433 AVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 512
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 513 QREGIEWSFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVDKLVQ--EQGTHGKFQKPRQLKDKadFCI 590
Cdd:COG5022 475 VKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 591 IHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQnfqrasfydvsslhespgevdrivgldqvagmn 670
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------------------- 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 671 etafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 750
Cdd:COG5022 598 --------IESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGF 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 751 PNRIVFQEFRQRYEILTPNA----IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDIII 826
Cdd:COG5022 670 PSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIAT 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 827 YFQSVCRGYLARKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVkerQVKV 906
Cdd:COG5022 750 RIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL---QKTI 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 907 ENELVEMERKHQQLLEEKNILAEQlqaetelFAEAEEMRARLVAKKQelEEILHDLESRVEEEEERNQSLQNEKKKMQSh 986
Cdd:COG5022 827 KREKKLRETEEVEFSLKAEVLIQK-------FGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDVKSISS- 896
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 987 iqdleeqldeeeAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEdrvgemTSQLaeEEEKAKNLGKVKNK 1066
Cdd:COG5022 897 ------------LKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLN------NIDL--EEGPSIEYVKLPEL 956
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1067 QEMMMVDleerlKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDElkiqLAKKEEELQAVlargdeevaqkNNALK 1146
Cdd:COG5022 957 NKLHEVE-----SKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKE----LAELSKQYGAL-----------QESTK 1016
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1147 QLRELQAQLAELQEDLE------SEKAARNKAEKLKRD-------LSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1213
Cdd:COG5022 1017 QLKELPVEVAELQSASKiissesTELSILKPLQKLKGLlllennqLQARYKALKLRRENSLLDDKQLYQLESTENLLKTI 1096
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1214 LKKAIDDETRNHESQIQEMR-----QRHGTALEEISEQLEQA----KRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE 1284
Cdd:COG5022 1097 NVKDLEVTNRNLVKPANVLQfivaqMIKLNLLQEISKFLSQLvntlEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAA 1176
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1285 SEHKRKKLEAQLQEV-MARFSEGEKVKGELADRTHKIQTElDNVSCLLEDAEKKGIKLT------KDVSSLESQLQDTQE 1357
Cdd:COG5022 1177 LSEKRLYQSALYDEKsKLSSSEVNDLKNELIALFSKIFSG-WPRGDKLKKLISEGWVPTeystslKGFNNLNKKFDTPAS 1255
|
1370 1380
....*....|....*....|..
gi 688558686 1358 LLQEETRQKLNLSSRIRQLEEE 1379
Cdd:COG5022 1256 MSNEKLLSLLNSIDNLLSSYKL 1277
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
102-806 |
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: 849.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-----------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL-----SNGNIPIPGQQD 335
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 336 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT--DQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 573 HGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdeiqnfqrasfydvsslhe 652
Cdd:cd00124 467 HPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 653 spgevdrivgldqvagmnetafgaayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 732
Cdd:cd00124 519 ---------------------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLE 559
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 733 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd00124 560 QLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
102-806 |
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: 776.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFL----ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14927 236 MATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14927 316 YVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 579 PR---QLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiQNFQRASFYDvsslhespg 655
Cdd:cd14927 472 PRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY----ENYVGSDSTE--------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 656 evdrivglDQVAGMNETafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 735
Cdd:cd14927 539 --------DPKSGVKEK------RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLR 604
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 736 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14927 605 CNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
103-806 |
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: 760.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14913 233 ATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKP 579
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 580 RQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrASFydvsslhespgev 657
Cdd:cd14913 469 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY---------ATF------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 658 drivgldqvAGMNETAFGAAYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 736
Cdd:cd14913 527 ---------ATADADSGKKKVAKKKGSsFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRC 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 737 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14913 598 NGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-806 |
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: 743.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippeSPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK----------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14909 311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKP 579
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 580 RQLK---DKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvsslhesPGE 656
Cdd:cd14909 467 KPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH------------------AGQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 657 vdrivgldqvAGMNETAFGAAYKtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 736
Cdd:cd14909 529 ----------SGGGEQAKGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTC 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 737 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14909 598 NGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
102-806 |
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: 720.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG------------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHL-RSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKP 579
Cdd:cd14934 388 NHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 580 RQLKDK---ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdKFVAELWKDEiqnfqrasfydvsslhespge 656
Cdd:cd14934 465 KGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFKE--------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 657 vdrivgldqvagmnETAFGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 735
Cdd:cd14934 523 --------------EEAPAGSKKQKRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLA 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 736 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14934 589 CNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
103-806 |
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: 710.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQ 340
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd01380 226 ETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd01380 306 IVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 500 FNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK--FQ 577
Cdd:cd01380 386 FNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 578 KPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLhqstdkfvaelwkdeiqnfqRASfydvsslhespgev 657
Cdd:cd01380 462 KPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVL--------------------KAS-------------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 658 drivgldqvagmnetafgaayKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 737
Cdd:cd01380 506 ---------------------KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRAC 561
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 738 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd01380 562 GVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
102-806 |
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: 698.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LR-DLLLVSANpsDFHFCSCGAVAVESLDDAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 579 PRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIqnfqrasfydvsslhespge 656
Cdd:cd14929 462 PKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYI-------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 657 vdrivgldqVAGmNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 736
Cdd:cd14929 522 ---------STD-SAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRC 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 737 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14929 592 NGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
103-806 |
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: 697.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPKavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPG----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14917 153 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASIDDAEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14917 232 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 579 PRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespge 656
Cdd:cd14917 468 PRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 657 vdrivgldqVAGMNETAFGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 735
Cdd:cd14917 526 ---------YAGADAPIEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLR 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 736 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14917 597 CNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
104-806 |
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: 684.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 183
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 184 GAGKTENTKKVIQYLAHVASSHKGRKDhnippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 263
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKE--------ESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 264 DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE-GFNSYRFLSNGNIPIPGQQDKDNFQET 342
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 343 MEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQ 422
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 423 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 502
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 503 TMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPRQ 581
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 LKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqraSFYdvsslheSPGEVDr 659
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF----------STY-------ASAEAD- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 660 ivgldqvagmneTAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 739
Cdd:cd14918 533 ------------SGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGV 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 740 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14918 601 LEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
103-806 |
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: 682.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPR 580
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 581 QLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydvSSLHESPGEvd 658
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---------------SGAQTAEGA-- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 659 rivgldqVAGMNETAFGaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 738
Cdd:cd14912 535 -------SAGGGAKKGG---KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNG 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 739 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14912 605 VLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
103-806 |
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: 678.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnippespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN--------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14916 154 HFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL-DMLLVTNNpyDYAFVSQGEVSVASIDDSEEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14916 233 LATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14916 313 YVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 500 FNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQK 578
Cdd:cd14916 392 FNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 579 PRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvsslhespge 656
Cdd:cd14916 469 PRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY--------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 657 vdrivgldQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 736
Cdd:cd14916 528 --------ASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRC 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 737 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14916 600 NGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
103-806 |
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: 677.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE-GFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPR 580
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 581 QLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespgevd 658
Cdd:cd14910 472 PAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG------------------------ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 659 rivgldQVAGMNETAFGAAYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 737
Cdd:cd14910 528 ------AAAAEAEEGGGKKGGKKKGSsFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCN 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 738 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14910 602 GVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-806 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 677.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14923 234 ATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKP 579
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 580 RQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfYDVSSLHESPGEv 657
Cdd:cd14923 470 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN----------YAGAEAGDSGGS- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 658 drivgldqvagmnetafGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 737
Cdd:cd14923 539 -----------------KKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCN 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 738 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14923 602 GVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-806 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 670.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYRF--LSNGNIPIPGQQDKDNFQ 340
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDY 420
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 421 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 500
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 501 NHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKP 579
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 580 RQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydvsslheSPGEv 657
Cdd:cd14915 471 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLF--------------------SGGQ- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 658 drivgldqvAGMNETAFGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 736
Cdd:cd14915 530 ---------TAEAEGGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRC 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 737 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14915 601 NGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
103-806 |
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: 636.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNF 339
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK-LCHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd14883 223 DHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIRQINVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 498
Cdd:cd14883 303 NVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 499 LFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQK 578
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 579 PRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdeiqnfqrasfydvsslhesPGEVD 658
Cdd:cd14883 459 PDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT--------------------YPDLL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 659 RIVGLDQVAGMNETAFGaaykTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 738
Cdd:cd14883 519 ALTGLSISLGGDTTSRG----TSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 739 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14883 594 MLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
103-806 |
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: 633.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQE 341
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 421
Cdd:cd01383 221 LKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 422 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 501
Cdd:cd01383 301 VKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 502 HTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRq 581
Cdd:cd01383 381 RHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 582 lkDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNFQRASfydvsslhespgevdriv 661
Cdd:cd01383 457 --GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKAL------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 662 gldqvagMNETAFGAAyktkkGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 741
Cdd:cd01383 516 -------PLTKASGSD-----SQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLE 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 742 GIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd01383 584 VVRISRSGYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
103-806 |
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: 628.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkaVKlqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQE 341
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVG---R 418
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 498
Cdd:cd01378 306 SVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 499 LFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVDKLVQEQGTHGKFQ 577
Cdd:cd01378 386 IFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 578 KPRQLKD--KADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQnfqrasfydvsslhespg 655
Cdd:cd01378 463 CPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 656 evdrivgldqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 735
Cdd:cd01378 525 -----------------------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVK 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 736 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd01378 582 YLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
102-806 |
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: 605.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPPespkavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS-----------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNF 339
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSpRIKV 416
Cdd:cd01384 226 RATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 417 GRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEK 495
Cdd:cd01384 305 TPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 496 LQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 575
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 576 FQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydvsslHESPG 655
Cdd:cd01384 461 FSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF------------------PPLPR 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 656 EvdrivgldqvagmnetafgaayKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 734
Cdd:cd01384 521 E----------------------GTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQL 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 735 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 806
Cdd:cd01384 579 RCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
102-806 |
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: 601.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQ 340
Cdd:cd01381 142 HFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKK--ERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd01381 222 DIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd01381 302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 497 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 575
Cdd:cd01381 382 QQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 576 FQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIqnfqrasfydvsslheSPG 655
Cdd:cd01381 458 YLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI----------------SMG 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 656 EVDRivgldqvagmnetafgaayktKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 735
Cdd:cd01381 521 SETR---------------------KKSP--TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLR 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 736 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd01381 578 YSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-806 |
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: 564.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLegfnsyrflsngnipIPGQQDKDNFQ 340
Cdd:cd01382 143 IHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT-------DQASMPENTAAQKlchLLGMNVMEF-----TRA 408
Cdd:cd01382 208 RMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 409 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFQLNSFEQLC 488
Cdd:cd01382 285 MQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 489 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQ 568
Cdd:cd01382 363 INYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 569 EQGTHGKFQKPRQ--------LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdeiqnFQ 640
Cdd:cd01382 440 KHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSL-------FE 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 641 RASFYDVSSLHespgevdrivgldqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 720
Cdd:cd01382 513 SSTNNNKDSKQ---------------------------KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKM 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 721 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQ 800
Cdd:cd01382 566 TSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGL 643
|
....*.
gi 688558686 801 SKIFFR 806
Cdd:cd01382 644 TKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
102-806 |
9.34e-180 |
|
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: 560.55 E-value: 9.34e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGfnSYRFLSNGN-IPIPGQQDKDNFQ 340
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVDDVADFE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCH---LLGMNVMEFTRAILSPRIKV- 416
Cdd:cd14872 220 EVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIk 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 417 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd14872 300 GCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 497 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKF 576
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 577 QKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdeiqnfqrasfydvsslhesPGE 656
Cdd:cd14872 457 VYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP--------------------PSE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 657 VDRivgldqvagmnetafgaayKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 736
Cdd:cd14872 517 GDQ-------------------KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRY 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 737 NGVLEGIRICRQGFPNRIVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14872 575 AGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
102-806 |
1.39e-174 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 547.07 E-value: 1.39e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 176
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 177 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFG 256
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 257 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDK 336
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 337 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKErntDQASMPEN-TAAQKLCH---LLGMNVMEFTRAILSP 412
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE---NDTTVLEDaTTLQSLKLaaeLLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 413 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVDKLVQE 569
Cdd:cd14890 397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 570 QGT-------------HGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdei 636
Cdd:cd14890 475 FGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 637 qnfqrasfydvSSLHESpgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIP 716
Cdd:cd14890 542 -----------RSIREV---------------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 717 NHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLY 796
Cdd:cd14890 578 NETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADW 652
|
730
....*....|
gi 688558686 797 RIGQSKIFFR 806
Cdd:cd14890 653 QIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
102-806 |
4.48e-171 |
|
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: 537.41 E-value: 4.48e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnippesPKAVKLQGElerQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRFGKYLEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG-NIPIPGQQDKDNFQ 340
Cdd:cd01387 143 FFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ---ASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVG 417
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 418 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 497
Cdd:cd01387 302 RERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 498 QLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQ 577
Cdd:cd01387 381 YYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 578 KPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNFQRASfydvsslhespgev 657
Cdd:cd01387 458 KPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAP-------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 658 drivgldqVAGMNetafgAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 737
Cdd:cd01387 522 --------PRLGK-----GRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYS 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 738 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 806
Cdd:cd01387 589 GMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-806 |
2.23e-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: 525.79 E-value: 2.23e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLahVASSHKGrkdHNippespkavklqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG------------SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNFQ 340
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKER-NTDQASMPENTAAQKL-CHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd01385 224 RLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFQLNSFEQLCINYTNE 494
Cdd:cd01385 304 ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 495 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHG 574
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 575 KFQKPrQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAEL----------WkdeiqNFQRASF 644
Cdd:cd01385 460 YYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrW-----AVLRAFF 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 645 YDVSSLHESPGEVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGK 724
Cdd:cd01385 533 RAMAAFREAGRRRAQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLR 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 725 LEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 804
Cdd:cd01385 613 FDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVF 688
|
..
gi 688558686 805 FR 806
Cdd:cd01385 689 LK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
102-806 |
1.77e-165 |
|
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: 522.41 E-value: 1.77e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkavklqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsdLLLEGFNSYRFL-SNGNIPIPGQQDKDNF 339
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASM--PENTAAQKLCHLLGMNVMEFTRAILSPRIKVG 417
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 418 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 497
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 498 QLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVqeqGTHGKFQ 577
Cdd:cd14903 380 QKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 578 K----PRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdeiqnfQRASFYDVSSlhes 653
Cdd:cd14903 453 DviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK------EKVESPAAAS---- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 654 pgevdrivgldqvagMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 733
Cdd:cd14903 521 ---------------TSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQ 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 734 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 806
Cdd:cd14903 586 LRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
102-806 |
4.18e-159 |
|
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: 504.71 E-value: 4.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELS----------LKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNF 339
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKkerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14873 231 REVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 420 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 498
Cdd:cd14873 308 EILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 499 LFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQK 578
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 579 PRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdeiqnfqrasFYDVSSLHespgevd 658
Cdd:cd14873 461 PRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDL------------FEHVSSRN------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 659 rivgldqvagmNETAFGAAYKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 738
Cdd:cd14873 520 -----------NQDTLKCGSKHRRP---TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSG 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 739 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14873 586 MLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
102-804 |
7.36e-159 |
|
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: 503.94 E-value: 7.36e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 173
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 174 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPPESpkavklqgeLERQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------VRDRVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 252 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIP 329
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 330 IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-KKERNTDQASMPENTAAQKLCHLLGMNVMEFTRA 408
Cdd:cd14901 231 RDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 409 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFQLNSFEQL 487
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 488 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFV 563
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 564 DKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdeiqnfqras 643
Cdd:cd14901 464 NKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 644 fydvsslhespgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAG 723
Cdd:cd14901 531 -------------------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPS 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 724 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYr 797
Cdd:cd14901 568 EFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ- 646
|
....*..
gi 688558686 798 IGQSKIF 804
Cdd:cd14901 647 VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
103-806 |
7.93e-159 |
|
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: 502.96 E-value: 7.93e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVAsshkgrkdhnippespKAVklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG----------------KAN--NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGagehLRSDLLLEGFNS-------YRFLSNGNIPIPGQQD 335
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKLpenkpprYLQNDGLTVQDIVNNS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 336 --KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENTAA-QKLCHLLGMNVMEFTRAI 409
Cdd:cd01379 220 gnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 410 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFQLNSFEQL 487
Cdd:cd01379 300 TSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 488 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVDKL 566
Cdd:cd01379 380 CINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 567 vqEQGTHGKFQKpRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdeiqnfqrasfyd 646
Cdd:cd01379 456 --HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ---------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 647 vsslhespgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 726
Cdd:cd01379 517 ----------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFD 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 727 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 806
Cdd:cd01379 557 REKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
102-768 |
4.37e-158 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 502.30 E-value: 4.37e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVT---------GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-- 329
Cdd:cd14888 145 LQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPis 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 330 ----------------------IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPE 387
Cdd:cd14888 225 idmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 388 NTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG 464
Cdd:cd14888 305 ASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 465 ASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGV 544
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 545 LALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQST 624
Cdd:cd14888 462 FCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 625 DKFVAELWKDEIqnfqrasfydvsslhespgevDRIVGLdqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLR 704
Cdd:cd14888 540 NPFISNLFSAYL---------------------RRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETID 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 705 NTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 768
Cdd:cd14888 584 KTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
102-806 |
7.82e-158 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 501.21 E-value: 7.82e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 174
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSR 254
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 255 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQ 333
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 334 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQ----ASMPENTAAQKLCHLLGMNVMEFTRAI 409
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 410 LSPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIF 479
Cdd:cd14892 313 VTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 480 QLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KAT 558
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 559 DKTFVDKLVQEQ-GTHGKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdeiq 637
Cdd:cd14892 470 DKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 638 nfqrasfydvsslhespgevdrivgldqvagmnetafgaayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPN 717
Cdd:cd14892 536 -----------------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPN 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 718 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALEL 791
Cdd:cd14892 562 NLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARAL 641
|
730
....*....|....*
gi 688558686 792 DPNLYRIGQSKIFFR 806
Cdd:cd14892 642 ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-806 |
7.12e-155 |
|
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: 492.28 E-value: 7.12e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD------------------DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD----- 335
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseele 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 336 --KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd14897 223 yyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFQLNSFEQLCI 489
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 490 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQE 569
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 570 QGTHGKFQKPrqLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeIQNFQRasfydvss 649
Cdd:cd14897 460 CGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---TSYFKR-------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 650 lhespgevdrivgldqvagmnetafgaayktkkgmfrtvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 729
Cdd:cd14897 527 ---------------------------------------------SLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDEL 561
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 730 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 806
Cdd:cd14897 562 VRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
103-766 |
4.90e-142 |
|
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: 456.31 E-value: 4.90e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 168
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 169 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkDHNIPPESPKAVKLQGeLERQLLQANPILESFGNAKT 246
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------DNNLAASVSMGKSTSG-IAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 247 VKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhlrsdlllegfnsyrflsng 326
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 327 nipipGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPENTAAQKL------CHLLG 399
Cdd:cd14900 214 -----AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 400 MNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAG 475
Cdd:cd14900 289 VDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 476 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP 555
Cdd:cd14900 369 FEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 556 KATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDplndnvatLLHQSTdkfvaelwkde 635
Cdd:cd14900 446 KGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 636 iqnfqrasfydvsslhespgeVDrivgldqvagmnetafgaayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCII 715
Cdd:cd14900 507 ---------------------VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLK 539
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 688558686 716 PNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 766
Cdd:cd14900 540 PNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-769 |
5.95e-141 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 454.87 E-value: 5.95e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 172
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 173 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAV-KLQGELERQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 252 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE----GFNSYRFLSNG 326
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 327 NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK-KERNTDQASMPENTAA-QKLCHLLGMNVME 404
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 405 FTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 477
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 478 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 555
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 556 KATDKTFVDKLVQEQGTHGKFQKPRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDE 635
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 636 IQNFQRASFYDVSSlhespgevdrivgldqvagmnetafgaaYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCII 715
Cdd:cd14907 557 DGSQQQNQSKQKKS----------------------------QKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIK 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558686 716 PNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 769
Cdd:cd14907 605 PNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
104-806 |
4.32e-140 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 452.05 E-value: 4.32e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 179
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 180 TGESGAGKTENTKKVIQYLAHVAsshkgrkdhnippespkavKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 259
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-------------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 260 RINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN--GNIPIPgQQDKD 337
Cdd:cd14889 144 QLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREV-QYWKK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 338 NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSPRI 414
Cdd:cd14889 222 KYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKTLTCTVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 415 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd14889 300 FTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 573 HGKFQKPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydVSSLHE 652
Cdd:cd14889 457 NSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF--------------TATRSR 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 653 SPGEVDRIVGLDQvagmNETAFGAAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 732
Cdd:cd14889 521 TGTLMPRAKLPQA----GSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQD 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 733 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 806
Cdd:cd14889 591 QLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
102-806 |
5.47e-136 |
|
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: 440.25 E-value: 5.47e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 174
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 175 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKDHNIPPESPKAVKLqgELERQLLQANPILESFGNAKTVKNDNS 252
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 253 SRFGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPI 330
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGcVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 331 PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK----LCHLLGMNVMEFT 406
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEalatAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 407 RAILSPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFQL-NSF 484
Cdd:cd14891 314 KVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 485 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIDLIErpANPPGVLALLDEECWFPKATD 559
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIA--SKPNGILPLLDNEARNPNPSD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 560 KTFVDKLVQEQGTHGKFQKPRQlKDKAD-FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQStdkfvaelwkdeiqn 638
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 639 fqrASFydvsslhespgevdrivgLDQVAGMNEtafgaayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNH 718
Cdd:cd14891 528 ---AKF------------------SDQMQELVD------------------------------TLEATRCNFIRCIKPNA 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 719 EKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYR 797
Cdd:cd14891 557 AMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYR 636
|
....*....
gi 688558686 798 IGQSKIFFR 806
Cdd:cd14891 637 LGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
102-806 |
5.53e-133 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 431.51 E-value: 5.53e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkavklqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------RQPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQDKDNFQ 340
Cdd:cd14896 143 HLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ--ASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGR 418
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 419 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 497
Cdd:cd14896 302 GRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 498 QLFNHTMFILEQEEYQREGIEWSFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQ 577
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 578 KPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdeiqnFQRASfydvsslhespgev 657
Cdd:cd14896 459 KPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSL-------FQEAE-------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 658 drivgldqvagmnetafgAAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 737
Cdd:cd14896 516 ------------------PQYGLGQGK-PTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQA 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 738 GVLEGIRICRQGFPNRIVFQEFRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14896 577 GILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
102-806 |
1.28e-131 |
|
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: 428.21 E-value: 1.28e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkavklqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA---------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIPIPGQQDKDN 338
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 339 FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASmpenTAAQKLCHLLGMNVMEFTR--AILSPRIKV 416
Cdd:cd14904 223 FASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRI----SNGSQLSQVAKMLGLPTTRieEALCNRSVV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 417 GR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 495
Cdd:cd14904 299 TRnESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 496 LQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGT 572
Cdd:cd14904 379 LQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 573 HGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydvsslhe 652
Cdd:cd14904 455 NESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF-------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 653 spgevdrivglDQVAGMNETAFGAAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 732
Cdd:cd14904 513 -----------GSSEAPSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVE 580
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 733 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 806
Cdd:cd14904 581 QLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
102-806 |
2.96e-130 |
|
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: 425.48 E-value: 2.96e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 171
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 172 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPEspkavklQGELERQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-------KLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 252 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HLRSDLLLEGFNSYRFL 323
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 324 SNGNIPIPGQ-QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPE---NTAAQKLCHLLG 399
Cdd:cd14908 234 GQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 400 MNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFE 477
Cdd:cd14908 314 VDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 478 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-K 556
Cdd:cd14908 393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 557 ATDKTFVDKLV--------QEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLM-KNmdplndnvatllhqstdkf 627
Cdd:cd14908 470 GSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKN------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 628 vaelwKDEIQNfqrasfydvsslhespgevdrivgldqvagmnetafgaaykTKKGMFRTvGQLYKESLTKLMATLRNTN 707
Cdd:cd14908 531 -----KDEIPL-----------------------------------------TADSLFES-GQQFKAQLHSLIEMIEDTD 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 708 PNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-------------- 773
Cdd:cd14908 564 PHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqk 642
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 688558686 774 ---GFMDGKQACERMIRALELDPNL----YRIGQSKIFFR 806
Cdd:cd14908 643 lcvKKMCKDLVKGVLSPAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
102-768 |
1.34e-129 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 424.69 E-value: 1.34e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 171
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 172 REDQSILCTGESGAGKTENTKKVIQYLAHVasshkGRKDHNIPPESPKAVKLQgeleRQLLQANPILESFGNAKTVKNDN 251
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-----GRDQSSTEQEGSDAVEIG----KRILQTNPILESFGNAQTIRNDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 252 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN---GNI 328
Cdd:cd14902 152 SSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 329 PIPGQQDKDN--FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKE-RNTDQASMPENTAAQ--KLCHLLGMNVM 403
Cdd:cd14902 232 RKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 404 EFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAG 475
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 476 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFP 555
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 556 KATDKTFVDKLVQEQGTHGKFqkprqlkdkadfCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDE 635
Cdd:cd14902 469 KGSNQALSTKFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 636 IQNfqrasfydvsslheSPGEVDrivgldqvagmnetafGAAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRC 713
Cdd:cd14902 537 NRD--------------SPGADN----------------GAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRC 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 714 IIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 768
Cdd:cd14902 587 LKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
100-859 |
1.10e-123 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 411.35 E-value: 1.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 100 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 179 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkavklqgelERQLLQANPILESFGNAKTVKNDNSSRFGKF 258
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI--------------QNAIMAANPVLEAFGNAKTIRNNNSSRFGRF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 259 IRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDN 338
Cdd:PTZ00014 251 MQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 339 FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASM--PENTAA-QKLCHLLGMNVMEFTRAILSPR 413
Cdd:PTZ00014 331 FEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFQLNSFEQLCINYTN 493
Cdd:PTZ00014 411 TYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITN 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 494 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQEQGTH 573
Cdd:PTZ00014 490 EMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNN 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 574 GKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvsslhes 653
Cdd:PTZ00014 567 PKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV------------------ 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 654 pgEVDRivgldqvagmnetafgaaYKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 733
Cdd:PTZ00014 628 --EVEK------------------GKLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQ 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 734 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFF-RTGV--L 810
Cdd:PTZ00014 686 LHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAAkeL 765
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 688558686 811 AHLEEERDLKITDIIIYFQSVCRGYLARKAFAKKqqqlsaLKVLQRNCA 859
Cdd:PTZ00014 766 TQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-806 |
1.59e-123 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 406.31 E-value: 1.59e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPEspkavKLQGelerqllqANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE-----KLNA--------ALTVLEAFGNVRTALNGNATRFSQLFSL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSyrflSNGNIPIPGQQDKD---- 337
Cdd:cd01386 144 DFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDkqka 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 338 --NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAI------ 409
Cdd:cd01386 220 aaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhls 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 410 ------LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGfeiFQLN- 482
Cdd:cd01386 300 ggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG---FQNPa 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 483 --------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERP---ANPP--------- 542
Cdd:cd01386 376 hsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrr 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 543 GVLALLDEECWFPKATDKTFVDKLVQEQG--THGKFQKPRQLKDKA-DFCIIHYAGR--VDYKADEWLMK-NMDPLNDNV 616
Cdd:cd01386 456 GLLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 617 ATLLHQSTDKFvaelwkdeiqnfqrasfydvsslhespgevdrivgldqvagmnetafgAAYKtKKGMFRTVgqlyKESL 696
Cdd:cd01386 536 TQLLQESQKET------------------------------------------------AAVK-RKSPCLQI----KFQV 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 697 TKLMATLRNTNPNFVRCIIPNHEkrAGKLEPH--------------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 762
Cdd:cd01386 563 DALIDTLRRTGLHFVHCLLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRR 640
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 688558686 763 YEILTPNAIPKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd01386 641 FQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
103-767 |
6.86e-123 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 405.11 E-value: 6.86e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 170
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 171 --DREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrKDHNIPPESPKAVKLQGElerQLLQANPILESFGNAKTVK 248
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESS------KHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 249 NDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNS--YR 321
Cdd:cd14895 146 NDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAqeFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 322 FLSNGNIPI--PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD---------------QAS 384
Cdd:cd14895 226 YISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 385 MPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK 461
Cdd:cd14895 306 PSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 462 ----------RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPC 531
Cdd:cd14895 386 falnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVC 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 532 IDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKAD--FCIIHYAGRVDYKADEWLMKNM 609
Cdd:cd14895 465 LEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 610 DPLNDNVATLLHQSTDKFVAELWKdeiqnfqrasFYDVSSLHE----SPGEVDRIVGLDQVAgmnetafgaayktkkgmf 685
Cdd:cd14895 541 DQPNAELFSVLGKTSDAHLRELFE----------FFKASESAElslgQPKLRRRSSVLSSVG------------------ 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 686 rtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 765
Cdd:cd14895 593 --IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRL 670
|
..
gi 688558686 766 LT 767
Cdd:cd14895 671 LV 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
102-804 |
4.49e-121 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 398.21 E-value: 4.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIPpespKAVklqgelerqlLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRIQ----TAI----------MAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQ 340
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 341 ETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIK 415
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 416 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFQLNSFEQLCINYTNE 494
Cdd:cd14876 304 AGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 495 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQEQGTHG 574
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 575 KFqKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIqnfqrasfydvsslhesp 654
Cdd:cd14876 459 KF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV------------------ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 655 gevdrivgldQVAGmnetafgaayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 734
Cdd:cd14876 520 ----------VEKG----------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQL 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 735 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 804
Cdd:cd14876 578 HALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-768 |
2.32e-116 |
|
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: 384.97 E-value: 2.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 177
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 178 LCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGK 257
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 258 FIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIpgqqDKD 337
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 338 NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTA---AQKLCHLLGMNVMEFTRAILSPRI 414
Cdd:cd14880 227 CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 415 KVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYT 492
Cdd:cd14880 307 RAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 493 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 573 HGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNfqrasfydvsSLHE 652
Cdd:cd14880 464 GNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEE----------KTQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 653 SPGEVDRIVGLdqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 732
Cdd:cd14880 534 EPSGQSRAPVL-----------------------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLS 590
|
650 660 670
....*....|....*....|....*....|....*.
gi 688558686 733 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 768
Cdd:cd14880 591 QLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-769 |
7.00e-115 |
|
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: 382.79 E-value: 7.00e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 179
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 180 TGESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKavklqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFI 259
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSS-NQQQNNNNNNNNNS-------IEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 260 RINFDVTGYIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEG-FNSYRFL------------- 323
Cdd:cd14906 153 KIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 324 -SNGNIPIPGQQDKD-NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQAS--MPENTAA-QKLCHLL 398
Cdd:cd14906 233 sSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 399 GMNVMEFTRAILSPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQGAS 466
Cdd:cd14906 313 GYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 467 FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLA 546
Cdd:cd14906 393 FIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 547 LLDEECWFPKATDKTFVDKLVQE-QGTHGKFQkpRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTd 625
Cdd:cd14906 470 LLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASS- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 626 kfvaelwkdeiqNFQRASFYDVSSLHESpgevdrivgldqvagmNETafgaaykTKKGMFRTVGQLYKESLTKLMATLRN 705
Cdd:cd14906 546 ------------NFLKKSLFQQQITSTT----------------NTT-------KKQTQSNTVSGQFLEQLNQLIQTINS 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 706 TNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 769
Cdd:cd14906 591 TSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-806 |
2.41e-109 |
|
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: 364.90 E-value: 2.41e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 178
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 179 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippeSPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKF 258
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSS---------NTSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 259 IRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDL-LLEGFNSYRFLSNGNI----PIPG 332
Cdd:cd14875 152 IKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 333 Q--QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAIL 410
Cdd:cd14875 232 KtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 411 sprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFQLNSFEQLCI 489
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 490 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQE 569
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 570 QGTHGK-FQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvs 648
Cdd:cd14875 465 WANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 649 slhesPGEVDRIvgldqvagmnetafgaayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 728
Cdd:cd14875 531 -----KGLARRK-------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNL 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 729 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQS 801
Cdd:cd14875 581 LVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKT 659
|
....*
gi 688558686 802 KIFFR 806
Cdd:cd14875 660 KVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
102-806 |
1.27e-108 |
|
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: 362.28 E-value: 1.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 176 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkavklQGELERQLLQANPILESFGNAKTVKNDNSSRF 255
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 256 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQ 334
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 335 DKDNFQETMEAMHIMsFNHEEILSMLKVVSAVLQFGNIVFKKERN--TDQASMPENTAA-QKLCHLLGMNVMEFTRAILS 411
Cdd:cd14886 223 DQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIIT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 412 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFQLNSFEQLC 488
Cdd:cd14886 302 KVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 489 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVdklvq 568
Cdd:cd14886 378 INYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFT----- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 569 eQGTHGKFQKPRQLKDKA---DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVaelwkdeiqnfqRASFY 645
Cdd:cd14886 450 -SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV------------NKAFS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 646 DVSslhespgevdrivgldqvagmNETAfgaaykTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKL 725
Cdd:cd14886 517 DIP---------------------NEDG------NMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKY 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 726 EPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKI 803
Cdd:cd14886 568 ETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKV 647
|
...
gi 688558686 804 FFR 806
Cdd:cd14886 648 FLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
102-763 |
2.84e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 354.79 E-value: 2.84e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 170
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 171 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPPESPKAVKLQGELERQLLQANPILESFGNAKTVKND 250
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 251 NSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-----AGEHLRSDLLLEGFNSYRFLS 324
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 325 NG--NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-----KKERNT--DQASMPENTAA---- 391
Cdd:cd14899 240 QSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 392 -QKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT---------- 460
Cdd:cd14899 320 fTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 461 ----KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE 536
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 537 RpaNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLN 613
Cdd:cd14899 479 H--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 614 DNVATLLHQSTDKFVAELWKDeiqnfqrasfydvSSLHESPGEVDRIVGLDQVAGMNETAFGAAyktkkgmfrTVGQLYK 693
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALAAG-------------SNDEDANGDSELDGFGGRTRRRAKSAIAAV---------SVGTQFK 614
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 694 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 763
Cdd:cd14899 615 IQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
102-806 |
3.13e-93 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 320.06 E-value: 3.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 173
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 174 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqgeLERQLLQANPILESFGNAKTVKNDNSS 253
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG--------------LEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 254 RFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFnsyrflsngnipiPG 332
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGD-------------PE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 333 QQDKDNFQETMEAMHIMSFNHEEIlsmLKVVSAVLQFGNIVFKKERNTDQASMPENTA--------AQKLCHLL------ 398
Cdd:cd14887 214 STDLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkcls 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 399 -GMNVMEFTRAILS--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 457
Cdd:cd14887 291 sGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 458 DRTKR-------------QGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREG--IEW 519
Cdd:cd14887 371 QRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 520 SFIDFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVDKLVQ--EQ 570
Cdd:cd14887 451 DCSAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKniIN 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 571 GTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLlhqstdkfvaelwkdeiqnFQRASFYdvssl 650
Cdd:cd14887 531 SAKYKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERL-------------------FLACSTY----- 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 651 hespgevDRIVGLDQVAGMNetafgaAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 730
Cdd:cd14887 587 -------TRLVGSKKNSGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYV 650
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 731 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 806
Cdd:cd14887 651 HRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
103-770 |
1.60e-92 |
|
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: 312.99 E-value: 1.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 182
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDvtGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLlegfNSYRFLSNGNIPIPGQQDKDNFQET 342
Cdd:cd14898 139 FD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 343 MEAMHIMSFNHEEILSMlkvvsAVLQFGNIVFKKERNTDQASmpeNTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQ 422
Cdd:cd14898 213 MKSLGIANFKSIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 423 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 502
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 503 TMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLvqeqgthGKFQKPRqL 582
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 583 KDKADFCII--HYAGRVDYKADEWLMKNmdplndnvatllhqsTDKFVAELWKDeiqnfqrasfydvsslhesPGEVDri 660
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-------------------LLIND-- 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 661 vgldqvagmnetafgaayktkKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 740
Cdd:cd14898 474 ---------------------EGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGIL 532
|
650 660 670
....*....|....*....|....*....|
gi 688558686 741 EGIRICRQGFPNRIVFQEFRQRYEILTPNA 770
Cdd:cd14898 533 ETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
99-805 |
8.16e-92 |
|
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: 313.33 E-value: 8.16e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 99 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 168
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 169 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKAVKLQGelerQLLQANPILESFGNAKTVK 248
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTKLSS----QISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 249 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN- 327
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGc 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 328 ---IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMpENTAA-QKLCHLLGMN 401
Cdd:cd14879 223 hplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 402 VMEFtRAILSPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGf 476
Cdd:cd14879 302 PEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPG- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 477 eiFQL------NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDE 550
Cdd:cd14879 376 --FQNrsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 551 EC-WFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD---FCIIHYAGRVDYKADEWLMKNMDPLndnvatllhqSTDk 626
Cdd:cd14879 451 QTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 627 FVAelwkdeiqnfqrasfydvsslhespgevdrivgldqvagmnetafgaayktkkgMFRTVGQLyKESLTKLMATLRNT 706
Cdd:cd14879 520 FVN------------------------------------------------------LLRGATQL-NAALSELLDTLDRT 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 707 NPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMI 786
Cdd:cd14879 545 RLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCAR 618
|
730
....*....|....*....
gi 688558686 787 RALELDPNLYRIGQSKIFF 805
Cdd:cd14879 619 ANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
102-806 |
5.32e-88 |
|
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: 302.50 E-value: 5.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 179 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqgELERQLLQANPILESFGNAKTVKNDNSSRFGKF 258
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT------------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 259 IRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG----NIPIPGQ 333
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 334 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd14878 223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFQLNSFEQLCIN 490
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 491 YTNEKLQQLFNHTMFILEQEEYQREGIewsfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATD 559
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 560 KTFVDKL---VQEQGTHGKFQKPRQ------LKDK-ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVA 629
Cdd:cd14878 450 PNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 630 ELWKDEIQnfqrasfydvsslhespgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPN 709
Cdd:cd14878 530 HLFQSKLV-------------------------------------------------TIASQLRKSLADIIGKLQKCTPH 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 710 FVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRAL 789
Cdd:cd14878 561 FIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLV 637
|
730
....*....|....*....
gi 688558686 790 ELDPNL--YRIGQSKIFFR 806
Cdd:cd14878 638 LQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-806 |
1.30e-85 |
|
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: 295.00 E-value: 1.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAhvasshkgrkdhnippespKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 261
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL-------------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 262 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQE 341
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 342 TMEAMHIMSFnHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENT--AAQKLCHLLGMNVMEFTRAILSPRIKV 416
Cdd:cd14937 218 LMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 417 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 497 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGKF 576
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 577 QKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvSSLHESPGE 656
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-------------VEVSESLGR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 657 VDRIvgldqvagmnetafgaAYKtkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 736
Cdd:cd14937 518 KNLI----------------TFK------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFS 569
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 737 NGVLEGIRIcRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 806
Cdd:cd14937 570 LSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
102-758 |
7.38e-77 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 270.62 E-value: 7.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 173
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 174 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNippespkavklqgELERQLLQANPILESFGNAKTVKNDNSS 253
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT-------------ERIDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 254 RFGKFIRINFD---------VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHLRSDLLLEGFNSYRFL 323
Cdd:cd14884 144 RCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 324 SN----------GNIPIPG----------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerntdqa 383
Cdd:cd14884 224 NPdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 384 smpentaaqkLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ 463
Cdd:cd14884 297 ----------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 464 GA-----------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCI 532
Cdd:cd14884 367 DEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 533 DLIERpanppgVLALLDE-----ECWFPKATDKTFVD-------KLVQEQGTHGK-------FQKPRQLKDKADFCIIHY 593
Cdd:cd14884 446 IFIAK------IFRRLDDitklkNQGQKKTDDHFFRYllnnerqQQLEGKVSYGFvlnhdadGTAKKQNIKKNIFFIRHY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 594 AGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdeiqnfqrasfydvsslhespgevdrivgldqvagmneta 673
Cdd:cd14884 520 AGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE------------------------------------------- 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 674 fgAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 753
Cdd:cd14884 557 --ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK 634
|
....*
gi 688558686 754 IVFQE 758
Cdd:cd14884 635 IPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
103-793 |
5.70e-73 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 257.73 E-value: 5.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 176 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpkavklqgELERQLLQANPILESFGNAKTVKNDNSSRF 255
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET--------DAFKHLAAAFTVLRSLGSAKTATNSESSRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 256 GKFIRINFdVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFN--SYRFLSNGNIPIPGQ 333
Cdd:cd14881 133 GHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 334 QDKDNFQETMEAMHIMSFnheEILSMLKVVSAVLQFGNIVFkKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 413
Cdd:cd14881 212 EDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 414 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFQLNSFE 485
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 486 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKTFVD 564
Cdd:cd14881 364 HLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 565 KLVQEQGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdeiqnfqrasf 644
Cdd:cd14881 440 KIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 645 ydvsslhespgevdrivgldqvagmneTAFGaayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGK 724
Cdd:cd14881 499 ---------------------------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNH 542
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 725 LEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 793
Cdd:cd14881 543 FDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
103-806 |
2.10e-71 |
|
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: 254.25 E-value: 2.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnippespkavklqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN-GNIPIPGQQDKDNF 339
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtdQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 419
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 420 YVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 499
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 500 FNHTMFILEQEEYQREGIEW-SFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGKF-Q 577
Cdd:cd14905 367 YLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 578 KPRQlkdkadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVaeLWKDEIQNFQRA-----SFYDV-SSLH 651
Cdd:cd14905 440 KPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL--FSRDGVFNINATvaelnQMFDAkNTAK 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 652 ESPGEVDRIV------GLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAG 723
Cdd:cd14905 512 KSPLSIVKVLlscgsnNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHL 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 724 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSK 802
Cdd:cd14905 592 TFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTK 669
|
....
gi 688558686 803 IFFR 806
Cdd:cd14905 670 IFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
105-805 |
2.33e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 249.89 E-value: 2.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 105 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 174
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipPESPKAVKLQGELERQLLQANPILESFGNAKTVKNDNSSR 254
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPR------PDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 255 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---LRSDLLL-EGFNSYRFLSN----- 325
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadpla 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 326 GNIPIpgqqDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF------KKERN-------TDQASMPENTAAQ 392
Cdd:cd14893 237 TNFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 393 KL--CHLLGMNVMEF-----TRAILSpriKVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DR 459
Cdd:cd14893 313 ILlaAKLLEVEPVVLdnyfrTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 460 TKRQG----ASFIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWSFIDFGL 526
Cdd:cd14893 390 YEKSNivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 527 DLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD------------FCIIHYA 594
Cdd:cd14893 470 EQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 595 GRVDYKADEWLMKNMDPLNDNVATLLHQStdkfvaelwkdeiqnfQRASFYDVSSLHESPGEVDRIVGLDQVAGMNETAF 674
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSS----------------KNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKF 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 675 G----AAYKTKKGMFRTVGQLYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 750
Cdd:cd14893 612 RksasSARESKNITDSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIF 690
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 751 PNRIVFQEFRQRYeiltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 805
Cdd:cd14893 691 TVHLTYGHFFRRY---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
102-771 |
2.66e-67 |
|
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: 240.93 E-value: 2.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 180
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 181 GESGAGKTENTKKVIQYLAHvasshkgrkdhniPPESPKAVKLQGELERqllqanpILESFGNAKTVKNDNSSRFGKFIR 260
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS-------------QPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 261 INFDvTGYIVGANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNF 339
Cdd:cd14874 131 LLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 340 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPE--NTAAQKLCHLLGMNVMEFTRAILSPRIKV 416
Cdd:cd14874 210 KHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 417 GrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFQLNSFEQLCINYTNEKL 496
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 497 QQLFNHTMFILEQEEYQREGIEwsfIDF----GLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 572
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 573 HGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNFQrasfydvsslhe 652
Cdd:cd14874 438 RSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTS------------ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 653 spgevDRIVgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 732
Cdd:cd14874 505 -----DMIV-------------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNR 554
|
650 660 670
....*....|....*....|....*....|....*....
gi 688558686 733 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 771
Cdd:cd14874 555 QIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
103-766 |
4.03e-60 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 220.00 E-value: 4.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 183 SGAGKTENTKKVIQYLAHVASShkgrkdhnippespkavkLQGELERqLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 262
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDG------------------NRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 263 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHLRSDLLLEGFNsYRFL--SNGNIPIPGQQDKDN 338
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKLKYRRDD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 339 -------FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILS 411
Cdd:cd14882 222 pegnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 412 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFQLNSFEQ 486
Cdd:cd14882 300 YCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 487 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECwfPKATDKTFVDKL 566
Cdd:cd14882 377 LMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYIMDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 567 VQEQgtHGKFQKPrqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfyd 646
Cdd:cd14882 452 IKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNS----------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 647 vsslhespgevdrivgldQVAGMnetafgaayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAG 723
Cdd:cd14882 516 ------------------QVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPR 562
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 688558686 724 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 766
Cdd:cd14882 563 GFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
124-268 |
6.60e-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: 6.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 124 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 202
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 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 ... |
103-804 |
1.42e-58 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 217.01 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 182 ESGAGKTENTKKVIQYLAHVA--SSHKGRKDHNIPPESPKAV---KLQGELERQLLQANPILESFGNAKTVKNDNSSRFG 256
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgSRRLPTNLNDQEEDNIHNEentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 257 KFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDK 336
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 337 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNI-----VFKKE---------------------RNTDQASMPENTA 390
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 391 AQKL-CHLLGMNVMEFTRAILSPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 467
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 468 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANppGVLAL 547
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 548 LDEECWFPKATDKT-FVDKLVQEQGTHGKF-QKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTD 625
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 626 KFVAELwkdeiqnfqrASFYDVSSLHESPGEVDRIvgldqVAGMNETAFGAAYKTKKGMFRTvgqLYKESLTKLMATLRN 705
Cdd:cd14938 558 EYMRQF----------CMFYNYDNSGNIVEEKRRY-----SIQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQET 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 706 TNPNFVRCIIPNHEKRA-GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACER 784
Cdd:cd14938 620 TFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEA 691
|
730 740
....*....|....*....|
gi 688558686 785 MIRALELDPNLYRIGQSKIF 804
Cdd:cd14938 692 LIKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1110-1969 |
3.99e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 147.13 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1110 QAQIDELkiqLAKKEEELQAVLargdEEVA-------QKNNALKQLRELQAQLA-------ELQEDLESEKAARNKAEKL 1175
Cdd:TIGR02168 143 QGKISEI---IEAKPEERRAIF----EEAAgiskykeRRKETERKLERTRENLDrledilnELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1176 KrDLSEELEALKTELEdTLDTTAAQQELRSKREQEvaelkkaiddetrnheSQIQEMRQRHGTALEEISEQLEQAKRVKG 1255
Cdd:TIGR02168 216 K-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELEELTAELQELEEKLEELRLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1256 NLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1335
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1336 KKGIKLTKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEeknnlleqqeeeeesrknlekQLATLQAQLVETKKKL 1415
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET-------LRSKVAQLEL---------------------QIASLNNEIERLEARL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1416 EDDVGALEGLEEVKRKLQKDMEvtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQivsNLEKKQKKFDQMLAEE 1495
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAEREL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1496 KTISAR-YAEERDRAEAEAREKDTKALSMARA--------LDEALEAKEEFER-LNKQLRAEMEDLI-SSKDDVGKNVHE 1564
Cdd:TIGR02168 485 AQLQARlDSLERLQENLEGFSEGVKALLKNQSglsgilgvLSELISVDEGYEAaIEAALGGRLQAVVvENLNAAKKAIAF 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1565 LEKSK--------------RTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF---DRDLQARDEQNEEKKR 1627
Cdd:TIGR02168 565 LKQNElgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1628 ALV-----KQVREMEAELEDERKQRALAVAAK---KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1699
Cdd:TIGR02168 645 YRIvtldgDLVRPGGVITGGSAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1700 RTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQleee 1779
Cdd:TIGR02168 725 SR-------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---- 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1780 leeEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSkFKASIAALEAKIL 1859
Cdd:TIGR02168 794 ---LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1860 QLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS-RRKL 1938
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEY 949
|
890 900 910
....*....|....*....|....*....|....*...
gi 688558686 1939 QRELDDA-------TEASEGLSREVNTLKNRLRRGGPV 1969
Cdd:TIGR02168 950 SLTLEEAealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
896-1727 |
1.01e-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: 145.97 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 896 LIKVKERQVKVENELVEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARL-VAKKQELEEILHDLESRVEEEEERNQ 974
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 975 SLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEE 1054
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1055 EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG 1134
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1135 DEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEvael 1214
Cdd:TIGR02168 417 ERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAEREL---- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1215 kkaidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNK-ELTNEV---KSLQQAKSESEHKRK 1290
Cdd:TIGR02168 485 -----AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEAalgGRLQAVVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1291 K-LEAQLQEVMAR--FSEGEKVKG-ELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQE-ETRQ 1365
Cdd:TIGR02168 560 KaIAFLKQNELGRvtFLPLDSIKGtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAlELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1366 KLNLSSRIRQLEEEK-----------NNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1434
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1435 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERDRAEAEAR 1514
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1515 EKDTKALSMARALDEALEAKEEFERLNKQ---LRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ 1591
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1592 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEkKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEaa 1671
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSE-LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-- 939
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1672 nkardeaikqlRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1727
Cdd:TIGR02168 940 -----------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1073-1839 |
2.02e-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: 141.73 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1073 DLEERLKKEEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1152
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1153 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqELRSKREQEVAELKKAiDDETRNHESQIQEM 1232
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE----------ELKEELESLEAELEEL-EAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1233 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLqqakseSEHKRKKLEAQLQEVMARFSEGEKVKGE 1312
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI------EELLKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1313 LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLLEQQEEEEE 1392
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1393 S---RKNLEKQLAT-----LQAQLVETKKKLEDDVGALEGLEEVK-----------RKLQKDMEVTSQKLEEKAIAFDKL 1453
Cdd:TIGR02168 528 LisvDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1454 EKTKNRLQQELDDLmvdLDHQRqIVSNLE-----KKQKKFDQML--AEEKTISARYAEERdraeaEAREKDTKALSMARA 1526
Cdd:TIGR02168 608 VKFDPKLRKALSYL---LGGVL-VVDDLDnalelAKKLRPGYRIvtLDGDLVRPGGVITG-----GSAKTNSSILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1527 LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQA 1606
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1607 MKAQFDRDLQARDEQNEEKKRAlvkqvremEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ 1686
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEA--------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1687 AQMKDYQRELEEARTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1766
Cdd:TIGR02168 831 RRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1767 RRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSA--------AQKSENARQQLERQNKDLKSKLQE 1838
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 688558686 1839 L 1839
Cdd:TIGR02168 984 L 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1012-1893 |
2.24e-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: 134.81 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1012 EAKIKKMEEDIllleDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKtrQELEKA 1091
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1092 KRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLRELQAQLAELQEDLESEKAARN 1170
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1171 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaidDETRNHESQIQEMRQRHGTALEEIS---EQL 1247
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1248 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1327
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1328 SCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLLEQQEEEEESRknlekq 1400
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNR------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1401 latLQAQLVEtkkkleDDVGALEGLEEVKRK-----------LQKDMEVTSQKLEEKA--------IAFDklEKTKNRLQ 1461
Cdd:TIGR02169 549 ---LNNVVVE------DDAVAKEAIELLKRRkagratflplnKMRDERRDLSILSEDGvigfavdlVEFD--PKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1462 QELDDLMV--DLDHQRQIVSN----------LEKKQKKFDQMLAEEKTISaRYAEERDRAEAEAREKDtkalSMARALDE 1529
Cdd:TIGR02169 618 YVFGDTLVveDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1530 ALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1609
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1610 QFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQM 1689
Cdd:TIGR02169 773 DLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1690 KDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1769
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1770 EARIAQLEEELEEEQSNMELLNDrFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfka 1849
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE--------- 999
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 688558686 1850 siaaleakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQV 1893
Cdd:TIGR02169 1000 --------------------EERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1036-1775 |
2.51e-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: 134.81 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1036 KKLLEDRVGemTSQLAEEEEKAKN-LGKVKNKQEMMMVDLEERLKKEEKTRQELEKA-------KRKLDAETTDLQDQIA 1107
Cdd:TIGR02169 156 RKIIDEIAG--VAEFDRKKEKALEeLEEVEENIERLDLIIDEKRQQLERLRREREKAeryqallKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1108 ELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnkaekLKRDLsEELEALK 1187
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKL----TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-----VKEKI-GELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1188 TELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESD 1267
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1268 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMarfSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvss 1347
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1348 lESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1427
Cdd:TIGR02169 454 -EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1428 VKRKLQKDME-----------VTSQKLEEKAIAFDKLEKTK-------NRLQQELDDL--------------MVDLDHQR 1475
Cdd:TIGR02169 533 VGERYATAIEvaagnrlnnvvVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1476 Q-----------IVSNLEKKQKKFDQM--------LAE-----------EKTISARYAEERDRAEAEAREKDtkalSMAR 1525
Cdd:TIGR02169 613 EpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1526 ALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1605
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1606 AMKAQFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKL 1685
Cdd:TIGR02169 769 ELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1686 QAQMKDYQRELEEARTSRDEIFTQSKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1758
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810
....*....|....*..
gi 688558686 1759 KAALLDEKRRLEARIAQ 1775
Cdd:TIGR02169 926 LEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
864-1658 |
1.47e-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: 129.02 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 864 LRHWQWWRLftkvkpLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEE 943
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 944 MRARLVAKKQELEEILHDLESrveEEEERNQSLQNEKKKmqshiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDIL 1023
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLER---QLEELEAQLEELESK------------------LDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1024 LLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLq 1103
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1104 dQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEEL 1183
Cdd:TIGR02168 434 -ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1184 EAlKTELEDTLDTTAAQQELRSKREQEV-AELKKAIDD-ETRNHESQIQ----------------EMRQRHGTALEeiSE 1245
Cdd:TIGR02168 513 KN-QSGLSGILGVLSELISVDEGYEAAIeAALGGRLQAvVVENLNAAKKaiaflkqnelgrvtflPLDSIKGTEIQ--GN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1246 QLEQAKRVKGNLEKNKQTLESDNK---------ELTNEVKSLQQAksesEHKRKKLEAQLQEVMA---RFSEGEKVKGEL 1313
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNA----LELAKKLRPGYRIVTLdgdLVRPGGVITGGS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1314 ADRTHKI---QTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1390
Cdd:TIGR02168 666 AKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1391 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSqkleekaIAFDKLEKTKNRLQQELDDLMVD 1470
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-------EELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1471 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1550
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1551 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVnMQAMKAQFDRDLQARDEQNEEK 1625
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRL 977
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 688558686 1626 KRAL----------VKQVREMEAELEDERKQRALAVAAKKKLE 1658
Cdd:TIGR02168 978 ENKIkelgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1001-1775 |
3.70e-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: 124.41 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1001 RQKLQLEKVTAEA----KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEE 1076
Cdd:TIGR02169 200 LERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1077 RLKKEEKTRQ-ELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG---DEEVAQKNNALKQL---- 1148
Cdd:TIGR02169 280 KIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelEREIEEERKRRDKLteey 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1149 RELQAQLAELQEDLES-EKAARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhES 1227
Cdd:TIGR02169 360 AELKEELEDLRAELEEvDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1228 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF---- 1303
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRavee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1304 ---SEGEKVKGELAD-----RTHKIQTE------LDNVSCLLEDAEKKGIKLTKDVsslesQLQDTQELLQEETRQKLNL 1369
Cdd:TIGR02169 515 vlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRR-----KAGRATFLPLNKMRDERRD 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1370 SSRIR------------QLEEEKNNLLEQQEEEEESRKNLEKQLATL-QAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1436
Cdd:TIGR02169 590 LSILSedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1437 EVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAE 1512
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1513 AREKDTKALSMARaLDEALEAKEefERLNKqLRAEMEDLisSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1592
Cdd:TIGR02169 750 EQEIENVKSELKE-LEARIEELE--EDLHK-LEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1593 TEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAAN 1672
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1673 KARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKE------NEKKLKSLEAEILQLQEDLASSERARRHAEQERD 1746
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
810 820
....*....|....*....|....*....
gi 688558686 1747 ELADEISNSASGKAALLDEKRRLEARIAQ 1775
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1397-1969 |
4.66e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 117.35 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1397 LEKQLATLQAQ---------LVETKKKLEDDVGAL--EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELD 1465
Cdd:COG1196 198 LERQLEPLERQaekaeryreLKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1466 DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1545
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1546 AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfDRDLQARDEQNEEK 1625
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1626 KRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE 1705
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1706 IftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE-----LADEISNSASGKAALLDEKRRLEARIAQLEEEL 1780
Cdd:COG1196 517 A--GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1781 EEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKilq 1860
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1861 leEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQR 1940
Cdd:COG1196 672 --AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580 590
....*....|....*....|....*....|...
gi 688558686 1941 ELDDATEAS----EGLSREVNTLKNRLRRGGPV 1969
Cdd:COG1196 750 EEALEELPEppdlEELERELERLEREIEALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
881-1579 |
2.00e-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: 115.54 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 881 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 960
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 961 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1040
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1041 DRVGEMTSQLAEEEEKAKNLGKVKNKQEM--------MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI---AEL 1109
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEGY 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1110 QAQIDelkiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE----DLESEKAARNKAEKLKRDLSEELEA 1185
Cdd:TIGR02168 536 EAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVK 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1186 LKTELEDTL-----------DTTAAQQELRSKREQEVAELKK--------AIDDETRNHESQIQEMRQRhgtaLEEISEQ 1246
Cdd:TIGR02168 610 FDPKLRKALsyllggvlvvdDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRRE----IEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1247 LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDN 1326
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1327 VSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQA 1406
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1407 QLVETKKKLEDDVGALEGLEEVKRKLQKD-------MEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1479
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1480 NLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1558
Cdd:TIGR02168 926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFL 1005
|
730 740
....*....|....*....|.
gi 688558686 1559 GKNVHELEKSKRTLEQQVEEM 1579
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEI 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1147-1894 |
9.34e-25 |
|
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: 113.29 E-value: 9.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1147 QLRELQAQLAELQEDLESEKAARNKAEKlkrDLSEELEALKTELEDTLDT----TAAQQELRSKREQEVAELKKA---ID 1219
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVI---DLQTKLQEMQMERDAMADIrrreSQSQEDLRNQLQNTVHELEAAkclKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1220 DETRNHESQIQEMRQ---RHGTALEEISEQLEQAKRVKGnleknKQTLESDNKElTNEVKSLQQAKSESehkRKKLEAQL 1296
Cdd:pfam15921 163 DMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASG-----KKIYEHDSMS-TMHFRSLGSAISKI---LRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1297 QEVMAR-FSEGEKVKGELADRTHKI----QTELDNVSCLLEDAEKKGIKLTKDVSSLESQ---LQDTQELLQEETRQKLn 1368
Cdd:pfam15921 234 SYLKGRiFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1369 lSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLVETKKKLEDDVgalegleevkRKLQKDMEVTSQKLEEKAI 1448
Cdd:pfam15921 313 -SMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI----------EELEKQLVLANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1449 AFDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKTISARYAEERDR-AEAEAREKDTKAL---- 1521
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMksec 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1522 --SMARALdEALEAKEEFERLNKQLRAEMEdliSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQAT--E 1594
Cdd:pfam15921 443 qgQMERQM-AAIQGKNESLEKVSSLTAQLE---STKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1595 DAKLRLEVNMQAMKAQfdrdlqarDEQNEEKkralvkQVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIE-AANK 1673
Cdd:pfam15921 519 ITKLRSRVDLKLQELQ--------HLKNEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1674 ARDEAIKQLRK--LQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1751
Cdd:pfam15921 582 GRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1752 ISNSASGKAALLDEKRRLEARIaqleeelEEEQSNMELLNDRFRkttMQVDTLNTELAGERSAAQKSENA---------- 1821
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNF-------RNKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSMEGSdghamkvamg 731
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1822 -RQQLER---QNKDLKSKLQELEGSVK--SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1894
Cdd:pfam15921 732 mQKQITAkrgQIDALQSKIQFLEEAMTnaNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
231-747 |
1.17e-24 |
|
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: 112.53 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 231 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------KDERTFHVFYQ 299
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 300 LLAGAGEH-----LRSDLLLEGFN--SYRFLSNGNIPIPG--------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVS 364
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 365 AVLQFGNIVFKKERNTDQASMPEN---TAAQKLCHLLGMNVMEFTRAIL---SPRIKVGRDYVQKAQTKEQADFAVEALA 438
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLmtkSVSLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 439 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQqlfnh 502
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 503 tmfileQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKAT----------DKTFVDKLVQEQGT 572
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 573 HGKfQKPRQLKDKA----------DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqra 642
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNES------- 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 643 sfydvSSLHESPgevdrivgldqvaGMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRA 722
Cdd:cd14894 710 -----SQLGWSP-------------NTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQP 770
|
570 580
....*....|....*....|....*
gi 688558686 723 GKLEPHLVLDQLRCNGVLEGIRICR 747
Cdd:cd14894 771 SLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
954-1716 |
1.59e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.47 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 954 ELEEILHDLEsRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQ--------LEKVTAEAKIKKMEEDILLL 1025
Cdd:TIGR02169 171 KKEKALEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1026 EDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1105
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1106 IAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELqedlesEKAARNKAEKLKrDLSEELEA 1185
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------DKEFAETRDELK-DYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1186 LKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLE 1265
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1266 SDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF-------SEGEKVKGELAD-----RTHKIQTE------LDNV 1327
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1328 SCLLEDAEKKGIKLTKDVS------------------------------------------------------------- 1346
Cdd:TIGR02169 553 VVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaa 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1347 ----------SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1416
Cdd:TIGR02169 633 rrlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1417 DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1496
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1497 TISARyaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQV 1576
Cdd:TIGR02169 793 IPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1577 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDR------DLQARDEQNEEKKRALVKQVREMEAELEdERKQRALA 1650
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqieKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEE 949
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1651 VAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEI--FTQSKENEKK 1716
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIleRIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
942-1572 |
1.59e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.26 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 942 EEMRARL--------VAKK-QELEEILHDLESRVeeeeernqsLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE 1012
Cdd:COG1196 196 GELERQLeplerqaeKAERyRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1013 AKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKAK 1092
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1093 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKA 1172
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1173 EKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR 1252
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1253 VKGNLEKNKQTLESDNKELTNEVkslQQAKSESEHKRKKLEAQL---------QEVMARFSEGEKVKGELADRTHKIQTE 1323
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGL---AGAVAVLIGVEAAYEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1324 L------------DNVSCLLEDAEKKGIK-LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1390
Cdd:COG1196 577 LpldkiraraalaAALARGAIGAAVDLVAsDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1391 EESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1470
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEE-------LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1471 LDHQRQIVSNLEkkqkkFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlSMAR-------ALDEALEAKEEFERLNKQ 1543
Cdd:COG1196 730 LEAEREELLEEL-----LEEEELLEEEALEELPEPPDLEELERELERLER-EIEAlgpvnllAIEEYEELEERYDFLSEQ 803
|
650 660
....*....|....*....|....*....
gi 688558686 1544 LraemEDLISSKDDVGKNVHELEKSKRTL 1572
Cdd:COG1196 804 R----EDLEEARETLEEAIEEIDRETRER 828
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1001-1590 |
2.14e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 108.61 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1001 RQKLQLEKV-TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1079
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1080 KEEKTRQELEKAKRkldaETTDLQDQIAELQAQIDELKIQLAKKEEELqavlargdEEVAQKNNALKQLRELQAQLAELQ 1159
Cdd:PRK03918 232 ELEELKEEIEELEK----ELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1160 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ---EVAELKKAID--DETRNHESQIQEMRQ 1234
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1235 RH-GTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE---------------SEHKRKKLeaqLQE 1298
Cdd:PRK03918 380 RLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKEL---LEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1299 VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK--KGIKLTKDVSSLESQLQ--DTQELLQ-----EETRQKLN- 1368
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKkyNLEELEKkaeeyEKLKEKLIk 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1369 LSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAI 1448
Cdd:PRK03918 537 LKGEIKSLKKE-----------LEKLEELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1449 AFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErdraeaEAREKDTKALSMARALD 1528
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELA 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1529 EALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1590
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1356-1921 |
2.65e-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: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1356 QELLQEETRQKLNLSS-RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1434
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1435 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1514
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1515 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1594
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1595 DAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAlvKQVREMEAELEDERKQRALAVAAKKKLEM---------DLKDVE 1665
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavaVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1666 AQIEAANKARDEAIKQ--LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQ 1743
Cdd:COG1196 534 AAYEAALEAALAAALQniVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1744 ERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEeqsnMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQ 1823
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE----GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1824 QLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQY 1903
Cdd:COG1196 690 EEELELEEALLAEEEEE-----------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 688558686 1904 KEQMEKANSRMKQLKRQL 1921
Cdd:COG1196 759 PPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1080-1952 |
5.17e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.46 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1080 KEEKTRQELEKAKRKLDaettDLQDQIAELQAQIDELKIQLAKKEE--ELQAVL--ARGDEEVAQKNNALKQLRELQAQL 1155
Cdd:TIGR02169 171 KKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAERyqALLKEKreYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1156 AELQEDLEsekaarnKAEKLKRDLSEELEALKTELEDtldttaAQQELRSKREQEVAELKKAIDD---ETRNHESQIQEM 1232
Cdd:TIGR02169 247 ASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGEleaEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1233 RQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFsegekvkGE 1312
Cdd:TIGR02169 314 ERE----LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------AE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1313 LADRTHKIQTELDnvsclledaekkgiKLTKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEEknnlleqqeeeee 1392
Cdd:TIGR02169 383 TRDELKDYREKLE--------------KLKREINELKRELDRLQEELQR-------LSEELADLNAA------------- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1393 srknlekqLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDdlmvDLD 1472
Cdd:TIGR02169 429 --------IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA----EAE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1473 HQRQIVSNLEKKQKKFDQMLaeEKTISARYAEERDRAEAEARekdtkalsMARALDEALEAkeefeRLNkqlraemeDLI 1552
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVGER--------YATAIEVAAGN-----RLN--------NVV 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1553 SSKDDVGKNVHELEKSK---RTLEQQVEEMRTQLEELEdelQATEDAKLRLEVNMqamkAQFDRDLQA------RDE--- 1620
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDL----VEFDPKYEPafkyvfGDTlvv 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1621 QNEEKKRALVKQVR--EMEAELEDE--------RKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMK 1690
Cdd:TIGR02169 627 EDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1691 DYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLE 1770
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1771 ARIAQLEEELEEEQsnMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSV------K 1844
Cdd:TIGR02169 786 ARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkK 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1845 SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRqLEEA 1924
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKGE 942
|
890 900
....*....|....*....|....*...
gi 688558686 1925 EEEATRANASRRKLQRELDDATEASEGL 1952
Cdd:TIGR02169 943 DEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
886-1646 |
1.97e-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: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 886 EEEMQAKDEELIKVKERQVKVE-------NELVEMERKHQQLLEEKNILAEQLQAE-TELFAEAEEMRARLVAKKQELEE 957
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 958 ILHDLESRVEEEEERNQSLqNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEakIKKMEEDILLLEDQNSKFLKEKK 1037
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1038 LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK 1117
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1118 IQLAKKEEELQavlaRGDEEVAQKNNALKQLRELQAQLAELQED-----------LESEKAARNKAEKLKRDLSEELEAL 1186
Cdd:TIGR02169 406 RELDRLQEELQ----RLSEELADLNAAIAGIEAKINELEEEKEDkaleikkqewkLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1187 KTELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE----------------EIS 1244
Cdd:TIGR02169 482 EKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1245 EQLEQAKRVKG-------------------------------------------------------NLEKNKQ------- 1262
Cdd:TIGR02169 562 EAIELLKRRKAgratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvveDIEAARRlmgkyrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1263 -TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1341
Cdd:TIGR02169 642 vTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1342 TKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDD--- 1418
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrip 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1419 --VGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1496
Cdd:TIGR02169 795 eiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1497 TISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTlEQQV 1576
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSL 953
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1577 EEMRTQLEELEDELQATEDaklrleVNMQAMKaQFDRDLQARDEQnEEKKRALV---KQVREMEAELEDERKQ 1646
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEVLKRLDEL-KEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
842-1484 |
9.82e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 842 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRLftkvkpllQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL 920
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 921 LEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshIQDLEEQLDEEEAA 1000
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1001 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1080
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1081 EEKTRQELEKAKRKLDAEttdlqdqIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE 1160
Cdd:COG1196 433 LEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1161 DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAL 1240
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1241 EEISEQLEQAKRVKGNLEKNKQTLESDNK----ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADR 1316
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARyyvlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1317 THKIQTEldnvscLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1396
Cdd:COG1196 666 SRRELLA------ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1397 LEKQLATLQAQLVETKKKLEDDVGALEG-LEEVKRKLQK----DMEVtsqkLEEkaiaFDKLEKTKNRLQQELDDLMVDL 1471
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELEReLERLEREIEAlgpvNLLA----IEE----YEELEERYDFLSEQREDLEEAR 811
|
650
....*....|...
gi 688558686 1472 DHQRQIVSNLEKK 1484
Cdd:COG1196 812 ETLEEAIEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1229-1840 |
3.25e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1229 IQEMRQRHGTaLEEISEQLEQAKRVKGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGE 1307
Cdd:COG1196 195 LGELERQLEP-LERQAEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1308 KVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQD-TQELLQEEtrqklnlsSRIRQLEEEKNNLLEQ 1386
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEElEEELAELE--------EELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1387 QEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1466
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1467 LMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalsmARALDEALEAKEEFERLNKQLRA 1546
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1547 EMEDLISSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmqamkaqfDRDLQARDEQNEEKK 1626
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1627 RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARTSRDEI 1706
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1707 FTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSN 1786
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1787 MELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1840
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1165-1723 |
4.25e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 100.91 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1165 EKAARNKAEKLKrdlseELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID---DETRNHESQIQEMRQRHGTaLE 1241
Cdd:PRK03918 161 ENAYKNLGEVIK-----EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisSELPELREELEKLEKEVKE-LE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1242 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQ 1321
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1322 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLLEQQ------------ 1387
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekel 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1388 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdmEVTSQKLEEkaiafDKLEKTKNRLQQELDDL 1467
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE-----EHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1468 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRA- 1546
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSl 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1547 -----EMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR-TQLEELEDELQATE----------DAKLRLEVNMQAMKAQ 1610
Cdd:PRK03918 545 kkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1611 FDRDLQARDEQNEEKKRA--LVKQVREMEAELEDERKQRAlaVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1688
Cdd:PRK03918 625 EEELDKAFEELAETEKRLeeLRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
570 580 590
....*....|....*....|....*....|....*...
gi 688558686 1689 ---MKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAE 1723
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 ... |
1034-1908 |
5.93e-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: 100.82 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1034 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQE--------------LEKAKRKLDAET 1099
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqlkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1100 TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDL 1179
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1180 SEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHgtaLEEISEQLEQAKRVKGNLEK 1259
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1260 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQlqevMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI 1339
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL----KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1340 KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDV 1419
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1420 GALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD--------------HQRQIVSNLEKKQ 1485
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIavleidpilnlaqlDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1486 KKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHEL 1565
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1566 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERK 1645
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1646 QRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQaqmKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1725
Cdd:pfam02463 782 KTEKLKVEEEKEE-KLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1726 QLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1805
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1806 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1885
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
890 900
....*....|....*....|...
gi 688558686 1886 LKEVFMQVEDERRHADQYKEQME 1908
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYL 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
907-1278 |
4.62e-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: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 907 ENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSH 986
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 987 IQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1066
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1067 QEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK 1146
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1147 QLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR----SKREQEVAELKKAIDDET 1222
Cdd:TIGR02168 909 KRSELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1223 RNHESQIQEmrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSL 1278
Cdd:TIGR02168 986 PVNLAAIEE--------YEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1034-1756 |
5.32e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.90 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1034 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQElEKAKRKLDAETTDLQDQIAELQAQI 1113
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA-EDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1114 DELKIQLAKKEEEL-QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnKAEKLKRDLSE---------EL 1183
Cdd:PTZ00121 1174 DAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEakkaeeernNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1184 EALKTELEDTLDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQT 1263
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1264 LESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA--RFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1341
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1342 TKdvSSLESQLQDTQELLQEETRQKLNLSSRI---RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDd 1418
Cdd:PTZ00121 1411 KK--AAAAKKKADEAKKKAEEKKKADEAKKKAeeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE- 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1419 vgALEGLEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQI--VSNLEKKQKKFDQMLAEEk 1496
Cdd:PTZ00121 1488 --AKKKAEEAKKK--------ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEE- 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1497 tisARYAEERDRAEAEAREKDTKALSMARAlDEALEAKEEfeRLNKQLRAEMEDLISSKDDVGKnvHELEKSKRTLEQQV 1576
Cdd:PTZ00121 1557 ---LKKAEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1577 EEMRTQLEELEDELQatEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAlaVAAKKK 1656
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEA--EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1657 LEMDLKDVEA--QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE---IFTQSKENEKKLKSLEAEILQLQEDL 1731
Cdd:PTZ00121 1705 EELKKKEAEEkkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
730 740
....*....|....*....|....*
gi 688558686 1732 ASSERARRHAEQERdELADEISNSA 1756
Cdd:PTZ00121 1785 LDEEDEKRRMEVDK-KIKDIFDNFA 1808
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1034-1618 |
8.29e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 96.65 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1034 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKakrkLDAETTDLQDQIAE----- 1108
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1109 --LQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLE----SEKAARNKAEKLKRD---- 1178
Cdd:PRK02224 275 eeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddl 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1179 ------LSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIddetrnhesqiqemrqrhgtalEEISEQLEQAKR 1252
Cdd:PRK02224 355 eeraeeLREEAAELESELEEA-------REAVEDRREEIEELEEEI----------------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1253 VKGNLEKNKQTLESDNKELTNEVKSlqqaksesehkrkkLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLE 1332
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAE--------------LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1333 DAEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETK 1412
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEER--------------REDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1413 KKLE---DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFD-KLEKTKNRLQQ--ELDDLMVDLDHQRQIVSNLEKKQK 1486
Cdd:PRK02224 537 ERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESleRIRTLLAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1487 KFDQMLAEEKTisaRYAEERDRAEAEAREKDtkalsmARALDEALEAKEEFERLNKQLRAEMEDLISSKDDvgknvheLE 1566
Cdd:PRK02224 617 ALAELNDERRE---RLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQ 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1567 KSKRTLEQQVEEmrtqLEELEDELQATEDAKLRLEV------NMQAMKAQFDRDLQAR 1618
Cdd:PRK02224 681 AEIGAVENELEE----LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
904-1492 |
1.87e-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: 95.47 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 904 VKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKM 983
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 984 QSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1059
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1060 LGKVKNKQEMMMVDLEERLKKEEKTRqELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVA 1139
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1140 QKNNALKQLRELQAQLAELQEDL-----ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL 1214
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1215 KKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA 1294
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1295 QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIR 1374
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1375 QLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE--DDVGALEGLEEVKRKLQKDMEVTSQ-------KLEE 1445
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQtqkslkkKQEE 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 688558686 1446 KAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1492
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1154-1773 |
2.75e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.11 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1154 QLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqelrskrEQEVAELKKAIDDetrnHESQIQEMR 1233
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIE----------------EKEEKDLHERLNG----LESELAELD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1234 qrhgTALEEISEQLEQAKRVKGN----LEKNKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKV 1309
Cdd:PRK02224 220 ----EEIERYEEQREQARETRDEadevLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1310 KGELADRTHKIQTELDNVSCLLEDaekkgikLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqee 1389
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA--------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1390 eeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMV 1469
Cdd:PRK02224 359 -----EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1470 DLdhqrqivSNLEKKQKKFDQMLAEEKTISAryaeerdraeaearEKDTKALSMARALDEALEAKEEferlnkqLRAEME 1549
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKCPEC--------------GQPVEGSPHVETIEEDRERVEE-------LEAELE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1550 DLISSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqfdrDLQARDEQNEEKKRAL 1629
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIA----------------------ERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1630 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1709
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1710 SKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKR-RLEARI 1773
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 ... |
882-1769 |
7.88e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.88 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 882 VTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlVAKKQELEEILHD 961
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 962 LESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1041
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1042 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLdaettdLQDQIAELQAQiDELKIQLA 1121
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------EKLQEKLEQLE-EELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1122 KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTtaaqQ 1201
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1202 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR---VKGNLEKNKQTLESDNKELTNEVKSL 1278
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglkVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1279 QQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ--TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1356
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKlrLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1357 ELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1436
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1437 EVTSQKLEEKAIAfdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREK 1516
Cdd:pfam02463 697 RQLEIKKKEQREK--EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1517 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDA 1596
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1597 KLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARD 1676
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1677 EAIKQLRKLQAQMKDYQRELEEartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSA 1756
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKE---------EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 688558686 1757 SGKAALLDEKRRL 1769
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
888-1579 |
2.62e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 888 EMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVE 967
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 968 EEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEdillledqNSKFLKEKKLLEDRVGEM 1046
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEE--------KKKADEAKKAEEKKKADE 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1047 TSQLAEEEEKAKNLGK----VKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAettdlqdqiAELQAQIDELKIQLAK 1122
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---------AEEKAEAAEKKKEEAK 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1123 KEEElqaVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRdlseeLEALKTELEDTLDTTAA 1199
Cdd:PTZ00121 1378 KKAD---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEA 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1200 QQELRSKREQEvaELKKAIDDETRNHESQIQEMRQRHGTAL----EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1275
Cdd:PTZ00121 1450 KKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1276 KSLQQAKS-----ESEHKRKKLEAQLQEVMARFSEGEKVkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1350
Cdd:PTZ00121 1528 KKAEEAKKadeakKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1351 QLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLVETKKKLEDDVGALEGLEE 1427
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEelkKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1428 VKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisARYAEE 1505
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEE 1754
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1506 RDRAEAEAREKDTKALSMARALDEALeAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1579
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM 1827
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
929-1307 |
3.52e-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: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 929 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEK 1008
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1009 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEmtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQEL 1088
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1089 EKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA 1168
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1169 RNKAEKLKRDLSEELEALKTELedtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtALEEIS---- 1244
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-----ALEPVNmlai 978
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1245 EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKR-KKLEAQLQEVMARFSEGE 1307
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 ... |
877-1726 |
6.75e-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: 90.80 E-value: 6.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 877 KPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL-LEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL 955
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLeLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 956 EEILHDLESRVEEEEERNQSLQN-EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1034
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1035 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1114
Cdd:pfam02463 336 EIEELE--------KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1115 ELKIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK---AEKLKRDLSEELEALKTELE 1191
Cdd:pfam02463 408 QLLLELARQLEDLLKEEK--KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdelELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1192 DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE- 1270
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQk 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1271 LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1350
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1351 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKR 1430
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1431 KLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1510
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1511 AEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1590
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1591 QATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElEDERKQRALAVAAKKKLEMDLKDVEAQIEA 1670
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE-EEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1671 ANKARDEAIKQLRKLQAQMKdyqrELEEARTSRDEIFTQSKENEKKLKSLEAEILQ 1726
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 ... |
1319-1965 |
8.51e-18 |
|
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: 90.62 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1319 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1398
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1399 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1478
Cdd:pfam01576 96 NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1479 SNLEKKQKKFDQMLAEektisaryAEERDRAEAEAREkdtkalsmaraldealeakeEFERLNKQLRAEMEDLISSKDDv 1558
Cdd:pfam01576 176 KSLSKLKNKHEAMISD--------LEERLKKEEKGRQ--------------------ELEKAKRKLEGESTDLQEQIAE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1559 gknvhelekskrtLEQQVEEMRTQLEELEDELQAtedAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEA 1638
Cdd:pfam01576 227 -------------LQAQIAELRAQLAKKEEELQA---ALARLE------------EETAQKNNALKKIRELEAQISELQE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1639 ELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARTSRDEIFTQSKENEKKL 1717
Cdd:pfam01576 279 DLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1718 KSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1797
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1798 TMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQElEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANK 1877
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1878 IVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVN 1957
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 688558686 1958 TLKNRLRR 1965
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
870-1466 |
3.91e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.20 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 870 WRLFTKVKPLLQVTRQEEEMQAKDEEliKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLV 949
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 950 AKKQELEEilhdLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlEKVTAEAKIKKMEEDILLLEDQN 1029
Cdd:PRK03918 242 ELEKELES----LEGSKRKLEEKIRELEERIEELKKEIEELE---------------EKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1030 SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDaETTDLQDQIAEL 1109
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1110 QAQIDELKIQlaKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE-----LE 1184
Cdd:PRK03918 378 KKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1185 ALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDE---TRNHE--SQIQEMRQR-HGTALEEISEQLEQAKRVKGNLE 1258
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKElaEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1259 KNKQTLESDNKELtNEVKSLQQAKSESEHKRKKLEAQLQEVMAR-----FSEGEKVKG-------------ELADRTHKI 1320
Cdd:PRK03918 536 KLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEErlkelepfyneylELKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1321 QTELDNVSCL---LEDAEKKGIKLTKDVSSLESQLQDTQELLQEET-----RQKLNLSSRIRQLEEEKNNLLEQQEEEEE 1392
Cdd:PRK03918 615 EREEKELKKLeeeLDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1393 SRKNLEKQLATLQaqlvETKKKLEDDVGALEGLEEVKRKLQKdmevtsQKLEEKAIAFDKLEKTKNRLQQELDD 1466
Cdd:PRK03918 695 TLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKK------YKALLKERALSKVGEIASEIFEELTE 758
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
934-1772 |
2.30e-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: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 934 ETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKkmqshiQDLEEQLDEEEAARQKLQLEKVTAEA 1013
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1014 KIKKMEEDILLLEDQNSKFLKEkklledrvgemtsqlaeeeekakNLGKVKNKQEMmmvdleerlkkEEKTRQELEKAKR 1093
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1094 KLDAETTDLQDQIAELQAQIdelkiqlAKKEEELQAVLARGDEEVAqknnalKQLRELQAQLAELQEDLES-EKAARNKA 1172
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRR-------SKIKEQNNRDIAGIKDKLA------KIREARDRQLAVAEDDLQAlESELREQL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1173 EKLKRDLSEELEALKTELEDT---LDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQ-LE 1248
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGELklrLNQATATPELLLQLENFDERIERA--REEQEAANAEVERLQSELRQARKRRDQaSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1249 QAKRVKGNLEKNKQTLEsdnkeltnEVKSLQQAKSESEHKRKKLEAQLQevmarfsegEKVKGELADRTHKIQTELDNVS 1328
Cdd:pfam12128 507 ALRQASRRLEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDW---------EQSIGKVISPELLHRTDLDPEV 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1329 clleDAEKKGIKLTKDVSSLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQL 1408
Cdd:pfam12128 570 ----WDGSVGGELNLYGVKLDLKRIDVPEWAASE-----------EELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1409 VETKKKLEDDVGALEGLEEVKRKLqkdmevTSQKLEEKaiafDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKF 1488
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRL------FDEKQSEK----DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAW 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1489 DQMLAEEKTiSARYAEERDRAEAEAREKDTKAlsmarALDEALEAKEE-FERLNKQLRAEMEDLISSKDDVGKNVHELEK 1567
Cdd:pfam12128 702 LEEQKEQKR-EARTEKQAYWQVVEGALDAQLA-----LLKAAIAARRSgAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1568 SKRTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFDRDLQardEQNEEKKRALVKQVREMEAELEDERKQR 1647
Cdd:pfam12128 776 EIRTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1648 ALAVAAKKkleMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARTSRDEIFTQSKENEKKLKSLEA 1722
Cdd:pfam12128 831 ARLIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSE 907
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1723 EILQLQEDLASSERARRHAEQER--DELADEISNSASGKAALLDEKRRLEAR 1772
Cdd:pfam12128 908 SVKKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1075-1650 |
2.92e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.35 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1075 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLA----KKEEELQAVLARGDEEVAQKNNALKQLR- 1149
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEa 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1150 --------------ELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1215
Cdd:COG4913 367 llaalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1216 KAIDDETRNHESQIQ------EMRQR------------HGTALEEISEQlEQAKRVKGNLEKNKQTLESDNKELTNEVKS 1277
Cdd:COG4913 447 DALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFALTLLVPP-EHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1278 LQQAKSESEHKRKKLEAQ-------LQEVMARF-------SEGE------------KVKGELADRTHKIQTELDNVSCLL 1331
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKphpfrawLEAELGRRfdyvcvdSPEElrrhpraitragQVKGNGTRHEKDDRRRIRSRYVLG 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1332 EDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeknnLLEQQEEEEESRKNLEKQLATLQAQLvet 1411
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAEL--- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1412 kKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkFDQM 1491
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1492 LAE------EKTISARYAEERDRAEAEAREKDTKALSMARA-----------LDEALEAKEEFERLNKQLRAemEDLISS 1554
Cdd:COG4913 755 FAAalgdavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLESLPEYLALLDRLEE--DGLPEY 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1555 KDDVGKNVHELEKSKRT-----LEQQVEEMRTQLEELEDELQATE---DAKLRLEVNMQ--AMKAQFDRDLQA------- 1617
Cdd:COG4913 833 EERFKELLNENSIEFVAdllskLRRAIREIKERIDPLNDSLKRIPfgpGRYLRLEARPRpdPEVREFRQELRAvtsgasl 912
|
650 660 670
....*....|....*....|....*....|...
gi 688558686 1618 RDEQNEEKKRALVKQVREMEAELEDERKQRALA 1650
Cdd:COG4913 913 FDEELSEARFAALKRLIERLRSEEEESDRRWRA 945
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
885-1724 |
9.01e-16 |
|
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: 83.94 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 885 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLES 964
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 965 RVEEEEERNQSLQ----------NEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1034
Cdd:TIGR00606 277 RKKQMEKDNSELElkmekvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1035 E-------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIA 1107
Cdd:TIGR00606 357 DrhqehirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1108 ELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAEL--------------------QEDLESEKA 1167
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaeknsltetlkkevkslqNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1168 ARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL---------KKAIDDETRNHESQIQEMRQRHGT 1238
Cdd:TIGR00606 517 LRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1239 ALEEIsEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE---------AQLQEVMARFSEGEKV 1309
Cdd:TIGR00606 596 LNKEL-ASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1310 KGE----LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLL 1384
Cdd:TIGR00606 675 ENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEkRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1385 EQQEEEEESRKNL---EKQLATLQAQLvETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLE--EKAIAFDKLEKTKNR 1459
Cdd:TIGR00606 755 KVNRDIQRLKNDIeeqETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQE 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1460 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA---EAREKDTKALSMARALDEALEAKEE 1536
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQDSP 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1537 FERLNKQLRAEMEDLISSKDDVGKNVH-ELEKSKRTLEQQVEEMRTQLEELEDelqATEDAKLRLEVNMQAMKAQFdrdl 1615
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL---- 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1616 qardEQNEEKKRALVKQVREMEAELEDERKQRALAV--AAKKKLEMDLKDVEAQIeaanKARDEAIKQLRKLQaQMKDYQ 1693
Cdd:TIGR00606 987 ----EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEEL----KQHLKEMGQMQVLQ-MKQEHQ 1057
|
890 900 910
....*....|....*....|....*....|....
gi 688558686 1694 RELEEARTSRDE---IFTQSKENEKKLKSLEAEI 1724
Cdd:TIGR00606 1058 KLEENIDLIKRNhvlALGRQKGYEKEIKHFKKEL 1091
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
887-1602 |
9.96e-16 |
|
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: 83.63 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 887 EEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRARLVAKK---QELEEILHDLE 963
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 964 srveeeeernqslQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQNSKFLKEKK-----L 1038
Cdd:pfam15921 198 -------------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1039 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK-EEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELK 1117
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1118 IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTT 1197
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1198 AAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISE---QLEQAK----RVKGNLEKNKQTLESDNKE 1270
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKemlrKVVEELTAKKMTLESSERT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1271 LTNEVKSLQQAK-------SESEHKRKKLEAQLQEVMARFSEG----------EKVKGELADRTHKIQ---TELDNVSCL 1330
Cdd:pfam15921 498 VSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKDKVIEilrQQIENMTQL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1331 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeESRKNLEK-QLATLQAQLV 1409
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR------------VSDLELEKvKLVNAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1410 ETKKKLEDDVGALegLEEVK------RKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1483
Cdd:pfam15921 646 RAVKDIKQERDQL--LNEVKtsrnelNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1484 KQ-KKFDQMLAEEKTISARyaeerdRAEAEAREKDTKAL--SMARALDEALEAKEEFERLNKqlraEMEDLISSKDDVGK 1560
Cdd:pfam15921 721 SDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLeeAMTNANKEKHFLKEEKNKLSQ----ELSTVATEKNKMAG 790
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 688558686 1561 NVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1602
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
884-1484 |
1.02e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 884 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLE 963
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 964 SRVEEEEERNQSLQN--EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEdillledqnSKFLKEKKLLED 1041
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---------KKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1042 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaETTDLQDQIAELQAQIDELKIQ-- 1119
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEev 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1120 --LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRdlSEELEALKTELEdtldtt 1197
Cdd:PTZ00121 1598 mkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE------ 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1198 aAQQELRSKREQEvaELKKAIDDETRNHESQIQEmrqrhgtalEEISEQLEQAKrvKGNLEKNKQTLESDNKELTNEVKS 1277
Cdd:PTZ00121 1667 -AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE---------AEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKA 1732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1278 LQQAKSESEHKRKKLEAQLQE------VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1351
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1352 --------LQDTQELLQEETRQKLNLSSriRQLEEEKNNLLEQQEEEEESRKNLEKqlatlQAQLVETKKKLEDDVGALE 1423
Cdd:PTZ00121 1813 ggkegnlvINDSKEMEDSAIKEVADSKN--MQLEEADAFEKHKFNKNNENGEDGNK-----EADFNKEKDLKEDDEEEIE 1885
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1424 GLEEVKRKLQKDMEV----TSQKLEEKAIAFDKLEKTKNRLQqelddlmvDLDHQRQIVSNLEKK 1484
Cdd:PTZ00121 1886 EADEIEKIDKDDIEReipnNNMAGKNNDIIDDKLDKDEYIKR--------DAEETREEIIKISKK 1942
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1326-1845 |
1.26e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1326 NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNNLLEQQEEEEEsrknLEKQLATLQ 1405
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELE-------KLEKEVKELEELKEEIEELEKELES----LEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1406 AQLVETKKKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1485
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1486 KKFDQMLAEEKTISARYAEERDRAEAeaREKDTKALSMARALdealeaKEEFERLNKQLRAEmedlisSKDDVGKNVHEL 1565
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAK------KEELERLKKRLTGL------TPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1566 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFDRDLQARDEQNEEKKRALvkqvREMEAELEDERK 1645
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL----EEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1646 QRALAVAAKKKLEMDLKDVEAQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARTSRDEIFTQSKENEKKLKSLEA 1722
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1723 EILQLQE---DLASSERARRHAEQERDELADEISNSASGKAALLDEK---------------------RRLEARIAQLEE 1778
Cdd:PRK03918 547 ELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelEREEKELKKLEE 626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1779 ELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSaaQKSENARQQLERQNKDLKSKLQELEGSVKS 1845
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
863-1561 |
1.44e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 863 KLRHWQWWRLFTKVKPLLQVTRQ---EEEMQAKDEELIKVKERQVKVENELVEMERKhqqlLEEKNILAEQLQAETELFA 939
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 940 EAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQ-NEKKKMQSHIQDLEEQLDEEEAARQ-----KLQLEKVTAEA 1013
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKaeekkKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1014 KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQELEKAKR 1093
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1094 KLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAE 1173
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1174 KLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAlEEISEQLEQAKRV 1253
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1254 ----KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRthkiqteldnvsc 1329
Cdd:PTZ00121 1636 eqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKK------------- 1696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1330 llEDAEKKGIKLTKdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLLEQQEEEEESRKNLEKQLATLQAQLV 1409
Cdd:PTZ00121 1697 --EAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK--KKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1410 ETKKKLEDDVgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ-KKF 1488
Cdd:PTZ00121 1771 EEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAF 1849
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1489 DQMLAEEKTISaryAEERDRAEAEAREKDTKalsmaRALDEALEAKEEFERLNKQlraEMEDLISSKDDVGKN 1561
Cdd:PTZ00121 1850 EKHKFNKNNEN---GEDGNKEADFNKEKDLK-----EDDEEEIEEADEIEKIDKD---DIEREIPNNNMAGKN 1911
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1241-1960 |
1.56e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1241 EEISEQLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmARFSEGEKVKGELADRT 1317
Cdd:PTZ00121 1053 DGNHEGKAEAKAHVGQDEGLKPSYkdfDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1318 HKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL 1397
Cdd:PTZ00121 1131 EEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1398 EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKlqkdmevtsqklEEKAiafDKLEKTKNRLQ-QELDDLMVDLDHQRQ 1476
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAE----AVKKAEEAKKD------------AEEA---KKAEEERNNEEiRKFEEARMAHFARRQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1477 IVSNLEKKQKKFDQMLAEE--KTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISS 1554
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEkkKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1555 KDDVGKNVHELEKSKR---TLEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKaQFDRDLQARDEQNEEKKRA 1628
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEkaeAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1629 L-VKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIF 1707
Cdd:PTZ00121 1428 EeKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1708 TQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE---LADEISNSASGKAAllDEKRRLEARIAQLEEELEEEQ 1784
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1785 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLE--RQNKDLKSKLQEL----EGSVKSKFKASIAALEAKI 1858
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLkkkeAEEKKKAEELKKAEEENKI 1661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1859 LQLEEQLEQEAKERAAAN-KIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeAEEEATRANASRRK 1937
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKE 1738
|
730 740
....*....|....*....|....*
gi 688558686 1938 LQRELDDATEA--SEGLSREVNTLK 1960
Cdd:PTZ00121 1739 AEEDKKKAEEAkkDEEEKKKIAHLK 1763
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
900-1728 |
3.42e-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: 82.09 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 900 KERQVKVENELVEMERKHQQLLEEKNILAEQlqaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNE 979
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEK---------QKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 980 KKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDilLLEDQNSKFLKEKKLL---EDRVGEMTSQLAEEEEK 1056
Cdd:pfam15921 144 RNQLQNTVH----------------ELEAA------KCLKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1057 AKNlgKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI-DELKIQLAKKEEELQAVLARGD 1135
Cdd:pfam15921 200 SGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1136 EEVA----QKNNALKQLRELQAQLAELQEDlesekaARNKAEKLKRDLSE----------ELEALKTELEDTLDTTAAQQ 1201
Cdd:pfam15921 278 VEITglteKASSARSQANSIQSQLEIIQEQ------ARNQNSMYMRQLSDlestvsqlrsELREAKRMYEDKIEELEKQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1202 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA 1281
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1282 KSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL---TKDVSSLESQLQDTQEL 1358
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLessERTVSDLTASLQEKERA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1359 LQEETRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEV 1438
Cdd:pfam15921 512 IEATNAEITKLRSRV----DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1439 TSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfDQMLAEEKTISAryAEERDRAEAEAREKDT 1518
Cdd:pfam15921 585 AGAMQVEKA----QLEKEINDRRLELQEFKILKDKKDAKIRELEARVS--DLELEKVKLVNA--GSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1519 KALSMARALDEALEA-KEEFERLNKQLRAEMEdlisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1597
Cdd:pfam15921 657 QLLNEVKTSRNELNSlSEDYEVLKRNFRNKSE--------------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1598 ---LRLEVNMQ----AMKAQFDrdlqardeqneekkrALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQiea 1670
Cdd:pfam15921 723 ghaMKVAMGMQkqitAKRGQID---------------ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE--- 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1671 ankaRDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQ 1728
Cdd:pfam15921 785 ----KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1398-1965 |
4.59e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1398 EKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafdklEKtknrlQQELDDLMVDLDHQRQI 1477
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1478 VSNLEKKQKKFDQMLAEEKTISARYAEERD--RAEAEAREKDTKALSMARaldEALEAKEEferlnkQLRAEMEDLISSK 1555
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARR---EELEDRDE------ELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1556 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdRDLQARDEQNEEKKRALVKQVRE 1635
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---------------EDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1636 MEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAikqlRKLQAQMK--DYQRELEEArtsrdEIFTQSKEN 1713
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA----EALLEAGKcpECGQPVEGS-----PHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1714 EKKLKSLEAEILQLQEDLASSErarrhaeqERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDR 1793
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1794 frkttmqVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfkASIAALEAKILqleeqleqeakerA 1873
Cdd:PRK02224 546 -------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIA-------------D 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1874 AANKIVRRTEKKlkEVFMQVEDERRhadqykEQMEKANSRMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEA 1948
Cdd:PRK02224 604 AEDEIERLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
570
....*....|....*..
gi 688558686 1949 SEGLSREVNTLKNRLRR 1965
Cdd:PRK02224 676 RDDLQAEIGAVENELEE 692
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1283-1964 |
4.85e-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: 81.65 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1283 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV----SCLLEDAEKKGIKLTKDVSSLESQLQDTQEL 1358
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1359 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL-EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKLQKDME 1437
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIA----SLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1438 VTSQKLEEKaiaFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKD 1517
Cdd:TIGR02169 322 ERLAKLEAE---IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1518 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1597
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1598 LRLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELE------------DERKQRALAVAAKKKLEMDLKDVE 1665
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1666 AQIEaankardEAIKQLRKLQA---------QMKDYQRELEEARTS------------------------RDEIFTQSKE 1712
Cdd:TIGR02169 558 AVAK-------EAIELLKRRKAgratflplnKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfGDTLVVEDIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1713 NEKKLK------SLEAEILQLQEDLASSERARRHAE-------QERDELADEISNSASGKAALLDEKRRLEARIAQLEEE 1779
Cdd:TIGR02169 631 AARRLMgkyrmvTLEGELFEKSGAMTGGSRAPRGGIlfsrsepAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1780 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEA--- 1856
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEArls 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1857 --KILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS 1934
Cdd:TIGR02169 790 hsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750
....*....|....*....|....*....|
gi 688558686 1935 RRKLQRELDDATEASEGLSREVNTLKNRLR 1964
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1160-1890 |
1.32e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1160 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQrhgta 1239
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1240 lEEISEQLEQAKRVkgnlEKNKQTLESDNKEltnEVKSLQQAKSESEHKRKKLEAQLQEVmaRFSEGEKvKGELADRTHK 1319
Cdd:PTZ00121 1166 -AEEARKAEDAKKA----EAARKAEEVRKAE---ELRKAEDARKAEAARKAEEERKAEEA--RKAEDAK-KAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1320 IQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEK 1399
Cdd:PTZ00121 1235 AKKDAEEAK--KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1400 QlATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQElddlmvdldhqrQIVS 1479
Cdd:PTZ00121 1310 K-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAA------------EKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1480 NLEKKQKKFDQMLAEEKtisaRYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVG 1559
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1560 KNVHELEKSKRTLEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFDRDLQARDEQNEEKKRALVKQVREME 1637
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1638 AELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1717
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1718 KSLEA----EILQLQEDLASSERARRHAEQERDELADEISNS---------ASGKAALLDEKRRLEARIAQLEEELEEEQ 1784
Cdd:PTZ00121 1608 KAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1785 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQ---KSENAR----QQLERQNKDLKSKLQEL--EGSVKSKFKASIAALE 1855
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENkikaEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEE 1767
|
730 740 750
....*....|....*....|....*....|....*..
gi 688558686 1856 AKILQLEEQLEQEAKERAAANKIVRR--TEKKLKEVF 1890
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDIF 1804
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1149-1858 |
1.39e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1149 RELQAQLAELQEDLESEKAARNKAEKLKR--DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaiDDETRNHE 1226
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR---LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1227 SQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE-LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1305
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1306 GEKvkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlle 1385
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL--------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1386 qqeeeeesRKNLEKQLATLQAQ------LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNR 1459
Cdd:COG4913 446 --------RDALAEALGLDEAElpfvgeLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1460 LQqelddlmVDLDHqrqivsnLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFE 1538
Cdd:COG4913 512 GR-------LVYER-------VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1539 RLNKQLRAEmeDLISSkddvGKNVHELEKSKRTLEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQ 1616
Cdd:COG4913 572 RHPRAITRA--GQVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEA--------LE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1617 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAvaakkklemdlkDVEAQIEAANKARDEaikqLRKLQAQMKDYQREL 1696
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIA------------ELEAELERLDASSDD----LAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1697 EEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQL 1776
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1777 EEELEEEQSNMELLNDRFRKT-TMQVDTLNTELAGERSAAQKsenaRQQLERQnkDLKSKLQELEGSVKSKFKASIAALE 1855
Cdd:COG4913 779 RARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEED--GLPEYEERFKELLNENSIEFVADLL 852
|
...
gi 688558686 1856 AKI 1858
Cdd:COG4913 853 SKL 855
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
894-1569 |
2.08e-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: 79.00 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 894 EELIKVKERQVKVENELVEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHD----------LE 963
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 964 SRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIK-KMEEDILLLEDQNSKFLKEKKLLEDR 1042
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1043 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTD----LQDQIAELQAQIDELKI 1118
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1119 ------QLAKKEE----ELQAVLARGDEEVAQKNNALKQLREL-----------QAQLAELQEDLESEKAARNKAEKLKR 1177
Cdd:pfam05483 322 atkticQLTEEKEaqmeELNKAKAAHSFVVTEFEATTCSLEELlrteqqrleknEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1178 DLSEELEALKT---ELEDTLDTTAAQQELRSK---REQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISEQLE 1248
Cdd:pfam05483 402 NKEVELEELKKilaEDEKLLDEKKQFEKIAEElkgKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1249 QAKRVKGNLEKNKQTLESDNKELTNE----VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1324
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1325 DNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1404
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1405 QAQLVETKKKLEDDVGALEGLEEVKRklqkdmeVTSQKLEEKAIAFDKLEKTKNRLQQELDdlmVDLDHQ-RQIVSNLEK 1483
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKK-------ISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKiAEMVALMEK 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1484 KQKKFDQMLaeektisaryaEERDRAEAEAREKDTKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNV 1562
Cdd:pfam05483 712 HKHQYDKII-----------EERDSELGLYKNKEQEQSSAKAALEIELSnIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
....*..
gi 688558686 1563 HELEKSK 1569
Cdd:pfam05483 781 AILKDKK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
879-1464 |
2.23e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 879 LLQVTRQEEEMQAKDeelikVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLvakkQELEEI 958
Cdd:PRK02224 189 LDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 959 LHDLESRVEEEEERNQSLQNEkkkmqshIQDLEeqldeeeAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1038
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE-------VRDLR-------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1039 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1118
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDAD-------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1119 QLAKKEEELQAVLARGDEEVAQKNnalkqlrELQAQLAELQEDLESEKAARNKAEKLKR-----------------DLSE 1181
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1182 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID--DETRNHESQIQEMRQRHGTALEEISEQLEQakrvkgnLEK 1259
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEE-------LRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1260 NKQTLEsdnkeltnevkslqqakSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTeLDNVSCLLEDAEKKGi 1339
Cdd:PRK02224 545 RAAELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1340 kltKDVSSLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEknNLLEQQEEEEESRKNLEKQLATLQ---AQLVETKKKL 1415
Cdd:PRK02224 606 ---DEIERLREKREALAE-LNDERRERLaEKRERKRELEAE--FDEARIEEAREDKERAEEYLEQVEeklDELREERDDL 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1416 EDDVGALEG----LEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQQEL 1464
Cdd:PRK02224 680 QAEIGAVENeleeLEELRERR-EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
879-1627 |
4.56e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 879 LLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQqlleeknilaEQLQAETELFAEAEEMRARLVAKKQELEEI 958
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE----------KELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 959 LHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1038
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1039 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1118
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1119 QLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA 1198
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1199 AQQELRSKREQEVAELKKAIDDETRNHES---QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1275
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEgilKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1276 KSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDT 1355
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1356 QELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQL---VETKKKLEDDVGALEGLEEVKRKL 1432
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELkeeAELLEEEQLLIEQEEKIKEEELEE 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1433 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAE 1512
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELL-----LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1513 AREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQA 1592
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-------EEEERNKRLLLAKEELGKVNLMAIEEFEE 985
|
730 740 750
....*....|....*....|....*....|....*
gi 688558686 1593 TEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1627
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1241-1909 |
5.75e-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: 77.75 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1241 EEISEQLEQAKRVKGNLEKNKQ---TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegEKVKGELADRT 1317
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDkinKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKEN-------KKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1318 HKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLS---SRIRQLEEEKNNLLEQQEEEEESR 1394
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1395 KNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL--MVDLD 1472
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1473 HQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEME 1549
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1550 DLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaKLRLEVNmqamkaqfdrDLQARDEQNEEKKRAL 1629
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE-----RLKETII----------KNNSEIKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1630 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1709
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1710 SKENEKKLKSLEAEILQLQEDLASSErarrhAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1789
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1790 -------LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkSKFKASIAALE--AKILQ 1860
Cdd:TIGR04523 608 kekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII----KKIKESKTKIDdiIELMK 683
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558686 1861 LEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEK 1909
Cdd:TIGR04523 684 DWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
842-1494 |
6.16e-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: 77.70 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 842 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELiKVKERQVKVENELVEMERKHQQLL 921
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 922 EEKNILAEQLQaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAAR 1001
Cdd:TIGR00618 297 AHIKAVTQIEQ-------QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1002 QKLQleKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKE 1081
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1082 EKTRQ-------ELEKAKRKLDAETTDLQDQ-----------------IAELQAQIDELKIQLAKKEEELQAV------- 1130
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1131 --LARGDEEVAQKNNALK----QLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1204
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1205 SK-----REQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQL------EQAKRVKGNLEKNKQTLESDNKELTN 1273
Cdd:TIGR00618 608 DMlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1274 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvSSLESQLQ 1353
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA-RTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1354 DTQELLQEETRQKL-----NLSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLvetKKKLEDDVGALEGLEEv 1428
Cdd:TIGR00618 767 NEEVTAALQTGAELshlaaEIQFFNRLREE------------------DTHLLKTLEAEI---GQEIPSDEDILNLQCE- 824
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1429 krKLQKDMEVTSQKLEEkaiafdklektKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1494
Cdd:TIGR00618 825 --TLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
916-1665 |
1.02e-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: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 916 KHQQLLEEKNILAEQLQAETELfaeAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQshiqdleeqld 995
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLC---TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 996 eeeaARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFlkekklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLE 1075
Cdd:TIGR00618 254 ----EQLKKQQLLKQLRARIEELRAQEAVLEETQERI------------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1076 ERLKKEEKTRQELEKAKrKLDAETTDLQDQIAELQAQIDELKIQ-----LAKKEEELQAVLARGDEEVAQKNNALKQLRE 1150
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQEIHIRDAhevatSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1151 LQAQLAELQEDLESEKAARNKAEklkRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQ 1230
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1231 EMRQrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1310
Cdd:TIGR00618 474 QLQT-----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1311 GELADRTHKIQTELDNVSCLLEDAEKKGIK---LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQ 1387
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1388 EEEEESRkNLEKQLATLQAQLVETKKKLEDdvgaleglEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1467
Cdd:TIGR00618 629 DVRLHLQ-QCSQELALKLTALHALQLTLTQ--------ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1468 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAE 1547
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1548 MEDLISskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLqardeqneEKKR 1627
Cdd:TIGR00618 780 LSHLAA----------EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKS 841
|
730 740 750
....*....|....*....|....*....|....*...
gi 688558686 1628 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVE 1665
Cdd:TIGR00618 842 ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1412-1775 |
3.10e-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: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1412 KKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqivsnlekkqkkfdqm 1491
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----------------------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1492 laeektisaRYAEERDRAEaearekDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1571
Cdd:TIGR02169 212 ---------RYQALLKEKR------EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1572 LEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1643
Cdd:TIGR02169 277 LNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1644 RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN-------EKK 1716
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlNAA 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1717 LKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQ 1775
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1098-1757 |
5.91e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1098 ETTDLQDQIAELQAQIDELkiqlakkeEELQAVLargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK-----A 1172
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1173 EKLKRDLSEELEALKTELEDTldttaaqqelrskrEQEVAELKKAIdDETRNHESQIQEMRQRHGTaleeisEQLEQAKR 1252
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARL-DALREELDELEAQIRGNGG------DRLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1253 vkgnleknkqtlesdnkeltnEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvkgELADRTHKIQTELDNVSCLLE 1332
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1333 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlleqqeeeeesRKNLEKQLATLQAQ----- 1407
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-----------------RDALAEALGLDEAElpfvg 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1408 -LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNRLQqelddlmVDLDHqrqivsnLEKKQK 1486
Cdd:COG4913 465 eLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLRGR-------LVYER-------VRTGLP 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1487 KFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFERLNKQLRAemEDLISSKDDVG-KNVHE 1564
Cdd:COG4913 525 DPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELRRHPRAITR--AGQVKGNGTRHeKDDRR 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1565 LEKSKRTL----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQNEEKKRalVKQVREMEAEL 1640
Cdd:COG4913 597 RIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDEID--VASAEREIAEL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1641 EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftQSKENEKKLKSL 1720
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALL 751
|
650 660 670
....*....|....*....|....*....|....*..
gi 688558686 1721 EAEILQLQEDlASSERARRHAEQERDELADEISNSAS 1757
Cdd:COG4913 752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEE 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1240-1894 |
1.23e-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: 73.13 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1240 LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA---RFSEGEKVKGELadr 1316
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlsKINSEIKNDKEQ--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1317 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1396
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1397 LEKQLATLQAqLVETKKKLEDDvgaLEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDlmvdldhQRQ 1476
Cdd:TIGR04523 199 LELLLSNLKK-KIQKNKSLESQ---ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1477 IVSNLEKKQKKFDQmlAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRaEMEDLISSKD 1556
Cdd:TIGR04523 265 IKKQLSEKQKELEQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1557 DVgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREM 1636
Cdd:TIGR04523 342 EQ---ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1637 EAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKK 1716
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1717 LKSLEAEILQLqedlasserarrhaEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEeleeeqsnmELLNDRFRK 1796
Cdd:TIGR04523 498 LKKLNEEKKEL--------------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---------ELNKDDFEL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1797 TTmqvDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAAN 1876
Cdd:TIGR04523 555 KK---ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
650
....*....|....*...
gi 688558686 1877 KIVRRTEKKLKEVFMQVE 1894
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVK 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1397-1944 |
2.00e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1397 LEKQLATLQaQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIafDKLEKTKNRLQQELDDLMVDLDHQRQ 1476
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1477 IVSNLEKkqkkfdQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLI 1552
Cdd:COG4913 324 ELDELEA------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1553 SSKDDVGKNVHELEKSKRTLEQQveemrtqLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQneekkralVK- 1631
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE--------LPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1632 -----QVREMEAE-----------------LEDERKQRALAVAAKKKLEMDL-------KDVEAQIEAA----------- 1671
Cdd:COG4913 463 vgeliEVRPEEERwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRLvyervrtGLPDPERPRLdpdslagkldf 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1672 --NKARDEAIKQLRKL--------QAQMKDYQREL---------EEARTSRDEIFTQSK-----ENEKKLKSLEAEILQL 1727
Cdd:COG4913 543 kpHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAItragqvkgnGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1728 QEDLASSERARRHAEQERDELAD---------EISNSASGKAALLDEKRRLEARIAQleeeleeeqsnMELLNDRFRKTT 1798
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELER-----------LDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1799 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKI 1878
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-----------DRLEAAEDLARLELRALLEERFAAALG 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1879 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKAnsrMKQLKRQLEEAEEEATRANASRRKLQRELDD 1944
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1049-1775 |
2.18e-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: 73.06 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1049 QLAEEEEK----AKNLGKVKNKQEMMMVDLE---ERL----------KKEEKTRQELEKAKRKLDAET---TDLQDQIAE 1108
Cdd:COG3096 300 QLAEEQYRlvemARELEELSARESDLEQDYQaasDHLnlvqtalrqqEKIERYQEDLEELTERLEEQEevvEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1109 LQAQ-------IDELKIQLAKKEEEL-----------QAVLARGDEEVAQKNNAL--KQLRELQAQL-AELQEDLESEKA 1167
Cdd:COG3096 380 AEARleaaeeeVDSLKSQLADYQQALdvqqtraiqyqQAVQALEKARALCGLPDLtpENAEDYLAAFrAKEQQATEEVLE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1168 ARNK---AEKLKRDLSEELEALK-----TELEDTLDTtaAQQELRSKREQE-----VAELKKAIDDETRNHESQIQEMRQ 1234
Cdd:COG3096 460 LEQKlsvADAARRQFEKAYELVCkiageVERSQAWQT--ARELLRRYRSQQalaqrLQQLRAQLAELEQRLRQQQNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1235 rhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfsegEKVKGELA 1314
Cdd:COG3096 538 -----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR----APAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1315 DRTHKIQTEldnVSCLLEDAekkgikltkdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR 1394
Cdd:COG3096 609 DALERLREQ---SGEALADS-----------QEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRL 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1395 KNLEKQL-ATLQAQLVEtKKKLEDD--VGALEG----------LEEVKRKLQkDMEVTSQKL---EEKAIAFDKlektKN 1458
Cdd:COG3096 675 LALAERLgGVLLSEIYD-DVTLEDApyFSALYGparhaivvpdLSAVKEQLA-GLEDCPEDLyliEGDPDSFDD----SV 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1459 RLQQELDDLMVDLDHQRQI-VSNLEK--------KQKKFDQMLAEEKTISARYAEER------DRAEAEAREKDTKALSM 1523
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASfdvqklQRLHQAFSQFVGGHLAV 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1524 ARALDEALEAKE------EFERLNKQLRAEMEDLISSKDDVGKNVHELEK--------SKRTLEQQVEEMRTQLEELED- 1588
Cdd:COG3096 829 AFAPDPEAELAAlrqrrsELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREELDAAQEa 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1589 --ELQATEDAKLRLEVNMQAMK---AQFDRdLQARDEQNEEKKRALVKQVREMEaeledERKQRALAVAAKKKLEM---- 1659
Cdd:COG3096 909 qaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVVQRRPHFSYEDAVGLlgen 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1660 -DLKD-VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEaeilqLQEDLASSERA 1737
Cdd:COG3096 983 sDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG-----VQADAEAEERA 1057
|
810 820 830
....*....|....*....|....*....|....*...
gi 688558686 1738 RrhaeQERDELADEISNSASGKAALLDEKRRLEARIAQ 1775
Cdd:COG3096 1058 R----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1104-1751 |
2.77e-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: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1104 DQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS--- 1180
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlr 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1181 ---EELEALKTELEDT-------------LDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1244
Cdd:TIGR00618 267 ariEELRAQEAVLEETqerinrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1245 EQLEQAKRVKGNLEKNKQTLESDNKE----LTNEVKSLQQAKSESEHKRK-------KLEAQLQEVMARFSEGEKVKGEL 1313
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCqqhtLTQHIHTLQQQKTTLTQKLQslckeldILQREQATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1314 ADRTHKIQTELD----------NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1383
Cdd:TIGR00618 427 AHAKKQQELQQRyaelcaaaitCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1384 LEQQEEEEESRKNLEKQLAT--LQAQLVETKKKLEDDVGALEGLEEVKRK----LQKDMEVTSQKLEEKAIAFDKLEKTK 1457
Cdd:TIGR00618 507 CGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKqrasLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1458 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlsmARALDEALEAKEEF 1537
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH---ALQLTLTQERVREH 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1538 ERLNKQLRAEMEDLISSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELEdelqatEDAKLRLEVNMQAMKAQfdRDLQ 1616
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIE------EYDREFNEIENASSSLG--SDLA 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1617 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL 1696
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1697 EEARTSRDEIFTQSKENEK----KLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1751
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1396-1964 |
1.02e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1396 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLmvdlDHQR 1475
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1476 QIVSNLEKKQKKFDQmlaEEKTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKqlraEMEDLISSK 1555
Cdd:PRK03918 238 EEIEELEKELESLEG---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1556 DDVGKNVHELEKSKRTLEQQV---EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFDRDLQARDEQNEEKKRALVKQ 1632
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1633 VREMEAELEDERKqralavaAKKKLEMDLKDVEAQI---EAANKARDEAIKQLRKLQAQMKDYQRELEEARtsRDEIFtq 1709
Cdd:PRK03918 386 PEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGRELTEEH--RKELL-- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1710 sKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsgkaaLLDEKRRLEARIAQLEEELEEEQSN-ME 1788
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEeYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1789 LLNDRFRKTTMQVDTLNTELagerSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLeqe 1868
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY--- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1869 aKERAAANKIVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEAT-----RANASRRKLQRELD 1943
Cdd:PRK03918 602 -NEYLELKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELA 676
|
570 580
....*....|....*....|.
gi 688558686 1944 DATEASEGLSREVNTLKNRLR 1964
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLE 697
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1010-1803 |
1.46e-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: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1010 TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM------MVDLEERLKKEEK 1083
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1084 TRQELEKAKRKLDAETTDLQDQIAElqaQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLaELQEDLE 1163
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDE---QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL-LVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1164 SEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQevaeLKKAIDDETRNHESQIQEMRQRHGTALEEI 1243
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL----VIERQEDEAKTAAQLCADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1244 SEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEhKRKKLEAQLQEVMARFSegekvkgeLADRTHKIQTE 1323
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAERELS--------KAEKNSLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1324 LDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQL 1401
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmlTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1402 ATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDME-VTSQKLEEKAIAFDKLekTKNRLQQELDDLMVDLDHQRQIVSN 1480
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVC--GSQDEESDLERLKEEIEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1481 LEKKQKKFDQMLAEEKTISARYAEERDR---AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK-- 1555
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRqs 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1556 --DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQaTEDAKLRLEVNMQAMKAQFDRdLQARDEQNEekkralvKQV 1633
Cdd:TIGR00606 738 iiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1634 REMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIKQLRKLQA---QMKDYQRELEEARTSRDEIFT 1708
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQheLDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1709 QSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADeiSNSASGKAALL------------------------- 1763
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS--SKETSNKKAQDkvndikekvknihgymkdienkiqd 966
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 688558686 1764 ---DEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1803
Cdd:TIGR00606 967 gkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1045-1773 |
1.48e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.99 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1045 EMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL--QDQIAELQAQIDELKIQLak 1122
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERL-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1123 keEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESE----------KAARNKAEKLKRD-------LSE 1181
Cdd:PRK04863 365 --EEQNEVVEEADEQQeeneARAEAAEEEVDELKSQLADYQQALDVQqtraiqyqqaVQALERAKQLCGLpdltadnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1182 ELEALKTELED-TLDTTAAQQELRS-----KREQEVAELKKAIDDET-------------------RNHESQIQEMRQRH 1236
Cdd:PRK04863 443 WLEEFQAKEQEaTEELLSLEQKLSVaqaahSQFEQAYQLVRKIAGEVsrseawdvarellrrlreqRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1237 GTALEEISEQ------LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvk 1310
Cdd:PRK04863 523 SELEQRLRQQqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1311 geLADRTHKIQTELDNVSclledaEKKGIKLTkDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNnlleqqeee 1390
Cdd:PRK04863 601 --RAPAWLAAQDALARLR------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE--------- 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1391 eesrknlekQLATLQAQLVETKKKLEDDVGAL---EGLEEVkrKLQkDMEVTSQKLEE--KAIAFDKLEKTKNRLQQE-- 1463
Cdd:PRK04863 663 ---------RLSQPGGSEDPRLNALAERFGGVllsEIYDDV--SLE-DAPYFSALYGParHAIVVPDLSDAAEQLAGLed 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1464 -LDDLMV---DLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErDRAEAEAREKDTKALSMARALDEALEAKEEF-- 1537
Cdd:PRK04863 731 cPEDLYLiegDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEV-PLFGRAAREKRIEQLRAEREELAERYATLSFdv 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1538 ---ERLNKQLR----------------AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL--------------- 1583
Cdd:PRK04863 810 qklQRLHQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnllad 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1584 -------EELEDELQATEDAKL-------------RLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMeaeleDE 1643
Cdd:PRK04863 890 etladrvEEIREQLDEAEEAKRfvqqhgnalaqlePIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TE 963
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1644 RKQRALAVAAKKKLEMDLKDVE------AQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1717
Cdd:PRK04863 964 VVQRRAHFSYEDAAEMLAKNSDlneklrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1718 KSleaeiLQLQEDLASSERARRHaeqeRDELADEISNSASGKAALLDEKRRLEARI 1773
Cdd:PRK04863 1044 QD-----LGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1192 |
1.62e-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: 70.09 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 841 FAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPL-LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQ 919
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 920 LLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeea 999
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-------- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1000 arqklqlekvtaeAKIKKMEEDILLLEDQnskflkekklledrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1079
Cdd:TIGR02168 845 -------------EQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1080 KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQK-NNALKQLRELQAQLAEL 1158
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRL 977
|
330 340 350
....*....|....*....|....*....|....
gi 688558686 1159 QEDLESEKAARNKAEKLKRDLSEELEALKTELED 1192
Cdd:TIGR02168 978 ENKIKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1075-1968 |
2.22e-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: 69.60 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1075 EERLKKEEKT---RQELEKAKRKLDAEttdlQDQIAELQAQIDELKIQLAKKEEELQAvlarGDEEVAQKNNALKQLREL 1151
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQA----ASDHLNLVQTALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1152 ---QAQLAELQEDLESEKAARnkaeklkrdlsEELEALKTELEDTLdtTAAQQELRSKREQeVAELKKAID-DETRNheS 1227
Cdd:COG3096 350 eryQEDLEELTERLEEQEEVV-----------EEAAEQLAEAEARL--EAAEEEVDSLKSQ-LADYQQALDvQQTRA--I 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1228 QIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegE 1307
Cdd:COG3096 414 QYQQAVQ----ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV-------C 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1308 KVKGELaDRthkiqteldnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEknnLLE 1385
Cdd:COG3096 483 KIAGEV-ER---------------SQAWQTARELLRRYRSQQALAQRLQQLRAQlaELEQRLRQQQNAERLLEE---FCQ 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1386 QQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVgalEGLEEVKRKLQkDMEVTSQKLEEKA----IAFDKLEKTKNRLQ 1461
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAV---EQRSELRQQLE-QLRARIKELAARApawlAAQDALERLREQSG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1462 QELDDLmVDLDHQRQIVSNLEKKQKKFDQMLAEEKtisARYAEERDRAEAEAREKDTKALSMARAL----------DEAL 1531
Cdd:COG3096 620 EALADS-QEVTAAMQQLLEREREATVERDELAARK---QALESQIERLSQPGGAEDPRLLALAERLggvllseiydDVTL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1532 EAKEEFERLNKQLR---------------AEMED------LIS----SKDDVGKNVHELEK------SKRTL-------- 1572
Cdd:COG3096 696 EDAPYFSALYGPARhaivvpdlsavkeqlAGLEDcpedlyLIEgdpdSFDDSVFDAEELEDavvvklSDRQWrysrfpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1573 --------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDL-----QARDEQNEEKKRALVKQVREMEA 1638
Cdd:COG3096 776 plfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1639 ELED----ERKQRALAVAAKKKLEMdlkdVEAQIEAANKARDEAikqlrkLQAQMKDYQRELEEARTSRDEIFTQSK--- 1711
Cdd:COG3096 851 ELAQhraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIQQHGKala 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1712 ENEKKLKSLEAEILQ---LQEDLASSERARRHAEQERDELADEISNSA----SGKAALLDEKRRLEARIAQLEEELEEEQ 1784
Cdd:COG3096 921 QLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1785 SNmelLNDRFRKTTMQVDTLNTELAGERSAAQkseNARQQLerqnKDLKSKLQELEGSVKSkfkasiaaleakilqleeq 1864
Cdd:COG3096 1001 RE---AREQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQADA------------------- 1051
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1865 leqEAKERAAANKivrrtekklkevfmqvederrhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDD 1944
Cdd:COG3096 1052 ---EAEERARIRR-----------------------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQ 1105
|
970 980 990
....*....|....*....|....*....|....
gi 688558686 1945 ATEASEG----------LSREvNTLKNRLRRGGP 1968
Cdd:COG3096 1106 EREQVVQakagwcavlrLARD-NDVERRLHRREL 1138
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1072-1856 |
2.70e-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: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1072 VDLEERLKKEEKTRQELEKAKR-KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARgdeevaqknnalkqlre 1150
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQ----------------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1151 lqaQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhesqIQ 1230
Cdd:pfam12128 331 ---HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAK----IR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1231 EMRQRHGTALEEISEQLEQAKRvkgnleknkQTLESDNKELTNEVKSLQQAKSEsehkrkkleAQLQEVMARFSEGEKVK 1310
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELR---------EQLEAGKLEFNEEEYRLKSRLGE---------LKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1311 GELAD-RTHKIQTELdnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqee 1389
Cdd:pfam12128 466 LENFDeRIERAREEQ-------EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ---------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1390 eeesrknLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLektknRLQQelddlmv 1469
Cdd:pfam12128 529 -------LFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL-----DLKR------- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1470 dLDHQRQIVSNlekkqkkfDQMLAEEKTISARYAEERDRAEAEarekdTKALSMARALDEALEAKEEFERlnkqlraemE 1549
Cdd:pfam12128 590 -IDVPEWAASE--------EELRERLDKAEEALQSAREKQAAA-----EEQLVQANGELEKASREETFAR---------T 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1550 DLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEledELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAL 1629
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE---RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1630 VKQVREMEAELEDERKQRALAVAAKkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIfTQ 1709
Cdd:pfam12128 724 EGALDAQLALLKAAIAARRSGAKAE------LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV-LR 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1710 SKENEKKLKSLEAEILQLQedlasSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1789
Cdd:pfam12128 797 YFDWYQETWLQRRPRLATQ-----LSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSK 871
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1790 LNdrfrktTMQVDTLNTELAGERSaaqksenarqQLERQNKDLKSKLQELEGSVKSK---FKASIAALEA 1856
Cdd:pfam12128 872 LA------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 |
3.44e-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: 59.75 E-value: 3.44e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 688558686 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, ... |
1034-1252 |
3.90e-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: 67.10 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1034 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1113
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1114 DELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLeseKAARNKAEKLKRDLSEELEALKTELEDT 1193
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL---RADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1194 LDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKR 1252
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1073-1314 |
7.86e-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: 66.33 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1073 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvlargdeevaqknnALKQLRELQ 1152
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------------LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1153 AQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhESQIQEM 1232
Cdd:COG4942 97 AELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1233 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG--EKVK 1310
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgfAALK 252
|
....
gi 688558686 1311 GELA 1314
Cdd:COG4942 253 GKLP 256
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1076-1747 |
8.00e-11 |
|
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: 67.44 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1076 ERLKK-EEKTRQELEKAKRKLDAETTDLQDQ---IAELQAQIDELKIQLakkEEELQAvlargDEEVAQKNNALKQ---- 1147
Cdd:pfam05483 88 EKIKKwKVSIEAELKQKENKLQENRKIIEAQrkaIQELQFENEKVSLKL---EEEIQE-----NKDLIKENNATRHlcnl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1148 LRELQAQLAELQEDLESEkaaRNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKREQE---VAELKKAIDDETR 1223
Cdd:pfam05483 160 LKETCARSAEKTKKYEYE---REETRQVYMDLNNNIEKMILAFEElRVQAENARLEMHFKLKEDhekIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1224 NHESQI---------QEMRQRHGT-ALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE 1293
Cdd:pfam05483 237 DKEKQVsllliqiteKENKMKDLTfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1294 AQLQ---EVMARFSEGEKVKGELADRTHK----IQTELDNVSCLLED---AEKKGIKLTKD-VSSLESQLQDTQELLQEE 1362
Cdd:pfam05483 317 EDLQiatKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEEllrTEQQRLEKNEDqLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1363 TRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQ------LVETKKK----LEDDVGALEGLEEVKRKL 1432
Cdd:pfam05483 397 TKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKeqelifLLQAREKeihdLEIQLTAIKTSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1433 QKDMEVTSQKLEEKAIAF----DKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKfdqMLAEEKTISARYAEERDR 1508
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1509 AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1588
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1589 ELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQI 1668
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM 709
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1669 EAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRdeiftqskenEKKLKSLEAEILQLQEDLASSERARRHAEQERDE 1747
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1103-1324 |
8.07e-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: 66.33 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1103 QDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1182
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1183 LEALKTELEDTLDTTAAQ--QELRSKREQEVAELKKAID-DETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEK 1259
Cdd:COG4942 92 IAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1260 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1324
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
935-1666 |
8.79e-11 |
|
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: 67.44 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 935 TELFAEAEEMR-------ARLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQshiqdleeqldeeeaarqkLQLE 1007
Cdd:pfam05483 81 SKLYKEAEKIKkwkvsieAELKQKENKLQENRKIIEAQRKAI----QELQFENEKVS-------------------LKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1008 KVTAEAKikkmeeDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNL-GKVKNKQEMMMVDLEERLKKEEKTRQ 1086
Cdd:pfam05483 138 EEIQENK------DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVyMDLNNNIEKMILAFEELRVQAENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1087 E----LEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQAQlaELQEDL 1162
Cdd:pfam05483 212 EmhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD-LTFLLEESRDKANQLEEKTKLQDE--NLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1163 ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAiddetRNHESQIQEMRQRHGTALEE 1242
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1243 ISEQLEQakrvkgNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQT 1322
Cdd:pfam05483 364 LLRTEQQ------RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1323 ELDNVSCLLEDAEKK----GIKLTKDVSSLESQLQDTQELLQEETRQKLnlssRIRQLEEEKNNLLEQQEEEEESRKNLE 1398
Cdd:pfam05483 437 KEQELIFLLQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKL----KNIELTAHCDKLLLENKELTQEASDMT 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1399 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTS----QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQ 1474
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVReefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1475 RQIVSNLEK----KQKKFDQMLAEEKTIsaryaeeRDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1550
Cdd:pfam05483 593 ENKCNNLKKqienKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1551 LISSKDDVgknVHELEKSKRTLEQQVeemrtqleELEDELQATEDAKLRLEVN-MQAMKAQFDRDLQARDEQ-----NEE 1624
Cdd:pfam05483 666 KKISEEKL---LEEVEKAKAIADEAV--------KLQKEIDKRCQHKIAEMVAlMEKHKHQYDKIIEERDSElglykNKE 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 688558686 1625 KKRALVKQVREME-----AELEDERKQRALAVAAKKKLEMDLKDVEA 1666
Cdd:pfam05483 735 QEQSSAKAALEIElsnikAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
888-1305 |
9.40e-11 |
|
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: 67.05 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 888 EMQAKDEELikvKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLESRVE 967
Cdd:pfam05483 385 ELQKKSSEL---EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 968 EEEERNQSLQNEKKKMqshiqdleeqldeeeaarqKLQLEKvtaeAKIKKMEedillLEDQNSKFLKEKKLLEDRVGEMT 1047
Cdd:pfam05483 461 AIKTSEEHYLKEVEDL-------------------KTELEK----EKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1048 SQLAEEEEKAKNlgkVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL 1127
Cdd:pfam05483 513 LELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1128 QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1207
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1208 EQ--------------EVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKN----KQTLESDNK 1269
Cdd:pfam05483 670 EEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEqssaKAALEIELS 749
|
410 420 430
....*....|....*....|....*....|....*.
gi 688558686 1270 ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1305
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
954-1308 |
1.02e-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: 66.97 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 954 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1033
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1034 KEKKLLEDRVgemtsqlaeeeekaKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1113
Cdd:TIGR04523 419 QEKELLEKEI--------------ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1114 DELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRDLSEELEALKTELedt 1193
Cdd:TIGR04523 485 EQKQKELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLESEK---KEKESKISDLEDELNKDDFEL--- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1194 ldTTAAQQELRSKREQEVAELKKAIDDETRNHEsQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTN 1273
Cdd:TIGR04523 555 --KKENLEKEIDEKNKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
330 340 350
....*....|....*....|....*....|....*
gi 688558686 1274 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEK 1308
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
804-1326 |
1.18e-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: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 804 FFRTGVLahleEERDL--KITDIIIYFQSVCRgylARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWW 870
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 871 RLFTKVKpLLQ--VTRQEEEMQAKDEELIKVKERQVKVENELVEMerkHQQLLEEKNILAEQLQAETElfaEAEEMRARL 948
Cdd:COG4913 285 FAQRRLE-LLEaeLEELRAELARLEAELERLEARLDALREELDEL---EAQIRGNGGDRLEQLEREIE---RLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 949 VAKKQELEEILHDLESRVEEEEernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1028
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1029 NS----KFLKEKKLLEDRVGEMTS---------QLAEEEEK-------------------AKNLGKV-----KNKQEMMM 1071
Cdd:COG4913 435 KSnipaRLLALRDALAEALGLDEAelpfvgeliEVRPEEERwrgaiervlggfaltllvpPEHYAAAlrwvnRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1072 VDLEERLKKEEKTRQELEKAK--RKLDAETTDLQDQI-AELQAQIDELKIQlakKEEELQ--------AVLARGDEEVAQ 1140
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitrAGQVKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1141 KN-------------NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELE---DTLDTTAAQQELR 1204
Cdd:COG4913 592 KDdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1205 SKrEQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA--- 1281
Cdd:COG4913 672 EL-EAELERLDASSDD--------LAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRlea 738
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 688558686 1282 --KSESEHKRKKLEAQLQEVMARFSEGEKVKgELADRTHKIQTELDN 1326
Cdd:COG4913 739 aeDLARLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNR 784
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
879-1467 |
1.20e-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: 67.17 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 879 LLQVTRQEE--EMQAKDEELIKVKERQVK-----VENELVEMERKHQQLLEEKNILAEQ----LQAETELFAEAEEMRAR 947
Cdd:pfam12128 272 TLIASRQEErqETSAELNQLLRTLDDQWKekrdeLNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 948 LVAKKQELEEILHDLESRVEEEEERNQSLqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDI-LLLE 1026
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1027 DQNSKFLKEKKLLEDRVGEMTSQLAE---EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1103
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1104 D---QIAELQAQIDELKIQLAKK---------------EEELQAVLARG------------DEEVAQKNNA------LKQ 1147
Cdd:pfam12128 510 QasrRLEERQSALDELELQLFPQagtllhflrkeapdwEQSIGKVISPEllhrtdldpevwDGSVGGELNLygvkldLKR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1148 L---------RELQAQLAELQEDLESEKA-----------ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1207
Cdd:pfam12128 590 IdvpewaaseEELRERLDKAEEALQSAREkqaaaeeqlvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1208 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKgnlEKNKQTLESDnkeLTNEVKSLQQAKSESEH 1287
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK---QAYWQVVEGA---LDAQLALLKAAIAARRS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1288 KRKKLEAQLQEVMARFSEGEKVKGelaDRTHKIQTELDNVSCLLEDAEKKGikltKDVSSLESQLQDTqeLLQEETRQKL 1367
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDP---DVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLAT 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1368 NLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVK-----RKLQKDMEVTSQK 1442
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERLAQ 894
|
650 660
....*....|....*....|....*
gi 688558686 1443 LEEkaiAFDKLEKTKNRLQQELDDL 1467
Cdd:pfam12128 895 LED---LKLKRDYLSESVKKYVEHF 916
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1569-1775 |
2.12e-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: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1569 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFDR--DLQARDEQNEEKKRALVKQVREMEAELEDERKQ 1646
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1647 RALAvaAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ-AQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1725
Cdd:COG4913 299 ELRA--ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1726 QLQEDLAS-SERARRHAE---QERDELADEISNSASGKAALLDEKRRLEARIAQ 1775
Cdd:COG4913 377 ASAEEFAAlRAEAAALLEaleEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1526-1760 |
2.14e-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: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1526 ALDEALEAKEEFERLNKQL---RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1602
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1603 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQL 1682
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1683 RKLQAQMKDYQRELEEARTSRDEIFTQSkenEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1760
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1054-1454 |
2.36e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1054 EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQA--VL 1131
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1132 ARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEV 1211
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1212 AELKKAIDDETRNHESQIQEMRQRHgtALEEISEQLEQAKR-------------------------------VKGNLEKN 1260
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLllliaaallallglggsllsliltiagvlflVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1261 KQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIK 1340
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1341 LTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEE--EKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1416
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558686 1417 DDVGALEGLEEVKRKLQKDMEVtSQKLEEKAIAFDKLE 1454
Cdd:COG4717 450 ELREELAELEAELEQLEEDGEL-AELLQELEELKAELR 486
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1275-1745 |
3.87e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1275 VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ- 1353
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1354 -DTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEddvgalEGLEEVKRKL 1432
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEER-----------LEELRELEEELEELEAELAELQEELE------ELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1433 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH--QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1510
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1511 AEAREKDTKALSMA----------RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR 1580
Cdd:COG4717 271 LILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1581 TQLEELEDELQ--ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVREMEAELEDERK--QRALAVAAKKK 1656
Cdd:COG4717 351 ELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGelEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1657 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY--QRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLASS 1734
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL-------KAELRELAEEWAALKLALELL 502
|
490
....*....|.
gi 688558686 1735 ERARRHAEQER 1745
Cdd:COG4717 503 EEAREEYREER 513
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1001-1772 |
4.49e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1001 RQKLQLEKVTAEAKIKKMEEDILLLEDQnskfLKEKKLLedrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKk 1080
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEER----LEEQNEV---VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1081 EEKTR--------QELEKAKRKLDA---ETTDLQDQIAELQAQIDEL---------KIQLAKK-----EEELQAVLARGD 1135
Cdd:PRK04863 408 VQQTRaiqyqqavQALERAKQLCGLpdlTADNAEDWLEEFQAKEQEAteellsleqKLSVAQAahsqfEQAYQLVRKIAG 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1136 E---EVAQKN--NALKQLRE----------LQAQLAELQEDLESEKAAR------NKAEKLKRDLSEELEALKTELEDTL 1194
Cdd:PRK04863 488 EvsrSEAWDVarELLRRLREqrhlaeqlqqLRMRLSELEQRLRQQQRAErllaefCKRLGKNLDDEDELEQLQEELEARL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1195 DTTAAQQElrskreqEVAELKKAIDDETRNHESQIQEMRQRhGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNE 1274
Cdd:PRK04863 568 ESLSESVS-------EARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1275 VKSLQQAKSESEHKRKKLEAQLQEVMAR-FSEGEKVKGeLADRTHKIQ-TEL-DNVSclLEDA----------------- 1334
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNA-LAERFGGVLlSEIyDDVS--LEDApyfsalygparhaivvp 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1335 EKKGIK---------------LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlleqqeeeeeSRKNLEK 1399
Cdd:PRK04863 717 DLSDAAeqlagledcpedlylIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLF----------GRAAREK 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1400 QLATLQAQ---LVETKKKLEDDVgalegleevkRKLQKDMEVTSQKL-EEKAIAFD-----KLEKTKNRLQQ---ELDDL 1467
Cdd:PRK04863 787 RIEQLRAEreeLAERYATLSFDV----------QKLQRLHQAFSRFIgSHLAVAFEadpeaELRQLNRRRVElerALADH 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1468 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTIsaryAEER--DRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1545
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNLL----ADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1546 AEMEDLisskDDVGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFDRDLQARDEQNEEK 1625
Cdd:PRK04863 932 SDPEQF----EQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQE 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1626 KRALVKQVREMEAELEDerkqralavaaKKKLEMDLKdveAQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARTSRD 1704
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQ-----------YNQVLASLK---SSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRD 1063
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1705 EIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL------DEKRRLEAR 1772
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1016-1524 |
4.59e-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: 64.84 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1016 KKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEE--EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELE 1089
Cdd:pfam10174 137 KTLEEMELRIETQkqtlGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELH 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1090 KAKRKLD--AETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQlaelqedlesEKA 1167
Cdd:pfam10174 217 RRNQLQPdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSH----------SKF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1168 ARNKAEKLKRDLSE---ELEALKTELE-------------DTLDTTAAQQELRSKREQ-EVAELKKAIDDETR---NHES 1227
Cdd:pfam10174 287 MKNKIDQLKQELSKkesELLALQTKLEtltnqnsdckqhiEVLKESLTAKEQRAAILQtEVDALRLRLEEKESflnKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1228 QIQEMRQRHGTALEEIS------------------------EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKS 1283
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlqkkienlqEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1284 ESE-------HKRKKLEAQLQEVMARFSEGEKV--------KGELADRTHKIQTELDNVSCLLEDAEKKGIKL------- 1341
Cdd:pfam10174 447 EKEriierlkEQREREDRERLEELESLKKENKDlkekvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLksleiav 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1342 ---TKDVSSLESQLQDTQElLQEETRQKLNLSSRIRQLEEEknnLLEQQEEEEESRKNLEKQLATLQAqlVETKKKLEDD 1418
Cdd:pfam10174 527 eqkKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE---VARYKEESGKAQAEVERLLGILRE--VENEKNDKDK 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1419 -VGALEGLEEVKRKLQ--KDMEVTSQKLEEKAIAFDKLEK--------TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1487
Cdd:pfam10174 601 kIAELESLTLRQMKEQnkKVANIKHGQQEMKKKGAQLLEEarrrednlADNSQQLQLEELMGALEKTRQELDATKARLSS 680
|
570 580 590
....*....|....*....|....*....|....*..
gi 688558686 1488 FDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1524
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1648-1882 |
5.42e-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: 63.63 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1648 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1727
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1728 QEDLasserarrhaEQERDELADEIS----NSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLnDRFRKTTMQVDT 1803
Cdd:COG4942 96 RAEL----------EAQKEELAELLRalyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1804 LNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1882
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1393-1656 |
8.14e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1393 SRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1472
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1473 HQRQivsNLEKKQKKFDQMLAEektisaryaeerdrAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLI 1552
Cdd:COG4942 94 ELRA---ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1553 SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQARDEQNEEKKRALVKQ 1632
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 688558686 1633 VREMEAELEDERKQRALAVAAKKK 1656
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1319-1963 |
9.24e-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: 63.89 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1319 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1398
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1399 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1478
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1479 SNLEKKQKKFDQMLAEektisaryaeerdraeAEAREKDTKALSmaralDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1558
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQ----------------ISELKKQNNQLK-----DNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1559 GKNVHELEKSkrtlEQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA 1638
Cdd:TIGR04523 263 NKIKKQLSEK----QKELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1639 ELEDERKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLK 1718
Cdd:TIGR04523 336 IISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1719 SLEAEILQLQEDLASSERARRHAEQERDELADEISNsasgkaaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1798
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-------LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1799 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKsKFKASIAALEAKILQleeqleqeaKERAAANKI 1878
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISD---------LEDELNKDD 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1879 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNT 1958
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
....*
gi 688558686 1959 LKNRL 1963
Cdd:TIGR04523 632 IIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1509-1734 |
1.56e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1509 AEAEAREKDTKALSMARA-LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1587
Cdd:COG4942 17 AQADAAAEAEAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1588 DELQATEDAKLRLEVNMQAMK--------------AQFDRDLQARDEQNeekkRALVKQVREMEAELEDERKQRALAVAA 1653
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLA----PARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1654 KKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLAS 1733
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPA 245
|
.
gi 688558686 1734 S 1734
Cdd:COG4942 246 A 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1520-1761 |
1.65e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1520 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1599
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1600 LEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAI 1679
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1680 KQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGK 1759
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 688558686 1760 AA 1761
Cdd:COG4942 244 PA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
880-1254 |
1.94e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 880 LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL---- 955
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 956 EEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKE 1035
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1036 KK------------LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1103
Cdd:COG4717 271 LIltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1104 DQIAELQAQIDELKIQLAKKEEE--LQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKlkrdlSE 1181
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----AL 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1182 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHEsqIQEMRQRHGTALEEISEQLEQAKRVK 1254
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALK 496
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1102-1846 |
1.97e-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: 62.82 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1102 LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLREL-QAQLAELQE-DLESEKAARNKAEKLK--R 1177
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEEIQenK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1178 DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqemrqrhgTALEEISEQLEQAK-----R 1252
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlemhfK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1253 VKGNLEKNKQTLESDNKELTN---EVKSLQQAKSESEHKRKKLEAQLQEVMARFSE-GEKVK------GELADRTHKIQT 1322
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDkekQVSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKlqdenlKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1323 ELDNVSCLLEDAEKKGIKLTKDV---SSLESQLQDTQELLQEET-RQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1398
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLqiaTKTICQLTEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1399 KQLATLQAQLVETKKKLEDdVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqiv 1478
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLL---------- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1479 SNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLISS 1554
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1555 KddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDEL-QATEDAKLRLEVNMQAMKAQFDRDLQARDEQN--EEKKRALVK 1631
Cdd:pfam05483 526 K----KQEERMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1632 QVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFtqsk 1711
Cdd:pfam05483 602 QIENKNKNIEELHQENK---ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL---- 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1712 ENEKKLKSLEAEILQLQEdlasserarrhaeqerdELADEISNSASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLN 1791
Cdd:pfam05483 675 EEVEKAKAIADEAVKLQK-----------------EIDKRCQHKIAEMVALMEKHKHQYDKIIEER------DSELGLYK 731
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1792 DRFRKTTMQVDTLNTELAGERsAAQKSENARQQLERQNKD-LKSKLQELEGSVKSK 1846
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIK-AELLSLKKQLEIEKEEKEkLKMEAKENTAILKDK 786
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1108-1941 |
2.25e-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: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1108 ELQAQIDEL--KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1185
Cdd:TIGR00606 170 ALKQKFDEIfsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1186 LKT---ELEDTL-------DTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKG 1255
Cdd:TIGR00606 250 LKNrlkEIEHNLskimkldNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1256 NLEKNKQTLESDNKELTNEVKSLQ-QAKSESEHKRKKlEAQLQEVMARFSEGEKVKGELADRthkiqtELDNVSCL-LED 1333
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLATRLELDGFERGPFSER------QIKNFHTLvIER 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1334 AEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrknLEKQlatlQAQLVETKK 1413
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI----------------LEKK----QEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1414 KLEDDVGALEGLEEVKRKLQKDMEVTSqKLEEKAIAFDKLEKTKNRLQQELDdlmvdldhqrqivsnLEKKQKKFDQMLA 1493
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNEKAD---------------LDRKLRKLDQEME 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1494 EEKtisaRYAEERDRAEAEAREKDTKalsmaraldealeakeeFERLNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLE 1573
Cdd:TIGR00606 526 QLN----HHTTTRTQMEMLTKDKMDK-----------------DEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHSKS 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1574 QQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQneekkralvkqvremEAELEDerkqRALAVAA 1653
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ---------------LSSYED----KLFDVCG 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1654 KKKLEMDLKDVEAQIEAANKardeaikQLRKLQAQMKDYQRELEEARTSR-------DEIFTQSKENEKKLKSLEAEILQ 1726
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRL 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1727 LQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMElLNDRFRKTTMQVDTLNT 1806
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAK 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1807 ELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVK----SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1882
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1883 EKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRE 1941
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
929-1317 |
2.61e-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: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 929 EQLQAETELFAEAEEMRA-------RLVAKKQELEEILHDLESRVEEEEERNQSLQNEK--KKMQSHIQDLEEQLDEEEA 999
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1000 ARQKLQLEKVTAEAKIKKmeEDILLLEDQNSKFLKEKKL----LEDRVGEMtsQLAEEEEKAKNLGKVKNKQEMMMvdle 1075
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKREL--ERIRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1076 ERLKKEEKTRQELEKAkRKLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLR-ELQAQ 1154
Cdd:pfam17380 386 ERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEERAREMERVRLEEqERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1155 LAELQEDLESEKAARNKAEKLKRDLSEelealkteledtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQ 1234
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKR-----------------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1235 RHGTALEEiseqleqAKRVKGNLEKNKQtlesdnKELtNEVKSLQQAKSESEHKRKKLEA--QLQEVMARFSEGEKVKGE 1312
Cdd:pfam17380 525 RQKAIYEE-------ERRREAEEERRKQ------QEM-EERRRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAE 590
|
....*
gi 688558686 1313 LADRT 1317
Cdd:pfam17380 591 YEATT 595
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1074-1550 |
3.16e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1074 LEERLKKEektRQELEKAKRKLDaetTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQA 1153
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1154 QLAELQEDLEsekaARNKAEKLKRDLSEELEALKtELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR 1233
Cdd:COG4717 120 KLEKLLQLLP----LYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1234 QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAksesehKRKKLEAQLQEVMARFSEGEKVKGEL 1313
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE------ERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1314 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEES 1393
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1394 RKNLEKQLATLQAQLvetkkkleddvgALEGLEEVKRKLQKDMEVTS-QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1472
Cdd:COG4717 349 LQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1473 HQRQIVSNLEKKQKKfdQMLAEEKTISARYAEERDRAEAEAREKDTKaLSMARALDEALEAKEEFERLNKQLRAEMED 1550
Cdd:COG4717 417 ELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAE-LEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
974-1200 |
3.40e-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: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 974 QSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEE 1053
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1054 EEKaknLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLAR 1133
Cdd:COG4942 103 KEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1134 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ 1200
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1434-1829 |
6.09e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1434 KDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQmLAEEKTISARYAEERDRAEA-E 1512
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1513 AREKDTKAL--SMARALDEALEAKEEFERLNKQL----RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEL 1586
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1587 EDELQATEDAK-----------------------------------LRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVK 1631
Cdd:COG4717 233 ENELEAAALEErlkearlllliaaallallglggsllsliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1632 QVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRkLQAQMKDYQRELEEARTSRDEIFTQSK 1711
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1712 ENEKKLKSLEAEILQLQEDLASSERARRH--AEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1789
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 688558686 1790 --LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQN 1829
Cdd:COG4717 472 aeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
919-1300 |
8.34e-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: 60.29 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 919 QLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEE 998
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 999 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERL 1078
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1079 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAvlargdeevaqknnALKQLRELQAQLAel 1158
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEA--------------LLEELRSLQERLN-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1159 qedlesekAARNKAEKLKRDLSE---------------ELEALKTELEdTLDTTAAQQELRSKREQEVAELKKAIDDETR 1223
Cdd:pfam07888 248 --------ASERKVEGLGEELSSmaaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1224 NHESQIQEMRQRHGTALEEISEQleQAKRVKGNLEK--NKQTLESDNKELTNEVKSLQQAKSESEHkrkkLEAQLQEVM 1300
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMER--EKLEVELGREKdcNRVQLSESRRELQELKASLRVAQKEKEQ----LQAEKQELL 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1001-1307 |
1.24e-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: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1001 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--VGEMTSQLAEEEEKAKNLgkvknKQEMMMVD-LEER 1077
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERL-----DASSDDLAaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1078 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1157
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1158 LQEDLESEKA-ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQE-----VAELKKAIDDETRNHESQIQ- 1230
Cdd:COG4913 774 RIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFVADLLs 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1231 EMRQrhgtALEEISEQLEQAKRVKGNLEKNKQT---LESDNKELTnEVKSLQQ--------AKSESEHKRKKLEAQLQEV 1299
Cdd:COG4913 854 KLRR----AIREIKERIDPLNDSLKRIPFGPGRylrLEARPRPDP-EVREFRQelravtsgASLFDEELSEARFAALKRL 928
|
....*...
gi 688558686 1300 MARFSEGE 1307
Cdd:COG4913 929 IERLRSEE 936
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1103-1328 |
1.25e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1103 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEE 1182
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1183 LEALK---------------TELEDTLDTTAAQQELRSKREQEVAELKKAIdDETRNHESQIQEMRQRHGTALEEISEQL 1247
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1248 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1327
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
.
gi 688558686 1328 S 1328
Cdd:COG3883 251 A 251
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1082-1304 |
1.27e-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: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1082 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ--LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1159
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1160 EDLES--EKAARNKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRH 1236
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQ-IAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1237 GTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFS 1304
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
916-1297 |
1.65e-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: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 916 KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEIlhdlESRVEEEEERNQSLQNEKKKMqshiqdleeqld 995
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAIYAEQERM------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 996 eeeAARQKLQLEKVTAEAKIKKMEEdillledqnskflkekklledrvgemtsqlAEEEEKAKNLGKVKNKQEMMMvdle 1075
Cdd:pfam17380 343 ---AMERERELERIRQEERKRELER------------------------------IRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1076 ERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDELK--------IQLAKKEEELQAVLARGDEEVAQKNNALKQ 1147
Cdd:pfam17380 386 ERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1148 LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEElealktELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHES 1227
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1228 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQtlesdNKELTNEVKslqqaksESEHKRKKLEAQLQ 1297
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----EREMMRQIV-------ESEKARAEYEATTP 596
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1573-1785 |
1.78e-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: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1573 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVA 1652
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1653 AKKKLEMDLKDVEAQIEAANKArdEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLA 1732
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1733 SSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQS 1785
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1495-1965 |
1.81e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1495 EKTISARYAEERDRAEAEArekdtkALSMARALDEALEAKEEFERLNkqlraemeDLISSKDDVGKNVHELEKSKRTLEQ 1574
Cdd:PRK02224 169 ERASDARLGVERVLSDQRG------SLDQLKAQIEEKEEKDLHERLN--------GLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1575 QVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1654
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIE------------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1655 KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlqedLASS 1734
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE-------LEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1735 ERARRHAEQERDELADEIsnsasgkaalldekRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELageRSA 1814
Cdd:PRK02224 376 REAVEDRREEIEELEEEI--------------EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL---RTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1815 AQKSENARQQLERQNkdLKSKLQELEGS----VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVrRTEKKLKEVF 1890
Cdd:PRK02224 439 RERVEEAEALLEAGK--CPECGQPVEGSphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLE 515
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1891 MQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1965
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1256-1855 |
2.38e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.53 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1256 NLEKNKQTLESDNKELTNEVKSLQQAK---SESEHKRKKLEAQLQEVMarfsegekvkgelaDRTHKIQTELDNVSCLLE 1332
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEkshSITLKEIERLSIEYNNAM--------------DDYNNLKSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1333 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIrqleeeknnlleqqeeeeESRKNLEKQLATLQAQLVETK 1412
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPV------------------YKNRNYINDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1413 KKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1492
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV--------LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1493 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEAleaKEEFERLNKQLRAemedLISSKDDVGKNVHEL------- 1565
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSKVSSLNQRIRA----LRENLDELSRNMEMLngqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1566 --------EKSKRTLEQQVEE---MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVR 1634
Cdd:PRK01156 457 vcgttlgeEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1635 EMEAELEDERKQRALAVAAKKklEMDLKDVEAQ---------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1699
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYK--SLKLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1700 RTSRDEIFtqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELAdeisnsasGKAALLDEKRRLEARIAQleee 1779
Cdd:PRK01156 614 KSYIDKSI---REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND---- 678
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1780 leeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvksKFKASIAALE 1855
Cdd:PRK01156 679 ----------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK-----KIKKAIGDLK 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
881-1301 |
2.38e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 881 QVTRQEEEMQAKDEELIKVKERQVKVENELVEME---RKHQQLLEEKNILAEQLQAETELFAEAEEMRaRLVAKKQELEE 957
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELReelEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 958 ILHDLESRVEEEEERNQSLQNEKKK----MQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1033
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1034 KEKKLLEDR-----VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1108
Cdd:COG4717 241 LEERLKEARlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1109 LQAQIDELKIQLAKKEEELQAVLARgdeevaqknnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKT 1188
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDR-----------IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1189 ELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1268
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
410 420 430
....*....|....*....|....*....|...
gi 688558686 1269 keltnevkSLQQAKSESEHKRKKLEAQLQEVMA 1301
Cdd:COG4717 470 --------ELAELLQELEELKAELRELAEEWAA 494
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1606-1773 |
2.91e-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: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1606 AMKAQFDR--DLQARD---EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIK 1680
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1681 QLRKLQA--QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsg 1758
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-- 158
|
170
....*....|....*
gi 688558686 1759 kAALLDEKRRLEARI 1773
Cdd:COG1579 159 -EELEAEREELAAKI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
894-1849 |
3.13e-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: 59.29 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 894 EELIKVKERQVKVENELVEMERKHQQLLEEKniLAEQLQAETELFAEAEEMRARLVAK-KQELEEILHDLESRVEEEEER 972
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETATVELH--LSNIENKKNELLDIIVEIKKHIHGEiNKDLNKILEDFKNKEKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 973 NQSLQNEK---KKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQ 1049
Cdd:TIGR01612 771 INDYAKEKdelNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1050 LAEEEEKAKNlgKVKNKQEMMmVDLEERLKKEEKTRQeLEKAKRKLDaettDLQDQIAELQAQIDE--LKIQLAKKEEEL 1127
Cdd:TIGR01612 851 FINFENNCKE--KIDSEHEQF-AELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLKKVDEY 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1128 QAVLARGDEEVAQKNNALKQLRE-LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTlDTTAAQQEL--- 1203
Cdd:TIGR01612 923 IKICENTKESIEKFHNKQNILKEiLNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLN-DYEAKNNELiky 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1204 ------------RSKREQEVAELKKAIDD---ETRNHESQIQEMRQRHGTALEEISEQLEqaKRVKGNLEK-NKQTLESD 1267
Cdd:TIGR01612 1002 fndlkanlgknkENMLYHQFDEKEKATNDieqKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlNKEILEEA 1079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1268 NKELTNEVKSLQQAK----------------SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNvsclL 1331
Cdd:TIGR01612 1080 EINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIND----L 1155
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1332 EDAEKKGIKlTKDVSSLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLLEQQEEEEESRKNLEKqlaTLQ 1405
Cdd:TIGR01612 1156 EDVADKAIS-NDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGK---LFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1406 AQLVETKKKLEDDVGALEG----LEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDD----LMVDLDHQRQI 1477
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAyiedLDEIKEK--------SPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1478 vSNLEKKQKKFDQMLAEEKTISARYAE-ERDRAEAEAREKDT--------------KALSMARALDEALEAKEEFERLNK 1542
Cdd:TIGR01612 1301 -SDIREKSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDInlylneianiynilKLNKIKKIIDEVKEYTKEIEENNK 1379
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1543 QLRAEM---EDLISS-KDDVgknvhELEKSKRTLEQQVEEmrTQLEELEDELQATEDAKLRLEVNMqamkaqfDRDLQAR 1618
Cdd:TIGR01612 1380 NIKDELdksEKLIKKiKDDI-----NLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNI-------DTYFKNA 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1619 DEQNEEKKrALVKQVremeaELEDERKQRALAVA---AKKKLEMDLKDVEAQIEAANKARDEA---IKQLRKLQAQMKDY 1692
Cdd:TIGR01612 1446 DENNENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQY 1519
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1693 QRELEE------ARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1766
Cdd:TIGR01612 1520 KKDVTEllnkysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQ 1599
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1767 RRLEA------RIAQLEEELEEEQSNMELLNDRFrkTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1840
Cdd:TIGR01612 1600 LSLENfenkflKISDIKKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD 1677
|
....*....
gi 688558686 1841 gSVKSKFKA 1849
Cdd:TIGR01612 1678 -ELDSEIEK 1685
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
844-1444 |
3.21e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 844 KQQQLSALKVLQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK---HQQL 920
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 921 LEEKNILAEQLQAETELFAEAEEMRAR------------LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQ 988
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 989 DLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFlkEKKL--------LEDRVGEMTSQLAEEEEKAKNL 1060
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY--EDKLfdvcgsqdEESDLERLKEEIEKSSKQRAML 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1061 GKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQ 1140
Cdd:TIGR00606 659 AGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1141 KNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRS---KREQEVAELKKA 1217
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKIAQQAAKLQGS 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1218 IDDETRnheSQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQ 1297
Cdd:TIGR00606 819 DLDRTV---QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1298 EVMARFSE--------------GEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQE--LLQE 1361
Cdd:TIGR00606 896 EVQSLIREikdakeqdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdyLKQK 975
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1362 ETrqklNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLveTKKKLEDDVGALEGLEEVKRKLQKDMEV 1438
Cdd:TIGR00606 976 ET----ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNL--TLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
....*.
gi 688558686 1439 TSQKLE 1444
Cdd:TIGR00606 1050 LQMKQE 1055
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1052-1228 |
3.73e-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: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1052 EEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVL 1131
Cdd:COG3883 17 QIQAKQKELSELQAELE----AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1132 A-----------------------------RGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1182
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688558686 1183 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQ 1228
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1581-1965 |
4.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1581 TQLEELEDELQATEDAKLRLevnmqamkaqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAL--AVAAKKKLE 1658
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1659 MDLKDVEAQIEAAnkarDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ-SKENEKKLKSLEAEILQLQEDLASSERA 1737
Cdd:COG4717 139 AELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1738 RRHAEQERDELADEISNSASGKAALLDEKRRLEARI------------AQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1805
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1806 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1885
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1886 --LKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEASEGLSREVNTLKN 1961
Cdd:COG4717 374 alLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
....
gi 688558686 1962 RLRR 1965
Cdd:COG4717 454 ELAE 457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
875-1300 |
4.16e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 875 KVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRarlvaKKQE 954
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 955 leeilhdlesrveeeeernqslqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1034
Cdd:PTZ00121 1631 ------------------------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1035 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAElqaQID 1114
Cdd:PTZ00121 1687 EKKAAE--------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEE 1755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1115 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRDLSEELEAlkTELE 1191
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiieGGKEGNLVINDSKEMED--SAIK 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1192 DTLDTTAAQQElRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1271
Cdd:PTZ00121 1834 EVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDL----KEDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
410 420
....*....|....*....|....*....
gi 688558686 1272 TNEVKSLQQAKSESEHKRKKLEAQLQEVM 1300
Cdd:PTZ00121 1909 GKNNDIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1094-1247 |
4.33e-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: 56.09 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1094 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAV---LARGDEEVAQKNNALKQLRELQA-------------QLAE 1157
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteLEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1158 LQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHG 1237
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
170
....*....|
gi 688558686 1238 TALEEISEQL 1247
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1101-1697 |
5.42e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1101 DLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS 1180
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1181 EELEALK--TELEDTLDTTAAQQELRSKRE-QEVAELKKAIDDETR---NHESQIQEMRQRHGTA--LEEISEQLEQAKR 1252
Cdd:PRK01156 267 MELEKNNyyKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKKQilsNIDAEINKYHAIIKKLsvLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1253 VKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSclle 1332
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS---- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1333 daekkgikltKDVSSLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNLLEQQEEEEESRknlekqlatlqa 1406
Cdd:PRK01156 423 ----------SKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSNHIINHYNEKKSR------------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1407 qLVETKKKLEDDVGAlegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1486
Cdd:PRK01156 481 -LEEKIREIEIEVKD---IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1487 KFDQMLAEEKTISARYAEER----------------DRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1550
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1551 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEqneekKR 1627
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQiaeIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LE 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1628 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIkqLRK-----LQAQMKDYQRELE 1697
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAM--IRKsasqaMTSLTRKYLFEFN 774
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1493-1756 |
5.91e-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: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1493 AEEKTISARYAEERDRaeaeaREKDTKALS-MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1571
Cdd:pfam05667 226 WNSQGLASRLTPEEYR-----KRKRTKLLKrIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1572 L----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQ---NEEKKRALVKQVREMEAELEDER 1644
Cdd:pfam05667 301 ThtekLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQElekEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1645 KQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-EEARTSRDEIFTQSKENEKKL---KSL 1720
Cdd:pfam05667 380 EELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLeeiKEL 459
|
250 260 270
....*....|....*....|....*....|....*.
gi 688558686 1721 EAEILQLQEDLASSERARRHAEQERDELADEISNSA 1756
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSA 495
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1348-1900 |
6.69e-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: 57.83 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1348 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEE 1427
Cdd:pfam05557 32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLAD-------ARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1428 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERD 1507
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1508 RAEaearekdtkalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELE 1587
Cdd:pfam05557 185 DSE------------IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-EKYREEAATLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1588 DELQATEdAKLRLEVNMQAMKAQFDR---DLQARDEQNEEKKRALVKQVREMEAELEDERKQRalavaakKKLEMDLKDV 1664
Cdd:pfam05557 252 LEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR-------RELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1665 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEART---SRDEIFTQSKENEKKLKSLE--AEILQLQEDLASSERARR 1739
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1740 HAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELL--NDRFR--KTTMQVDTLNTELAGERSAA 1815
Cdd:pfam05557 404 SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEleRQRLReqKNELEMELERRCLQGDYDPK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1816 -----QKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK---LK 1887
Cdd:pfam05557 484 ktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKnqrLK 563
|
570
....*....|...
gi 688558686 1888 EVFMQVEDERRHA 1900
Cdd:pfam05557 564 EVFQAKIQEFRDV 576
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1287-1960 |
7.74e-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: 57.93 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1287 HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSslesqlQDTQELLQEETRQK 1366
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1367 LNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE--------VKRKLQKDMEV 1438
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1439 TSQKLE--------EKAIAFDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKTISARyaEERDRA 1509
Cdd:pfam12128 395 IKDKLAkireardrQLAVAEDDLQALESELREQLEAGKLEFnEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1510 EAEAREKDTKAL-SMARALDEALEAKEEFERLNKQLRAEmedlisskddvgknvhelekskrtlEQQVEEMRTQLEELED 1588
Cdd:pfam12128 473 IERAREEQEAANaEVERLQSELRQARKRRDQASEALRQA-------------------------SRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1589 ELQA---TEDAKLRLEVNM--QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA-ELEDERKQRALAVAAKKKLEMDLK 1662
Cdd:pfam12128 528 QLFPqagTLLHFLRKEAPDweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1663 DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSrdeiFTQSKENEKKLKS-LEAEILQLQEdlaSSERARRHA 1741
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1742 EQERDELADEISNSASGKAALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTMQVDTLNTELAGERSAAQKSE 1819
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1820 NArqqLERQNK-DLKSKlqELEGSVKSKFKASIAALEAKIlqleeqleqeakERAAankiVRRTEKKLKEVFMQvEDERR 1898
Cdd:pfam12128 750 KA---LETWYKrDLASL--GVDPDVIAKLKREIRTLERKI------------ERIA----VRRQEVLRYFDWYQ-ETWLQ 807
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1899 HADQYKEQMEKANSRMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLS---REVNTLK 1960
Cdd:pfam12128 808 RRPRLATQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRcemSKLATLK 876
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1001-1215 |
1.03e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1001 RQKLQlekvTAEAKIK--KMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEErL 1078
Cdd:COG3206 188 RKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-S 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1079 KKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAkkeEELQAVLARGDEEVAQknnALKQLRELQAQL 1155
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1156 AELQEDLESEKAARNKAEKLKRDlseeLEALKTELEDTLdttAAQQELRSKREQEVAELK 1215
Cdd:COG3206 337 AQLEARLAELPELEAELRRLERE----VEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1171-1888 |
1.11e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1171 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR-QRHGTAL--EEISEQL 1247
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNaTRHLCNLlkETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1248 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRTHKIQTELDNV 1327
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE------DHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1328 SCLLEDAEKKgikltkdvsslESQLQDTQELLqEETRQKLNlssrirQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQ 1407
Cdd:pfam05483 243 SLLLIQITEK-----------ENKMKDLTFLL-EESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1408 L---VETKKKLEDDVG-ALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQ----ELDDLMVDLDHQRQIVS 1479
Cdd:pfam05483 305 LqrsMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1480 NLEKKQKKFDQMlaeektisaryAEERDRAEAEAREKDTKALSMARALDEaleaKEEFERLNKQLRAEMEDLISSKDDVG 1559
Cdd:pfam05483 385 ELQKKSSELEEM-----------TKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1560 KNVHELE-------KSKRTLEQQVEEMRTQLE-ELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ--------NE 1623
Cdd:pfam05483 450 KEIHDLEiqltaikTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQediinckkQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1624 EKKRALVKQVREMEAELEDE--------RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE 1695
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDElesvreefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1696 LEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASserARRHAEQERDELADEISNSASGKAALLDEKRRLEARIaq 1775
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA-- 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1776 leeeleeeqsnmellnDRFRKTTMQVDTLNTELAGERSAAQKSENAR--QQLERQNKDL---KSKLQElEGSVKSKFKAS 1850
Cdd:pfam05483 685 ----------------DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIE 747
|
730 740 750
....*....|....*....|....*....|....*...
gi 688558686 1851 IAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1888
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1356-1599 |
1.18e-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: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1356 QELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1434
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1435 DMEVTSQKLEEKAIAFDKLEktknrlQQELDDLMVDLDHQRQIVSNLEkkqkKFDQMLAEEKTISARYAEERDRAEAEAR 1514
Cdd:COG4942 98 ELEAQKEELAELLRALYRLG------RQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1515 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1594
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 688558686 1595 DAKLR 1599
Cdd:COG4942 248 FAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
922-1144 |
1.28e-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: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 922 EEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDE--EEA 999
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1000 ARQKLQLEKVTAEA-KIKKMEEDILLLEDQN-SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEER 1077
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1078 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAVLARGDEEVAQKNNA 1144
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1613-1824 |
1.39e-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: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1613 RDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1692
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1693 QRELEEA-RTSRDEIFTQSKENEKKLKSLE----------AEILQLQEDLASSERARRHAEQERDELADEISNSASGKAA 1761
Cdd:COG4942 110 LRALYRLgRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1762 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQ 1824
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1013-1435 |
1.46e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1013 AKIKKMEEDILLLEDQNSKF---LKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM---------MVDLEERLKK 1080
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1081 EEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQL-AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1159
Cdd:COG4717 151 LEERLEELRELEEELEE----LEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1160 EDLESEKAARNKAEKLKRDLSEE-----------LEALKTELEDTLDTTAA------------QQELRSKREQEVAELKK 1216
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1217 AIDDETRN--HESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELtnEVKSLQQAKSESEHKRK-KLE 1293
Cdd:COG4717 307 LQALPALEelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGvEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1294 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLNLSSRI 1373
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1374 RQLEEEKNNLleqqeeeeesrkNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1435
Cdd:COG4717 463 EQLEEDGELA------------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
881-1446 |
1.57e-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: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 881 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELE 956
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 957 EILHDLESRVEEEEernQSLQNEKKKMQSHiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1036
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKN--------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1037 KLLedrvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERlkkeektrqelEKAKRKLDAETTDLQDQIAELQAQIDEL 1116
Cdd:pfam05483 412 KIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR-----------EKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1117 KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldt 1196
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE----- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1197 tAAQQELRSKREqevaELKKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVK 1276
Cdd:pfam05483 552 -SVREEFIQKGD----EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1277 SLQQAKSESEHKRKKLEAQLQEVMARFsegekvkGELADRTHK-IQTELDNVSCLLEDAEK------KGIKLTKDVsSLE 1349
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKF-------EEIIDNYQKeIEDKKISEEKLLEEVEKakaiadEAVKLQKEI-DKR 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1350 SQlQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDvgaleglEEVK 1429
Cdd:pfam05483 698 CQ-HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIE-------KEEK 769
|
570
....*....|....*..
gi 688558686 1430 RKLQKDMEVTSQKLEEK 1446
Cdd:pfam05483 770 EKLKMEAKENTAILKDK 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1075-1285 |
1.67e-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: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1075 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRE-LQA 1153
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREeLGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1154 QLAELQED----------LESE----------------KAARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQELRSKR 1207
Cdd:COG3883 91 RARALYRSggsvsyldvlLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1208 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1285
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1314-1550 |
1.68e-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: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1314 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeees 1393
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1394 rKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH 1473
Cdd:COG4942 86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1474 QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1550
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1539-1965 |
1.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1539 RLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnmqamkAQFDRDLQAR 1618
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1619 DEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV----EAQIEAANKARDEAIKQLRKLQAQMKDYQR 1694
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1695 ELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL-----DEKRRL 1769
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLflllaREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1770 EARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKskLQELEGSVKSKFKA 1849
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1850 SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVfmqvedERRHADQYKEQMEKansRMKQLKRQLEEAEEEAT 1929
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL------EELLEALDEEELEE---ELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558686 1930 RANASRRKLQRELDDATEASE--GLSREVNTLKNRLRR 1965
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
977-1730 |
2.29e-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: 56.60 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 977 QNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQ-NSKFLKEKKLLEDRVGEMTSQLaEEEE 1055
Cdd:TIGR01612 532 QNIKAKLYKEIEAGLKESYELAKNWKKLIHE---IKKELEEENEDSIHLEKEiKDLFDKYLEIDDEIIYINKLKL-ELKE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1056 KAKNLGKvKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI-AELQAQIDEL-KIQLAKKEEELQAVLAR 1133
Cdd:TIGR01612 608 KIKNISD-KNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIySTIKSELSKIyEDDIDALYNELSSIVKE 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1134 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELEDTLDTTAaqQELRSKR 1207
Cdd:TIGR01612 687 NAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsniENKKNELLDIIVEIKKHIHGEINKDLNKIL--EDFKNKE 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1208 EQEVAELK--KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRvkgNLEKNKQTL------ESDNKELTNEVKSLQ 1279
Cdd:TIGR01612 765 KELSNKINdyAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQ---NYDKSKEYIktisikEDEIFKIINEMKFMK 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1280 QAKSESEHKRKKLEAQLQEVM----ARFSE-GEKVKGELADR-------------------THKIQTELDNVSCLLEDAE 1335
Cdd:TIGR01612 842 DDFLNKVDKFINFENNCKEKIdsehEQFAElTNKIKAEISDDklndyekkfndskslineiNKSIEEEYQNINTLKKVDE 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1336 KkgIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKl 1415
Cdd:TIGR01612 922 Y--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIE--KSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNN- 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1416 eddvGALEGLEEVKRKLQKDMEVTSQKleekaiAFDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEE 1495
Cdd:TIGR01612 997 ----ELIKYFNDLKANLGKNKENMLYH------QFDEKEKATNDIEQKIEDA-------NKNIPNIEIAIHTSIYNIIDE 1059
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1496 ktISARYAEERDRAEAEAREKDTKALSMARALDEALE-------AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKS 1568
Cdd:TIGR01612 1060 --IEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1569 KRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQARDEQNEekkraLVKQVREMEAELEDERK 1645
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEE 1211
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1646 QRALAVA---------------AKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMkDYQRELEEARTSRDEI---F 1707
Cdd:TIGR01612 1212 VKGINLSygknlgklflekideEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETFNISHDDDkdhH 1290
|
810 820
....*....|....*....|...
gi 688558686 1708 TQSKENEKKLKSLEAEILQLQED 1730
Cdd:TIGR01612 1291 IISKKHDENISDIREKSLKIIED 1313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1555-1775 |
2.92e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1555 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVR 1634
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAK-LLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1635 EMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIK-------QLRKLQAQMKDYQREL-EEARTSRD 1704
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1705 EIFTQSKENEKKLKSLEAEILQLQEDLAS-SERARRHAEQERD-ELADEISNSasgkaaLLdeKRRLEARIAQ 1775
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1126-1298 |
3.22e-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: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1126 ELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtlDTTAAQQELRS 1205
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1206 KREQEvaelkkAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1285
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 688558686 1286 EHKRKKLEAQLQE 1298
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1405-1623 |
3.89e-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: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1405 QAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1484
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1485 QKKFDQMLAEEKTI--SARYAEERDRAEAEAREKDtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknv 1562
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEALKA------ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 1563 hELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNE 1623
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1217-1459 |
4.29e-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: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1217 AIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQL 1296
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1297 QEVMARFsegEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1376
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1377 EEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKT 1456
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 688558686 1457 KNR 1459
Cdd:COG4942 250 ALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1482-1965 |
4.56e-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: 55.46 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1482 EKKQKKFDQMLAEEKTISARYAEERDRAEA----EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDD 1557
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1558 VGKNVHELEKSKRTLEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRAL 1629
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1630 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1709
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1710 SKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1782
Cdd:TIGR02169 415 LQRLseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1783 EQSNMELLNDRFRKTTMQVDTLNTEL------------------------AGERSAAQKSEN------ARQQLERQN--- 1829
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgeryataievaAGNRLNNVVVEDdavakeAIELLKRRKagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1830 ------KDLKSKLQELE--------------------------------------------------------------- 1840
Cdd:TIGR02169 575 atflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtlegelfeksga 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1841 ---GSVKSKFKASIAA-LEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQ 1916
Cdd:TIGR02169 655 mtgGSRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1917 LKRQLEEAEEE-------ATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1965
Cdd:TIGR02169 735 LKERLEELEEDlssleqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
886-1412 |
4.65e-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: 55.44 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 886 EEEMQAKDEELIKVKERQVKVENELVEMER-KHQQLLEEKNILAEQLQAETELFAeaeemrarlVAKKQELEEILHDLES 964
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQnKNHINNELESKEEQLSSYEDKLFD---------VCGSQDEESDLERLKE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 965 RVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVG 1044
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1045 EMTS----QLAEEEEKAKNLGKVKNKQEMMMVD-------LEERLKKEEKTRQELEKAK---------RKLDAETTDLQD 1104
Cdd:TIGR00606 727 EMLGlapgRQSIIDLKEKEIPELRNKLQKVNRDiqrlkndIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDVER 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1105 QIAELQAQID---------ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQedleSEKAARNKAEKL 1175
Cdd:TIGR00606 807 KIAQQAAKLQgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK----SEKLQIGTNLQR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1176 KRDLSEELEALKTELEDTLdttaaqQELRSKREQEVAELKKAIDDETRNHE--SQIQEMRQRHGTALEEISEQLEQAKRV 1253
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLI------REIKDAKEQDSPLETFLEKDQQEKEEliSSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1254 KGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSegekvkgeladrTHKIQTELDNVSCLLE 1332
Cdd:TIGR00606 957 MKDIENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID------------TQKIQERWLQDNLTLR 1024
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1333 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETK 1412
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL--EENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1071-1948 |
4.68e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1071 MVDLEERLKKEEKT---RQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlakkEEELQAVLARgdeeVAQKNNAL-- 1145
Cdd:PRK04863 275 MRHANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAASDH----LNLVQTALrq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1146 -KQLRELQAQLAELQEDLESEKAARNKAeklkRDLSEELEALKTELEDTLDTTAAQqelrskreqeVAELKKAID-DETR 1223
Cdd:PRK04863 347 qEKIERYQADLEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDELKSQ----------LADYQQALDvQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1224 NheSQIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarf 1303
Cdd:PRK04863 413 A--IQYQQAVQ----ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1304 segekvkgeladrtHKIQTELDNvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEKN 1381
Cdd:PRK04863 483 --------------RKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLQQLRMRlsELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1382 NLLEQQEeeeesrkNLEKQLATLQAQLVEtkkkleddvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK---- 1457
Cdd:PRK04863 544 KRLGKNL-------DDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawl 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1458 ------NRLQ----------QELDDLMVD-LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKA 1520
Cdd:PRK04863 607 aaqdalARLReqsgeefedsQDVTEYMQQlLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1521 LSMARAlDEALEAKEEFERLNKQLR---------------AEMEDL----------ISSKDDVGKNVHELEK------SK 1569
Cdd:PRK04863 687 LSEIYD-DVSLEDAPYFSALYGPARhaivvpdlsdaaeqlAGLEDCpedlyliegdPDSFDDSVFSVEELEKavvvkiAD 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1570 RTL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDLQ-----ARDEQNEEKKR 1627
Cdd:PRK04863 766 RQWrysrfpevplfgraarEKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1628 ALVKQVREMEAELED----ERKQRALAVAAKKKL--------EMDLKDVEAQIEAANKARDEaIKQLRKLQAQMKDYQRE 1695
Cdd:PRK04863 841 QLNRRRVELERALADhesqEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQ-LDEAEEAKRFVQQHGNA 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1696 LEeartsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAllDEKRRLEARIAq 1775
Cdd:PRK04863 920 LA-----------QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD- 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1776 leeeleeeqsnmelLNDRFRkttmqvdtlntelagersaaQKSENARQQLERQNKDLKSKLQELegsvkSKFKASIAALE 1855
Cdd:PRK04863 986 --------------LNEKLR--------------------QRLEQAEQERTRAREQLRQAQAQL-----AQYNQVLASLK 1026
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1856 AkilqleeqleqeakERAAANKIVRRTEKKLKEVFMQVEDE-----RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR 1930
Cdd:PRK04863 1027 S--------------SYDAKRQMLQELKQELQDLGVPADSGaeeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDN 1092
|
970
....*....|....*...
gi 688558686 1931 ANASRRKLQRELDDATEA 1948
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1346-1770 |
4.95e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1346 SSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEkQLATLQAQLVETKKKLEDDVGALEG 1424
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1425 LEEVKRKLQKDMEVTSQ---------KLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkfDQMLAEE 1495
Cdd:COG4717 124 LLQLLPLYQELEALEAElaelperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1496 KTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR-----AEMEDLISSKDDVGKNVHE------ 1564
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaAALLALLGLGGSLLSLILTiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1565 ------------LEKSKRTLEQQVEEMR--TQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDL-----QARDEQNEEK 1625
Cdd:COG4717 281 lvlgllallfllLAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1626 KRALVKQVREMEAEL--------EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRK--LQAQMKDYQRE 1695
Cdd:COG4717 361 EELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1696 LEEARTSRDEIftqskenEKKLKSLEAEILQLQED--LASSERARRHAEQERDELADEISNSASGKAALLDEKRRLE 1770
Cdd:COG4717 441 LEELEEELEEL-------REELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
963-1174 |
5.87e-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: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 963 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIlllEDQNSKFLKEKKLLEDR 1042
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1043 VGEM-----TSQLAEEEEKAKNLGKVKNKQEMMMVDLE---ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1114
Cdd:COG3883 92 ARALyrsggSVSYLDVLLGSESFSDFLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1115 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1174
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1374-1963 |
6.23e-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: 54.74 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1374 RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKL 1453
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV---HEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1454 EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDR-AEAEAREKDTKALSMARALD---- 1528
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDteis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1529 -------------EAL--EAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTleqQVEEMRTQLEELEDELQAT 1593
Cdd:pfam15921 235 ylkgrifpvedqlEALksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1594 EDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELE----------------DERKQRALAVAAKKKL 1657
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdqfsqesgnlDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1658 EMDLKDVEAQ------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAE-- 1723
Cdd:pfam15921 392 ELSLEKEQNKrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQle 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1724 -----ILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNmellNDRFRKTT 1798
Cdd:pfam15921 472 stkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQ 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1799 MQVDTLNTELAGERSAA----QKSENARQ-----------------QLERQNKDLKSKLQELEgSVKSKFKASIAALEAK 1857
Cdd:pfam15921 548 TECEALKLQMAEKDKVIeilrQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQEFK-ILKDKKDAKIRELEAR 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1858 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQME--KANSRMK---------QLKRQLEEAEE 1926
Cdd:pfam15921 627 VSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKseemetttnKLKMQLKSAQS 706
|
650 660 670
....*....|....*....|....*....|....*..
gi 688558686 1927 EATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1963
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1055-1187 |
6.57e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.45 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1055 EKAK-NLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLakkEEELQAVLAR 1133
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1134 GDEEVAQknnALKQLRELQAQLA------ELQEDLESEKAARNKAEKLKRDLSEELEALK 1187
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYasvkahELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1399-1965 |
7.95e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1399 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEekaiafDKLEKTKNRLQQELDDLMVDLDHQRQIV 1478
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1479 SNLEKKQKKFDQMLAEEKtisARYAEERD--RAEAEAREKDTKALsmaraLDEALEAKEEFERLnKQLRAEmedliSSKD 1556
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKAL-----TGKHQDVTAKYNRR-RSKIKE-----QNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1557 DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlEVNMQamkaqfdrdlQARDEQNEEKKRALVKQVREM 1636
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-EFNEE----------EYRLKSRLGELKLRLNQATAT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1637 EAELEDERKQRALAVAAKKKLEMDLKDVE-AQIE--AANKARDEAIKQLRKLQAQMKDYQRELEEARTsrdEIFTQSKEN 1713
Cdd:pfam12128 460 PELLLQLENFDERIERAREEQEAANAEVErLQSElrQARKRRDQASEALRQASRRLEERQSALDELEL---QLFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1714 EKKLKSLEAEILQLQEDLASSE---RARRHAEQERDELADEISNSASGkaalLDEKR-----------RLEARIAQLEEE 1779
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPEllhRTDLDPEVWDGSVGGELNLYGVK----LDLKRidvpewaaseeELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1780 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKiL 1859
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ-L 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1860 QLEEQLEQEAKERAAANKIVRRTEK--KLKEVfmqVEDERRHADQYKEQMEKANSrmkQLKRQLEEAEEEATRANASRrk 1937
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASL-- 763
|
570 580
....*....|....*....|....*...
gi 688558686 1938 lqrelDDATEASEGLSREVNTLKNRLRR 1965
Cdd:pfam12128 764 -----GVDPDVIAKLKREIRTLERKIER 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1001-1157 |
8.95e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1001 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknLGKVKNKQEMmmvdleERLKK 1080
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEY------EALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1081 EEKTrqeLEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1157
Cdd:COG1579 97 EIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1542-1758 |
1.11e-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: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1542 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdlQARDEQ 1621
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1622 NEEKKR-------------ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1688
Cdd:COG3883 97 RSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1689 MKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1758
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1665-1888 |
1.13e-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: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1665 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLasserarrhaEQE 1744
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1745 RDELADEI------SNSASGKAALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAqks 1818
Cdd:COG3883 85 REELGERAralyrsGGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1819 ENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1888
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1278-1943 |
1.17e-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: 53.96 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1278 LQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADrthKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQE 1357
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE---EIQENKDLIK--ENNATRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1358 LLQEETRQ-KLNLSSRIrqleeEKNNLLEQQEEEEESRKNLEKQLatlqaqlvetkkKLEDDVGALEGLEEVKRKLQKDm 1436
Cdd:pfam05483 176 YEREETRQvYMDLNNNI-----EKMILAFEELRVQAENARLEMHF------------KLKEDHEKIQHLEEEYKKEIND- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1437 evtsqklEEKAIAFDKLEKTKNrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEARek 1516
Cdd:pfam05483 238 -------KEKQVSLLLIQITEK--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1517 dtKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAted 1595
Cdd:pfam05483 307 --RSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI--- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1596 aklrlevnmqamkaqFDRDLQARDEQNEEkkraLVKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKAR 1675
Cdd:pfam05483 382 ---------------ITMELQKKSSELEE----MTKFKNNKEVELEELKK----ILAEDEKLLDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1676 DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNS 1755
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1756 ASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1835
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1836 LQELEGSVKSKFKasiaaleaKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMK 1915
Cdd:pfam05483 596 CNNLKKQIENKNK--------NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660
....*....|....*....|....*...
gi 688558686 1916 QLKRQLEEAEEEATRANASRRKLQRELD 1943
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
886-1375 |
1.34e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 886 EEEMQAKDEELIKVKErqvkvenELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVA---KKQELEEILHDL 962
Cdd:PRK01156 189 EEKLKSSNLELENIKK-------QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 963 ESRVEEEEERN---QSLQNEKKKMQS--------HIQDLEEQLDEEEAARQKLQ---LEKVTAEAKIKKMEEdillLEDQ 1028
Cdd:PRK01156 262 ESDLSMELEKNnyyKELEERHMKIINdpvyknrnYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1029 NSKFLKEKKLLEDRVGEMT----------SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAE 1098
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1099 TTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG----------------------------DEEVAQKNNALKQLRE 1150
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiinhynekksrlEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1151 LQAQLAELQEDLESEKAARNKAEKLKrdlseeLEALKTELEDTLDTTAAQQELRSKREQEVAELKKA-IDDETRNHESQI 1229
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1230 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN-----------KELTNEVKSLQQAKSESEHKRKKLEA---- 1294
Cdd:PRK01156 572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddksyidksiREIENEANNLNNKYNEIQENKILIEKlrgk 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1295 --QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDA-------EKKGIKLTKDVSSLESQLQDTQELLQ--EET 1363
Cdd:PRK01156 652 idNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTIEILRTRINELSDRINDINETLEsmKKI 731
|
570
....*....|..
gi 688558686 1364 RQKLNLSSRIRQ 1375
Cdd:PRK01156 732 KKAIGDLKRLRE 743
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
829-1291 |
1.36e-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: 53.82 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 829 QSVCRGYLARkafAKKQQQLSALKVLQRNCAAY-----LKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVKErq 903
Cdd:TIGR00618 419 FRDLQGQLAH---AKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL-- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 904 vKVENELVEMER---KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEK 980
Cdd:TIGR00618 494 -ARLLELQEEPCplcGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 981 KKMQSHIQDLEEQLDEEEAARQKLQLE-KVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1059
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLtEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1060 LGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAKKEEELQAVLARGDE 1136
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlaQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1137 EVAQKNNALKQ-LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1215
Cdd:TIGR00618 733 DLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1216 KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKK 1291
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1271-1653 |
1.45e-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: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1271 LTNEVKSLQQAKSESEhkrkKLEAQLQEVMArfsEGEKVKGELADRTHKIQT---ELDNVSCLLEDAEKKGIKLTKDVSS 1347
Cdd:pfam19220 36 IEAILRELPQAKSRLL----ELEALLAQERA---AYGKLRRELAGLTRRLSAaegELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1348 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1427
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEE--------------NKALREEAQAAEKALQRAEGELATARERLALLEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1428 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERD 1507
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQ-----------------AERERAEAQLEEAVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1508 RAEAEARekdtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1587
Cdd:pfam19220 238 AHRAERA-------SLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1588 DELQATEDAKLRLEVNMQAM-KAQFDRD------------LQARDEQ----NEEKKRALVKQVREMEAELEDERKQRALA 1650
Cdd:pfam19220 311 QQFQEMQRARAELEERAEMLtKALAAKDaaleraeeriasLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALA 390
|
...
gi 688558686 1651 VAA 1653
Cdd:pfam19220 391 QGA 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1451-1664 |
1.56e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1451 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1514
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1515 EKDTKALSMARALDEALEAKEEFERLNKQLR---------AEMEDLISSKDDVGKnvhelekskrtLEQQVEEMRTQLEE 1585
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITK-----------IKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1586 LEDELQatEDAKLRLEVNMQAMKAqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1664
Cdd:PHA02562 318 LDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1014-1222 |
1.66e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1014 KIKKMEEDILL-LEDQNSKFLKE-------------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK--------QEMMM 1071
Cdd:PRK05771 2 APVRMKKVLIVtLKSYKDEVLEAlhelgvvhiedlkEELSNERLRKLRSLLTKLSEALDKLRSYLPKlnplreekKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1072 VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK------------------------IQLAKKEEEL 1127
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1128 QAVLARGDEEVAQKNN---------------ALKQLRELQAQLAELQEDLESEKAARNKAEKLKR------DLSEELEAL 1186
Cdd:PRK05771 162 LESDVENVEYISTDKGyvyvvvvvlkelsdeVEEELKKLGFERLELEEEGTPSELIREIKEELEEiekereSLLEELKEL 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 688558686 1187 KTELEDTLdtTAAQQELRSKREQEVAELKKAIDDET 1222
Cdd:PRK05771 242 AKKYLEEL--LALYEYLEIELERAEALSKFLKTDKT 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1435-1654 |
1.89e-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: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1435 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEA 1513
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1514 REKDT----KALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1589
Cdd:COG3883 97 RSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1590 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1654
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
885-1108 |
1.98e-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: 52.46 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 885 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELEEILH 960
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 961 DLESRVEEEEERNQSLQneKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE--AKIKKMEEDILLLEDQNSKFLKEKKL 1038
Cdd:COG4942 98 ELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1039 LEdrvgemtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1108
Cdd:COG4942 176 LE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1127-1356 |
2.92e-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: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1127 LQAVLARGDEEVAQKNNALKQLRE----LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQE 1202
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1203 LRSKREQevaeLKKaiddetRNHESQIQEMRQRHGTAL---EEISEQLEQAKRVKGNLEKNKQTLE---SDNKELTNEVK 1276
Cdd:COG3883 81 IEERREE----LGE------RARALYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEelkADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1277 SLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1356
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1074-1642 |
3.21e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1074 LEERLKKEEKTRQELEKAKRKLDAETT-------DLQDQIAELQAQIDELKIQLAKKE--EELQAVLARGDEEVAQKNNA 1144
Cdd:PRK10246 299 IQEQSAALAHTRQQIEEVNTRLQSTMAlrarirhHAAKQSAELQAQQQSLNTWLAEHDrfRQWNNELAGWRAQFSQQTSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1145 LKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE---LEDTLDTTAAQQELRSKREQEVAELKKAIDDE 1221
Cdd:PRK10246 379 REQLRQWQQQLTHAEQKLNALPAI---TLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1222 TRNHESQIQEMRQRHGTALEEISEQ---LEQAKRVKgNLEKNKQTLESDNK-----ELTNEVKSLQQAKSESEHKRKkLE 1293
Cdd:PRK10246 456 QTQRNAALNEMRQRYKEKTQQLADVktiCEQEARIK-DLEAQRAQLQAGQPcplcgSTSHPAVEAYQALEPGVNQSR-LD 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1294 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELL-----QEETRQKLN 1368
Cdd:PRK10246 534 ALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaQEEHERQLR 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1369 LSSRIRQLEEEKNNLleqqeeeeesrknlEKQLATLQAQLVETKKKLEDDVGAL------EGLEEvkrKLQKDMEVTSQK 1442
Cdd:PRK10246 614 LLSQRHELQGQIAAH--------------NQQIIQYQQQIEQRQQQLLTALAGYaltlpqEDEEA---SWLATRQQEAQS 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1443 LEEKAIAFDKLEKTKNRLQQELDDL--MVDLDHQRQIVSnLEKKQKKFDQML---AEEKTISARYAEERDRAeAEAREKD 1517
Cdd:PRK10246 677 WQQRQNELTALQNRIQQLTPLLETLpqSDDLPHSEETVA-LDNWRQVHEQCLslhSQLQTLQQQDVLEAQRL-QKAQAQF 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1518 TKALSMARALDealeaKEEFerlnkqLRAEMEDlisskddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA----- 1592
Cdd:PRK10246 755 DTALQASVFDD-----QQAF------LAALLDE---------ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQhqqhr 814
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1593 ------TEDAKlRLEVNMQAMKAQFdRDLQAR----------DEQNEEKKRALVKQVREMEAELED 1642
Cdd:PRK10246 815 pdgldlTVTVE-QIQQELAQLAQQL-RENTTRqgeirqqlkqDADNRQQQQALMQQIAQATQQVED 878
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
1073-1186 |
3.41e-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: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1073 DLEERLK--KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL----------------------- 1127
Cdd:pfam14362 107 EIDRELLeiQQEEADAAKAQLAAAYRARLAELEAQIAALDAEIDAAEARLDALQAEArceldgtpgtgtgvpgdgpvakt 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 1128 -QAVLARGDEEVAQ-KNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1186
Cdd:pfam14362 187 kQAQLDAAQAELAAlQAQNDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEAL 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1718-1962 |
3.63e-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: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1718 KSLEAEILQLQEDLASSERARRHAEQERDeladeisnsasgKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1797
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDARE------------QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1798 tmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEeqleqeaKERAAANK 1877
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-------RELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1878 IVRRTEKKLKEVFMQVEDErrhADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDateasegLSREVN 1957
Cdd:COG4913 360 RRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 688558686 1958 TLKNR 1962
Cdd:COG4913 430 SLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1564-1740 |
3.90e-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: 50.31 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1564 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQNEEKKralVKQVREMEAELEDE 1643
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN---NKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1644 RKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAqmkdyqrELEEARTSRDEIFTQSKENEKKLKSLEAE 1723
Cdd:COG1579 102 KRRIS-------DLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|....*....
gi 688558686 1724 ILQL--QEDLASSERARRH 1740
Cdd:COG1579 168 LAAKipPELLALYERIRKR 186
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1070-1451 |
4.33e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1070 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLR 1149
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1150 ELQAQLAELQEDLESekaarnkaeklkrdLSEELEALKTELEDTLDTtaAQQELRSKREQEvaELKKAIDDETRNHESQI 1229
Cdd:pfam07888 126 AHEARIRELEEDIKT--------------LTQRVLERETELERMKER--AKKAGAQRKEEE--AERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1230 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTL------ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1303
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1304 SEGE-----------KVKGELADRTHKIQTELDNVS----CLLEDAEKKGIKLTKdvssLESQLQDTQELLQEETRQKLN 1368
Cdd:pfam07888 268 DRTQaelhqarlqaaQLTLQLADASLALREGRARWAqereTLQQSAEADKDRIEK----LSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1369 LSSrirQLEEEKnnlLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKdmeVTSQKLEEKAI 1448
Cdd:pfam07888 344 LEV---ELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET---VADAKWSEAAL 414
|
...
gi 688558686 1449 AFD 1451
Cdd:pfam07888 415 TST 417
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1464-1842 |
4.49e-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: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1464 LDDLMVDLDHQRQIvsNLEKKQKKFDQMlaeektisaryAEERDRAEaeaREKDTKALSMARALDEALEAKEEFERLNKQ 1543
Cdd:pfam17380 271 LNQLLHIVQHQKAV--SERQQQEKFEKM-----------EQERLRQE---KEEKAREVERRRKLEEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1544 LRAEMEDLisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaQFDRDLQARDEQNE 1623
Cdd:pfam17380 335 IYAEQERM------------AMERERELERIRQEERKRELERIRQEEIAMEISRMR----------ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1624 ekkralvkQVREmeaELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1703
Cdd:pfam17380 393 --------RVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1704 DEIFTQsKENEKKLKSLEAEILQLQEDLASSERaRRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEE 1783
Cdd:pfam17380 462 VERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1784 QSNMELLNDRFRKTTMQVDTLNTElagERSAAQKSENARQQLeRQNKDLKSKLQELEGS 1842
Cdd:pfam17380 540 EERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1728-1966 |
4.68e-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: 51.30 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1728 QEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTE 1807
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1808 LAGERSAAQKSENARQQLERQNKdLKSKLQeleGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLK 1887
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1888 EVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRRG 1966
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1106-1345 |
5.00e-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: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1106 IAELQAQIDELKIQLAKKEEELQAvlaRGDEEVAQKNNA-LKQlrELQAQLAEL---QEDLES-EKAARNKAEKLKRD-L 1179
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNA---LADKERAEADRQrLEQ--EKQQQLAAIsgsQSQLEStDQNALETNGQAQRDaI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1180 SEELEALKTELE------DTLDTTAAQQELRSK--REQEVAELKKAID---DETRNHES-QIQEMRQRHGTALEEISEQL 1247
Cdd:NF012221 1612 LEESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKISGkQLADAKQRHVDNQQKVKDAV 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1248 EQAKRVKGNLEKNKQTLESDnkeltnevksLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1327
Cdd:NF012221 1692 AKSEAGVAQGEQNQANAEQD----------IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK 1761
|
250
....*....|....*...
gi 688558686 1328 SCLLEdAEKKGIKLTKDV 1345
Cdd:NF012221 1762 ANQAQ-ADAKGAKQDESD 1778
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1007-1516 |
5.55e-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: 51.67 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1007 EKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQ 1086
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK----------YLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1087 ELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE------ 1160
Cdd:pfam05557 98 QLADAREVISC----LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1161 -----------------DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETR 1223
Cdd:pfam05557 174 elefeiqsqeqdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1224 NH--ESQIQE---MRQRHGTAL---EEISEQLEQakrvkgnLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1295
Cdd:pfam05557 254 KEklEQELQSwvkLAQDTGLNLrspEDLSRRIEQ-------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1296 LQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLED------AEKKGIKLTKDVSSLESQLQDTQ-----------EL 1358
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydkeltMSNYSPQLLERIEEAEDMTQKMQahneemeaqlsVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1359 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR-KNLEKQLATLQAQLvetkKKLEDDVGALEgLEEVKRKLQKDME 1437
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvDSLRRKLETLELER----QRLREQKNELE-MELERRCLQGDYD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1438 VTSQK---LEEKAIAfdkleKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERdRAEAEAR 1514
Cdd:pfam05557 482 PKKTKvlhLSMNPAA-----EAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESA 555
|
..
gi 688558686 1515 EK 1516
Cdd:pfam05557 556 EL 557
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
919-1377 |
6.63e-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: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 919 QLLEEKNILaEQLQAETELfAEAEEMRARLvakkqELEEILHDLESRVEEEEERNQSLQNEKKKMQshiQDLEEQLDEEE 998
Cdd:pfam05557 3 ELIESKARL-SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 999 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMmmvdLEERL 1078
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL----LKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1079 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEE-----ELQAVLARGDEEVAQKNNALKQLRELQA 1153
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSElaripELEKELERLREHNKHLNENIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1154 QLAELQEDLESEKAARNKAEKLKRDLS---EELEALKTELEDTLDTTAAQQELRSK------REQEVAELKKAIDDETRN 1224
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEkleQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1225 HESQIQEMRQRHGTALEEISE---QLEQAKRVKGNLEKN-----------KQTLESDNKELTNEVKSLQQAK--SESEHK 1288
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDlnkKLKRHKALVRRLQRRvllltkerdgyRAILESYDKELTMSNYSPQLLEriEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1289 RKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLN 1368
Cdd:pfam05557 389 TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNE 466
|
....*....
gi 688558686 1369 LSSRIRQLE 1377
Cdd:pfam05557 467 LEMELERRC 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1517-1761 |
7.61e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1517 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL------ 1590
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1591 -QATEDAKLRLEV------------NMQAMKAQFDRDLQARDEQNEEKKralvkQVREMEAELEDERKQralAVAAKKKL 1657
Cdd:COG3883 95 lYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1658 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1737
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260
....*....|....*....|....
gi 688558686 1738 RRHAEQERDELADEISNSASGKAA 1761
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1053-1187 |
8.31e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1053 EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL--KIQLAKKEEELQav 1130
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLerELSEARSEERRE-- 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558686 1131 lARGDEEVAQKNNALKQLR----ELQAQLAELQEDLESEKAARNKaeklkrDLSEELEALK 1187
Cdd:COG2433 461 -IRKDREISRLDREIERLEreleEERERIEELKRKLERLKELWKL------EHSGELVPVK 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
899-1195 |
9.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 899 VKERQVKVEnelvEMERKHQQLLEEKNILAEQLQAETELfAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQN 978
Cdd:PRK02224 470 IEEDRERVE----ELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 979 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIllledqnskflkekklleDRVGEMTSQLAEEEEKAK 1058
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI------------------ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1059 NLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDlqDQIAELQAQIDELKIQLAKKEEELQAVLARGDE-- 1136
Cdd:PRK02224 607 EIERLREKRE----ALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDlq 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1137 -EVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLK---RDLSEEL-----EALKTELEDTLD 1195
Cdd:PRK02224 681 aEIGAVENELEELEELRERREALENRVEALEALYDEAEELEsmyGDLRAELrqrnvETLERMLNETFD 748
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1565-1769 |
9.61e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1565 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1643
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1644 RKQRALAVAAKKKLEMDLKDVEAQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARTSRDE-- 1705
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1706 -IFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1769
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1082-1358 |
1.01e-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: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1082 EKTRQELEKAkRKLDAETTD----LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1157
Cdd:pfam04108 17 TDARSLLEEL-VVLLAKIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1158 LQE-----------DLESEKAARNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKreQEVAELKKAIDDETRNH 1225
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDLKRfDDDLRDLQKELESL--SSPSESISLIPTLLKEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1226 ESQIQEMRQRhgtaLEEIS---EQLEQAKRV-KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA 1301
Cdd:pfam04108 174 ESLEEEMASL----LESLTnhyDQCVTAVKLtEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNS 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1302 RFSEGEKVKGELADrthkIQTELDN-VSCLLEDAEkkgiKLTKDVSSLESQLQDTQEL 1358
Cdd:pfam04108 250 LIDELLSALQLIAE----IQSRLPEyLAALKEFEE----RWEEEKETIEDYLSELEDL 299
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
932-1170 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 932 QAETELFAEAEEMRArLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTA 1011
Cdd:COG3883 13 FADPQIQAKQKELSE-LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1012 EAKIKKMEE-------------------DILLLEDQNSKFLKEKKLLeDRVGEMTSQLAEEEEKAKNlgKVKNKQEmmmv 1072
Cdd:COG3883 78 EAEIEERREelgeraralyrsggsvsylDVLLGSESFSDFLDRLSAL-SKIADADADLLEELKADKA--ELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1073 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1152
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....*...
gi 688558686 1153 AQLAELQEDLESEKAARN 1170
Cdd:COG3883 231 AAAAAAAAAAAAAASAAG 248
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1069-1300 |
1.20e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1069 MMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQL 1148
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1149 RELQAQLAELQEDLESEKAARNKAEKLKRD---LSEELEALKTELEDTLDTTAAQQEL--RSKR-EQEVAELKKAID--D 1220
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEknE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1221 ETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE---LTNEVKSLQQAKSESEHKRKKLEAQLQ 1297
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEadeLHKEIVEAQEKADELHEEIIELQKELR 240
|
...
gi 688558686 1298 EVM 1300
Cdd:COG1340 241 ELR 243
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1074-1249 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1074 LEERLKKEEKTRQELEK-----AKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLArgdeevaqknnalKQL 1148
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-------------QNV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1149 RELQAQLAELQEDLesEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ-----QELRSKREQEVAELKKAIDDETR 1223
Cdd:pfam01442 69 EELRQRLEPYTEEL--RKRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*.
gi 688558686 1224 NHESQIQEMRQRHGTALEEISEQLEQ 1249
Cdd:pfam01442 147 EVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1095-1310 |
1.25e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1095 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1174
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY---DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1175 LKRDLSEELEALKTEL----EDTLDTTAAQQ-----ELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRhgtaLEEISE 1245
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKELQHSLEKL----DTAIDELEEI----MDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1246 QLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1310
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLitlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
692-716 |
1.31e-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: 1.31e-05
10 20
....*....|....*....|....*
gi 688558686 692 YKESLTKLMATLRNTNPNFVRCIIP 716
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1032-1378 |
1.34e-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: 50.34 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1032 FLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQA 1111
Cdd:COG5185 171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1112 QIDELKIQLAKKEEELQAVLARGDEEVA----QKNNALKQLRELQAQLAELQEDLESEKA------------ARNKAEKL 1175
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKrlneNANNLIKQFENTKEKIAEYTKSIDIKKAtesleeqlaaaeAEQELEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1176 KRDLSEELEALKTELEDTLDT-TAAQQELRSKREQEVAELKKAIDDET-RNHESQIQEMRQRHGTALEEiseQLEQAKRV 1253
Cdd:COG5185 331 KRETETGIQNLTAEIEQGQESlTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQN---QRGYAQEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1254 KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKiqteldnvSCLLED 1333
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN--------RSVRSK 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 688558686 1334 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1378
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAE 524
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1620-1772 |
1.36e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1620 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE--------AANKARD----EAIKQLRKLQA 1687
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1688 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK- 1766
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 688558686 1767 RRLEAR 1772
Cdd:COG1842 175 EEMEAR 180
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1088-1244 |
1.44e-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: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1088 LEKAKRKLDAETTDLQDQIAELQAQIDelkiQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKA 1167
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1168 ARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQE-LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1244
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
936-1572 |
1.63e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 936 ELFAEAEEMRaRLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKI 1015
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1016 KKMEEDILLLED---QNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqemmmvDLEERLKKEEKTRQeleKAK 1092
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYK-----------ELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1093 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ--AVLARGDEEVAQKNnalKQLRELQAQLAELQEDLESEKAARN 1170
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKK---SRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1171 KAEKLK---RDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQL 1247
Cdd:PRK01156 371 SIESLKkkiEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1248 ------------------EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA-QLQEVMARFSEGEK 1308
Cdd:PRK01156 447 emlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1309 VKGELADRTHKIQTeldnvsclLEDAEKKGIKLTKDVSSLEsqlqdtQELLQEETRQKLNLSSRIRQLEEEknnlleqqe 1388
Cdd:PRK01156 527 ARADLEDIKIKINE--------LKDKHDKYEEIKNRYKSLK------LEDLDSKRTSWLNALAVISLIDIE--------- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1389 eeeesrknlekqlaTLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNrlqqELDDLM 1468
Cdd:PRK01156 584 --------------TNRSRSNEIKKQLND---LESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN----EIQENK 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1469 VDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEaearekdtkalSMARALDEALEAKEEFERLNKQLRAEM 1548
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK-----------KSRKALDDAKANRARLESTIEILRTRI 711
|
650 660
....*....|....*....|....
gi 688558686 1549 EDLISSKDDVGKNVHELEKSKRTL 1572
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKKAI 735
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1505-1947 |
1.69e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1505 ERDRAEAEAREKDTKALsmARALDEALEAKEEFERLNKQLRAEMEDLisskdDVGKNVHELEKSKRTLEQQVEEMRTQLE 1584
Cdd:COG4717 77 EEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1585 ELEDELQATEDaklrLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1664
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1665 EAQIEA-ANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEK--------------KLKSLEAEILQLQE 1729
Cdd:COG4717 226 EEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1730 DLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELA 1809
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1810 GERSAAQKSEnARQQLERQNKDLKSKLQELEGSVKSKFKA-SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKe 1888
Cdd:COG4717 386 ELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELE- 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1889 vfmQVEDERRHADQYKEQmekansrmKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1947
Cdd:COG4717 464 ---QLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1157-1417 |
1.76e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1157 ELQEDLESEK--AARNKAEKLK-RDLSEELEALKTELEDTLDTTAAQQ----ELRSKREQEVAELKKAIDD---ETRNHE 1226
Cdd:PHA02562 154 KLVEDLLDISvlSEMDKLNKDKiRELNQQIQTLDMKIDHIQQQIKTYNknieEQRKKNGENIARKQNKYDElveEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1227 SQIqemrqrhgtalEEISEQLEqakrvkgNLEKNKQTLESDNKELTNEvkslqQAKSESEHKRKKLEAQLQE-------V 1299
Cdd:PHA02562 234 AEI-----------EELTDELL-------NLVMDIEDPSAALNKLNTA-----AAKIKSKIEQFQKVIKMYEkggvcptC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1300 MARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI---KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1376
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDefnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 688558686 1377 EEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLED 1417
Cdd:PHA02562 371 QAE--------------FVDNAEELAKLQDELDKIVKTKSE 397
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
954-1594 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 954 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaarQKLQLEKVTAEA-------KIKKMEEDILLLE 1026
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---------QINDLEDVADKAisnddpeEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1027 DQNSKFLKEKKLLEDRVGEM-TSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1105
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1106 IAELQAQIDelkiqlAKKEEELQAVLARGDEE---VAQKNNalkqlrelqaqlaelqedlESEKAARNKAEKLKRDLSEE 1182
Cdd:TIGR01612 1263 ENEMGIEMD------IKAEMETFNISHDDDKDhhiISKKHD-------------------ENISDIREKSLKIIEDFSEE 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1183 --LEALKTELEDTLDTTAAQQELRSKREQEVAELK--------KAIDDETRNHESQIQEMRQRHGTALEEiSEQLEQAKR 1252
Cdd:TIGR01612 1318 sdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYnilklnkiKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLIKKIK 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1253 VKGNLEKNKQTLES--DNKELTNEVKSLQQAKSEsehkrkkleaqlqevmarfsegekvkgeladrthkIQTELDNVSCL 1330
Cdd:TIGR01612 1397 DDINLEECKSKIEStlDDKDIDECIKKIKELKNH-----------------------------------ILSEESNIDTY 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1331 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQlatlqaqlv 1409
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNdHDFNINELKEHIDKSKGCKDEADKNAKAIEKN--------- 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1410 etkkkleddvgaleglEEVKRKLQKDMEVTSQKLEEKAIAfDKLEKTKNRLQQELDDLMvdlDHQRQIVSNLEKKQKKFD 1489
Cdd:TIGR01612 1513 ----------------KELFEQYKKDVTELLNKYSALAIK-NKFAKTKKDSEIIIKEIK---DAHKKFILEAEKSEQKIK 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1490 QMLAEEKTISARYAEERDRAEA------EAREKDTKALSMARALDEALEAKEEFERLNKQLRA----EMEDLISSKDDVG 1559
Cdd:TIGR01612 1573 EIKKEKFRIEDDAAKNDKSNKAaidiqlSLENFENKFLKISDIKKKINDCLKETESIEKKISSfsidSQDTELKENGDNL 1652
|
650 660 670
....*....|....*....|....*....|....*
gi 688558686 1560 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1594
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
897-1918 |
2.08e-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: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 897 IKVKERQVKVENELVEMERKHQQLLEEKNILAEQLqAETELFAEAEEMRAR---LVAKKQELEEILHD--------LESR 965
Cdd:TIGR01612 605 LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQVPEHLKNKdkiYSTIKSELSKIYEDdidalyneLSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 966 VEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlekvtaeAKIKKMEEDILLLEDQNSKFLKEKklLEDRVGE 1045
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKIDKEY---------------------DKIQNMETATVELHLSNIENKKNE--LLDIIVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1046 MTSQLAEE--EEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAelqaqIDELKIQLAK- 1122
Cdd:TIGR01612 741 IKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-----IDNIKDEDAKq 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1123 ---KEEELQAVLARGDEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDtldttaa 1199
Cdd:TIGR01612 812 nydKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD------- 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1200 qqELRSKREQEVAELKKAIDDETRNHESQIQEMrqrhgTALEEISEQLEQAKRVKGNLEK--NKQTL--ESDNKEL---- 1271
Cdd:TIGR01612 883 --DKLNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTLKKVDEYIKICENTKESIEKfhNKQNIlkEILNKNIdtik 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1272 -TNEVK---------SLQQAKSESEHKRKKL-----EAQLQEVMARFSEGEKVKGElaDRTHKIQTELDNVSCLLEDAEK 1336
Cdd:TIGR01612 956 eSNLIEksykdkfdnTLIDKINELDKAFKDAslndyEAKNNELIKYFNDLKANLGK--NKENMLYHQFDEKEKATNDIEQ 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1337 KGIKLTKDVSS---------------LESQLQDTQELLQEETRQKLNLS----SRIRQ----------LEEEKNNLLEQQ 1387
Cdd:TIGR01612 1034 KIEDANKNIPNieiaihtsiyniideIEKEIGKNIELLNKEILEEAEINitnfNEIKEklkhynfddfGKEENIKYADEI 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1388 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVgaleglEEVKRKLQKDMEVTsqkleEKAIAFDKLEKTKNRLQqeldDL 1467
Cdd:TIGR01612 1114 NKIKDDIKNLDQKIDHHIKALEEIKKKSENYI------DEIKAQINDLEDVA-----DKAISNDDPEEIEKKIE----NI 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1468 MVDLDHQRQIVSNLEK------KQKKFDQMLAEEKTISARYAE-------ERDRAEAEAREKDTKAL-SMARALDEALEA 1533
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGINLSYGKnlgklflEKIDEEKKKSEHMIKAMeAYIEDLDEIKEK 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1534 KEEFER---LNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNM-QAMKA 1609
Cdd:TIGR01612 1259 SPEIENemgIEMDIKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLlDAQKH 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1610 QFDRDLQARDEQN------EEKKRALVKQVREMEAELEDERKQ------RALAVAAKKKLEMDLKDVEAQIEAA--NKAR 1675
Cdd:TIGR01612 1338 NSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDDINLEECKSKIESTldDKDI 1417
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1676 DEAIKQLRKLQAQMkdyqreLEEaRTSRDEIFTQSKENEKKL----KSLE------AEILQLQEDLASSERARRHAE-QE 1744
Cdd:TIGR01612 1418 DECIKKIKELKNHI------LSE-ESNIDTYFKNADENNENVlllfKNIEmadnksQHILKIKKDNATNDHDFNINElKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1745 RDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN--DRFRKTTMQVD----------TLNTELAGER 1812
Cdd:TIGR01612 1491 HIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNkfAKTKKDSEIIIkeikdahkkfILEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1813 SAAQKSENARQQLERQNKDLKSK----LQELEGSVKSKFkASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK--- 1885
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKNDKSNKaaidIQLSLENFENKF-LKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKeng 1649
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 688558686 1886 -----LKEVFMQVEDERRHADQYKEQMEKANSRMKQLK 1918
Cdd:TIGR01612 1650 dnlnsLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1506-1771 |
2.84e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1506 RDRAEAEAREKDTKALSMARALDEA---LEAKEEFERLNKQLRAEMEdlISSKDDVGKnvhELEKSKRTLEQQVEEMRTQ 1582
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEAldkLRSYLPKLNPLREEKKKVS--VKSLEELIK---DVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1583 LEELEDELQATEDAKLRLEVnmqaMKAqFDRDLQARDEQ----------NEEKKRALVKQVREMEAELEDERKQRALAVA 1652
Cdd:PRK05771 109 ISELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1653 AKKKlemdlkdveaqieaanKARDEAIKQLRKLqaqmkDYQR-ELEEARTSRDEIftqsKENEKKLKSLEAEILQLQEDL 1731
Cdd:PRK05771 184 VVLK----------------ELSDEVEEELKKL-----GFERlELEEEGTPSELI----REIKEELEEIEKERESLLEEL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 688558686 1732 ASSerarrhaeqeRDELADEISNSasgKAALLDEKRRLEA 1771
Cdd:PRK05771 239 KEL----------AKKYLEELLAL---YEYLEIELERAEA 265
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1675-1840 |
2.84e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1675 RDEAIKQLRKLQAQMKDyQRELEEARTSrdeiftqskenekklkSLEAEILQLQEDLASSERARRHAEQERDELADEISn 1754
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1755 SASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS 1834
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
|
170
....*....|....
gi 688558686 1835 KL--------QELE 1840
Cdd:PRK09039 180 RLnvalaqrvQELN 193
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
886-1254 |
2.94e-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: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 886 EEEMQAKDEELIKVKERQV----KVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRAR--------LVAKKQ 953
Cdd:pfam09731 51 LGEDPPLAPKPKTFRPLQPsvvsAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE--KEATKDAAEakaqlpksEQEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 954 ELEEILHDLESRVEEEEERNQSLQNEKKK-MQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEDILLLEDQNSK 1031
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQaVKAHTDSLKEASDTAEISREKaTDSALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1032 FLKEKKLLEDRVGEMTS----QLAEEEEKAKNLGKVKNKqemmMVDLEErlKKEEKTRQELEK--------AKRKLDAET 1099
Cdd:pfam09731 209 AAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQQELVSifpdiipvLKEDNLLSN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1100 TDLQDQIAELQAQIDELKIQLA--KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLA--ELQEDLESEKAARNKAEKL 1175
Cdd:pfam09731 283 DDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRESY 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1176 KRDLSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNHESQIQEMRQRHG---TALEEISEQLEQAKR 1252
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRK 441
|
..
gi 688558686 1253 VK 1254
Cdd:pfam09731 442 AQ 443
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1422-1919 |
2.94e-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: 49.36 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1422 LEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK-KQKKFD--QMLAEEKTI 1498
Cdd:pfam07111 75 LRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEgSQRELEeiQRLHQEQLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1499 SARYAEERDRA----EAEAREKDTKALSMARA--LDEALEAKEEFERLNKQLRAEMEDLISS------------------ 1554
Cdd:pfam07111 155 SLTQAHEEALSsltsKAEGLEKSLNSLETKRAgeAKQLAEAQKEAELLRKQLSKTQEELEAQvtlveslrkyvgeqvppe 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1555 ---------KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEK 1625
Cdd:pfam07111 235 vhsqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1626 KRALVKQVREMEAELEDERKQRALAVAAKKK-----------LEMDLKDVEAQIEA--------------ANKAR----- 1675
Cdd:pfam07111 315 VFALMVQLKAQDLEHRDSVKQLRGQVAELQEqvtsqsqeqaiLQRALQDKAAEVEVermsakglqmelsrAQEARrrqqq 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1676 --DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL----------KSLEAEILQLQEDLASSERARRHAEQ 1743
Cdd:pfam07111 395 qtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQESCPPPPPAPP 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1744 ERDELADEISNSASGKAALlDEKRRLEARIAQLEEELEEEQSNMELLndRFRKTTMQVDT---------------LNTEL 1808
Cdd:pfam07111 475 VDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAERQ--QLSEVAQQLEQelqraqeslasvgqqLEVAR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1809 AGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqlEEQLEQEAKERAAANKIVRRT--EKKL 1886
Cdd:pfam07111 552 QGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAtqEKER 628
|
570 580 590
....*....|....*....|....*....|...
gi 688558686 1887 KEVFMQVEDERRhadqyKEQMEKANSRMKQLKR 1919
Cdd:pfam07111 629 NQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1009-1213 |
3.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1009 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQEL 1088
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL---QAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1089 EKAKRK--------------LDAETTD-----------LQDQIAELQAQIDELKIQLAKKEEELQAVLArgdEEVAQKNN 1143
Cdd:COG3883 89 GERARAlyrsggsvsyldvlLGSESFSdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLA---ELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1144 ALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1213
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
884-1304 |
3.42e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 884 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL------LEEKNILAEQLQAETE-LFAEAEEMRARLVAKKQELE 956
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksIESLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 957 EILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDillledqnskFLKEK 1036
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINH----------YNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1037 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVD-LEERLKKEEKTRQELEKAKRKLdAETTDLQDQIAELQAQIDE 1115
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKS 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1116 LKIQL--AKKEEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE 1189
Cdd:PRK01156 558 LKLEDldSKRTSWLNALAVISLIDIetnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1190 LEDTLDTTAAQQELRSKRE---QEVAElKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLES 1266
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDnykKQIAE-IDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRARLESTIEILRT 709
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558686 1267 DNKELTNEVKSLQQaKSESEHKRKKLEAQLQEVMARFS 1304
Cdd:PRK01156 710 RINELSDRINDINE-TLESMKKIKKAIGDLKRLREAFD 746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1427-1678 |
3.46e-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: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1427 EVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisaryaeER 1506
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1507 DRAEAEAREKDTKALsMARALDEAleakeefERLNKQLRAEMedLISSKDdvgknVHELEKSKRTLEQQVEEMRTQLEEL 1586
Cdd:COG4942 91 EIAELRAELEAQKEE-LAELLRAL-------YRLGRQPPLAL--LLSPED-----FLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1587 E---DELQATEdaklrlevnmQAMKAQFDRDLQARDEQNEEKKR--ALVKQVREMEAELEDERKQRALAVAAKKKLEMDL 1661
Cdd:COG4942 156 RadlAELAALR----------AELEAERAELEALLAELEEERAAleALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*..
gi 688558686 1662 KDVEAQIEAANKARDEA 1678
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
880-1111 |
3.78e-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: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 880 LQVTRQE------EEMQAKDEELIKVKERQVKVENELVEMERkhqqlleeknILAEQLQAETELFAEAEEMRARlvakkq 953
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEMEQ----------IRAEQEEARQREVRRLEEERAR------ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 954 ELEEI-LHDLESRVEEEEERNQSLQNEKKKMQshIQDLEEQLDEEEAARQKLqLEKVTAEAKIKKMEEDillledqnskf 1032
Cdd:pfam17380 447 EMERVrLEEQERQQQVERLRQQEEERKRKKLE--LEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEE----------- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1033 lKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEM---MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAEL 1109
Cdd:pfam17380 513 -RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeerRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
..
gi 688558686 1110 QA 1111
Cdd:pfam17380 592 EA 593
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1219-1449 |
4.11e-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: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1219 DDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQE 1298
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1299 VmarFSEGEKVK-----------GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqkl 1367
Cdd:COG3883 95 L---YRSGGSVSyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1368 nLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKA 1447
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
..
gi 688558686 1448 IA 1449
Cdd:COG3883 245 SA 246
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1015-1242 |
4.70e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1015 IKKMEEDILLLE-------DQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQE 1087
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE-EQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1088 LEKA-KRKLDAETTDLQDQIAELQAQIDELKIQLA--KKEEELQAVLargdeevaQKNNAL--KQLRELQAQLAELQEDL 1162
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKL--------EKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1163 esekaarNKAEKLKRD-LSEELEalktELEDTLDTTAAQ-----------QELRSKREQEVAELKKAiddETRNHESQIQ 1230
Cdd:PLN02939 288 -------SKLSPLQYDcWWEKVE----NLQDLLDRATNQvekaalvldqnQDLRDKVDKLEASLKEA---NVSKFSSYKV 353
|
250
....*....|..
gi 688558686 1231 EMRQRHGTALEE 1242
Cdd:PLN02939 354 ELLQQKLKLLEE 365
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1014-1328 |
4.92e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1014 KIKKMEEDILLLEDQNSK--FLKEKKLL----------EDRVGEMTSQLAE----EEEKAKNLGKVKNKQEMMMVD---- 1073
Cdd:PRK04778 80 SLPDIEEQLFEAEELNDKfrFRKAKHEIneieslldliEEDIEQILEELQEllesEEKNREEVEQLKDLYRELRKSllan 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1074 ----------LEERLKKEEKTRQELEKAK------------RKLDAETTDLQDQIA-----------ELQAQIDELKIQL 1120
Cdd:PRK04778 160 rfsfgpaldeLEKQLENLEEEFSQFVELTesgdyveareilDQLEEELAALEQIMEeipellkelqtELPDQLQELKAGY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1121 AKKEEE--------LQAVLARGDEEVAQKNNALKQLR--ELQAQLAELQED-------LESEKAARNKAEKLKRDLSEEL 1183
Cdd:PRK04778 240 RELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDldEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1184 EALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---IDDETRNHE---SQIQEMrqrhgtaLEEISEQL 1247
Cdd:PRK04778 320 EHAKEQNKELKEEIDrvkqsytlNESELESVRqlEKQLESLEKQydeITERIAEQEiaySELQEE-------LEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1248 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKL----------------EAQLQEVMARFSEG----E 1307
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSnlpglpedylemffevSDEIEALAEELEEKpinmE 472
|
410 420
....*....|....*....|.
gi 688558686 1308 KVKGELadrtHKIQTELDNVS 1328
Cdd:PRK04778 473 AVNRLL----EEATEDVETLE 489
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1331-1536 |
5.96e-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: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1331 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVE 1410
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1411 TKKKLEDDVGAL----------------EGLEEVKRK---LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDL 1471
Cdd:COG3883 84 RREELGERARALyrsggsvsyldvllgsESFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1472 DHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEE 1536
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1112-1280 |
6.65e-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: 47.32 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1112 QIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELqaqLAELQEDLESEKAARNKAEKLKrdlSEELEALKTELE 1191
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDCD---PTELDRAKEKLK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1192 DTLDTTAAQQELRSKREQEVAELKKAIDDETrnhesqiqemrqrhgtalEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1271
Cdd:smart00787 215 KLLQEIMIKVKKLEELEEELQELESKIEDLT------------------NKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
|
....*....
gi 688558686 1272 TNEVKSLQQ 1280
Cdd:smart00787 277 KEQLKLLQS 285
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1474-1965 |
6.96e-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: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1474 QRQIVSNLEKKQKkFDQMLAEEKTISAryaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIS 1553
Cdd:TIGR00618 165 KKELLMNLFPLDQ-YTQLALMEFAKKK---SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1554 SKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrDLQARDEQNEEKKRALVKQV 1633
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA---AHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1634 REMEAELEDERKQRALAVAAKKKLEmdlkdveaqieaankardEAIKQLRKLQAQMKDYQRELEEArTSRDEIFTQSKEN 1713
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIE------------------EQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1714 EKKLKSLEA--EILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN 1791
Cdd:TIGR00618 378 TQHIHTLQQqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1792 DRFRKTTMQvdtlntELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSvKSKFKASIAALEAKILQLEEQLEQEAKE 1871
Cdd:TIGR00618 458 KIHLQESAQ------SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1872 RAAANKiVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeaeeeATRANASRRKLQRELDDATEASEG 1951
Cdd:TIGR00618 531 QRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....
gi 688558686 1952 LSREVNTLKNRLRR 1965
Cdd:TIGR00618 603 LSEAEDMLACEQHA 616
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1102-1749 |
7.92e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1102 LQDQIAELQAQIDELKIQLAKKEEELQAVLargdeevaqknNALKQLRElqaqlAELQEDLESEKAARNKAEKLK---RD 1178
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTFWS-----PELKKERALRKEEAARISVLKeqyRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1179 LSEELEALKTELEDTLDTTAAQQELRSKREQEV------AELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQakr 1252
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1253 VKGNLEKNKQTLESDNKELTN-----EVKSLQQAKSESEHKRKK----LEAQLQEVMARFSEGEKVKGELADRTHK---I 1320
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKllemlQSKGLPKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREELHRrnqL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1321 QTELDNVSCLLEDAEKKGIKltkdVSSLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKN-----NLLEQQEEEE 1391
Cdd:pfam10174 222 QPDPAKTKALQTVIEMKDTK----ISSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKShskfmKNKIDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1392 ESRKN-----LEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1466
Cdd:pfam10174 298 LSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1467 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMArALDEALEAKEE-FERLN 1541
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1542 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ------ATEDAKLR-LEVNMQAMKAQFDR- 1613
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSKl 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1614 DLQARDEQNEE----KKRALVKQVREMEAELEDERKQRALAVA-------AKKKLEMDLKDVEAQIEAANKARDEAIKQL 1682
Cdd:pfam10174 537 ENQLKKAHNAEeavrTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMKEQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1683 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKlkslEAEILQLQEDLASSERARRHAEQERDELA 1749
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1140-1443 |
8.09e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1140 QKNNALKQLRELQA-QLAELQEDLESEKAarNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEVAELKKAI 1218
Cdd:PRK05771 17 YKDEVLEALHELGVvHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLP------KLNPLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1219 DDetrnhesqiqemrqrhgtaLEEISEQLEqaKRVKGnleknkqtLESDNKELTNEVKSLQQAKSESEhkrkKLEAqLQE 1298
Cdd:PRK05771 89 KD-------------------VEEELEKIE--KEIKE--------LEEEISELENEIKELEQEIERLE----PWGN-FDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1299 VMARFSEGEKVKGELAdRTHKIQTE----LDNVSCLLEDAEKKG------IKLTKDVSSLESQLQDTqELLQEETRQKLN 1368
Cdd:PRK05771 135 DLSLLLGFKYVSVFVG-TVPEDKLEelklESDVENVEYISTDKGyvyvvvVVLKELSDEVEEELKKL-GFERLELEEEGT 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1369 LSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGL--EEVKRKLQKDMEVTSQKL 1443
Cdd:PRK05771 213 PSELIREIKEEL--------------EEIEKERESLLEELKELAKKYLEELLALYEYleIELERAEALSKFLKTDKT 275
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1175-1305 |
8.15e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1175 LKRDLSEELEALKTELEDTLDttAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtalEEISEQLEQAKRVK 1254
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR-------NELQKLEKRLLQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 688558686 1255 GNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1305
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1071-1167 |
8.76e-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: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1071 MVDLEERLKKEEKTRQELEKAKRKLDAET-TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNnalkQLR 1149
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG----KIP 488
|
90
....*....|....*...
gi 688558686 1150 ELQAQLAELQEDLESEKA 1167
Cdd:COG0542 489 ELEKELAELEEELAELAP 506
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1145-1489 |
8.77e-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: 47.81 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1145 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTaaQQELRSKREQEVAELKKAIDDETRN 1224
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1225 HESQIQEMRQRHGtalEEISEQLEQAKRVKgNLEKNKQtlesdnKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfs 1304
Cdd:pfam17380 379 ELERLQMERQQKN---ERVRQELEAARKVK-ILEEERQ------RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1305 EGEKVKGELADRTHKIQTELDnvscllEDAEKKGIKLTKDvsslesqlqdtqellQEETRQKLnlssrirqLEEEKnnll 1384
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQ------QEEERKRKKLELE---------------KEKRDRKR--------AEEQR---- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1385 eqqeeeeesRKNLEKQLATLQAQLVETKKK-------LEDDVGALegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK 1457
Cdd:pfam17380 494 ---------RKILEKELEERKQAMIEEERKrkllekeMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
330 340 350
....*....|....*....|....*....|..
gi 688558686 1458 NRlQQELDDLMVDLDHQRQIVSNlEKKQKKFD 1489
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVES-EKARAEYE 592
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1504-1731 |
8.85e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1504 EERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL 1583
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1584 EELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDeQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKD 1663
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRA-ELKE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1664 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDL 1731
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1107-1361 |
9.19e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1107 AELQAQIDELKiqlakKEEELQAvlargDEEVAQKNnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1186
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQD--LEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1187 KTELEDTLDTTAAQQELRSkREQEVAELkkaiddetrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEs 1266
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQ-LESRLAQT-----------LDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1267 dnkELTNEVKSLQQAKSESEHKRK-KLEAQLQEVMARFSEGekvkgeladrthkiQTELDNVSCLLEDAEKKGIKLTKDV 1345
Cdd:PRK11281 174 ---QIRNLLKGGKVGGKALRPSQRvLLQAEQALLNAQNDLQ--------------RKSLEGNTQLQDLLQKQRDYLTARI 236
|
250
....*....|....*.
gi 688558686 1346 SSLESQLQDTQELLQE 1361
Cdd:PRK11281 237 QRLEHQLQLLQEAINS 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1520-1761 |
9.20e-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: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1520 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtleQQVEEMRTQLEELEDELQATEDAKLR 1599
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1600 LEVNMQAMKAQFDRdlQARDEQNEEKKRALVKQVreMEAELEDERKQRALAV-----AAKKKLEmDLKDVEAQIEAANKA 1674
Cdd:COG3883 77 AEAEIEERREELGE--RARALYRSGGSVSYLDVL--LGSESFSDFLDRLSALskiadADADLLE-ELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1675 RDEAIKQLRKLQAQMKDYQRELEeartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISN 1754
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE----------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
....*..
gi 688558686 1755 SASGKAA 1761
Cdd:COG3883 222 AAAAAAA 228
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1620-1743 |
9.44e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.83 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1620 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE------------AANKARDEAIKQLRKLQA 1687
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaaltkGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1688 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQ 1743
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1031-1467 |
1.11e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1031 KFLKEKKLLEDRVGEMTSQ-LAEEEEKAKNLGkvknkqemMMVDLEERLKKEEKTRQELEkakrklDAETTDLQDQIAEL 1109
Cdd:pfam06160 7 KIYKEIDELEERKNELMNLpVQEELSKVKKLN--------LTGETQEKFEEWRKKWDDIV------TKSLPDIEELLFEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1110 QAQIDELKIQLAKKE-EELQAVLARGDEEVAQKNNALKQLrelqaqlaelqedLESEKAARNKAEKLK---RDLSEELEA 1185
Cdd:pfam06160 73 EELNDKYRFKKAKKAlDEIEELLDDIEEDIKQILEELDEL-------------LESEEKNREEVEELKdkyRELRKTLLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1186 LKTELEDTLDTTAAQ-QELRSKREQEVaELKKAID-DETRNHESQIQEMrqrhgtaLEEISEQLEqakRVKGNLEKNKQT 1263
Cdd:pfam06160 140 NRFSYGPAIDELEKQlAEIEEEFSQFE-ELTESGDyLEAREVLEKLEEE-------TDALEELME---DIPPLYEELKTE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1264 LESDNKELTNEVKSLQQAKSESEH-----KRKKLEAQLQEVMARFSEGE--KVKGELADrthkIQTELDNVSCLLE---D 1333
Cdd:pfam06160 209 LPDQLEELKEGYREMEEEGYALEHlnvdkEIQQLEEQLEENLALLENLEldEAEEALEE----IEERIDQLYDLLEkevD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1334 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQkLNLSSRIRQLEEEKNnlleqqeeeeesrKNLEKQLATLQAQLVETKK 1413
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELER-VQQSYTLNENELERV-------------RGLEKQLEELEKRYDEIVE 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1414 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1467
Cdd:pfam06160 351 RLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEF 404
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1013-1293 |
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 688558686 1013 AKIKKMEEDILLLEDqnskFLKEKKLLEDRVGEMTSQLAEEEEKAkNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKak 1092
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEK-- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1093 rKLDAETTDLQDQIAELQA--QIDELkIQLAKKEEElqavlaRGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARN 1170
Cdd:pfam18971 636 -KLESKSGNKNKMEAKAQAnsQKDEI-FALINKEAN------RDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFD 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1171 KAEKLK-RDLS---EELEALKTELED----------TLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqeMRQRH 1236
Cdd:pfam18971 708 EFKNGKnKDFSkaeETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI--INQKV 785
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1237 GTALEEISEQLEQAKRVkGNLEKNKQTLeSDNKELTNEVKSLQQAKSESEHKRKKLE 1293
Cdd:pfam18971 786 TDKVDNLNQAVSVAKAM-GDFSRVEQVL-ADLKNFSKEQLAQQAQKNEDFNTGKNSE 840
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1662-1858 |
1.35e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1662 KDVEAQIEAANKARDeaikqlrkLQAQMKDYQRELEEARTSRDEIFTQSKENE---KKLKSLEAEILQLQEDLASSERAr 1738
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1739 rhaeqerdelADEISNSASGKAALldekRRLEARIAQLEEELEEEQSNMELLNDrfrkttmQVDTLNTelAGERSAAQKS 1818
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQNDLAEYNS-------QLVSLQT--QPERAQAALY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 688558686 1819 ENAR--QQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKI 1858
Cdd:PRK11281 167 ANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN 208
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1500-1819 |
1.36e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1500 ARYAEERDRaEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1579
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1580 RTQLEELEDELQATEDAKLRLEVNMQAMKaqfdrdlqardeqneEKKRALVKQVREMEAElederkqralavaaKKKLEM 1659
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAE--------------RKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1660 DLKDVEAQIEAANKardeAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERArr 1739
Cdd:pfam07888 179 KLQQTEEELRSLSK----EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1740 hAEQERDELADEISNSASGKAALldEKRRLEAR----------------IAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1803
Cdd:pfam07888 253 -VEGLGEELSSMAAQRDRTQAEL--HQARLQAAqltlqladaslalregRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330
....*....|....*.
gi 688558686 1804 LNTELAGERSAAQKSE 1819
Cdd:pfam07888 330 LEERLQEERMEREKLE 345
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1441-1965 |
1.44e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1441 QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKD 1517
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1518 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR-----------------TLEQQVEEMR 1580
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1581 TQLEELEDELQATEDAKLRLEVnMQAMKAQFDRDLQARDEQN---------EEKKRALVKQVREMEAELEDERKQR---- 1647
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilelegyEMDYNSYLKSIESLKKKIEEYSKNIerms 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1648 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQS----------------- 1710
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhi 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1711 -KENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1789
Cdd:PRK01156 471 iNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1790 LNDRFRKTTMQ-VDTLNTELAgeRSAAQKS----ENARQQLERQNK---DLKSKLQELEGS---VKSKFKASIAALEAKI 1858
Cdd:PRK01156 551 IKNRYKSLKLEdLDSKRTSWL--NALAVISlidiETNRSRSNEIKKqlnDLESRLQEIEIGfpdDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1859 LQLEEQLEQEAKERAAANKIvRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEeaeeeatRANASRRKL 1938
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-------DAKANRARL 700
|
570 580
....*....|....*....|....*..
gi 688558686 1939 QRELDDATEASEGLSREVNTLKNRLRR 1965
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLES 727
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1664-1918 |
1.62e-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: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1664 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFT--QSKENEKKLKSLEAEILQLQEDLASSERARRHA 1741
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1742 EQERDELADEISNSASGKAAlldekRRLEARIAQleeeleeeqsnmellndrfrkttmqvdtLNTELAGERSAAQKSENA 1821
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVI-----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1822 RQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqleeqleqeakerAAANKIVRRTEKKLKEvFMQVEDE----R 1897
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQARE--------------ASLQAQLAQLEARLAE-LPELEAElrrlE 357
|
250 260
....*....|....*....|.
gi 688558686 1898 RHADQYKEQMEKANSRMKQLK 1918
Cdd:COG3206 358 REVEVARELYESLLQRLEEAR 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
949-1131 |
1.79e-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: 45.30 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 949 VAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1028
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1029 NSKFLKEKklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1108
Cdd:COG1579 82 LGNVRNNK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|...
gi 688558686 1109 LQAQIDELKIQLAKKEEELQAVL 1131
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPEL 176
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1522-1875 |
1.86e-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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1522 SMARALDEALEAKEEFERLNKQLRAEMEDLISSKddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLe 1601
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELPQAK----SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1602 vnmQAMKAQFDRDLQARDEQNEEKK---RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEA 1678
Cdd:pfam19220 89 ---VARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1679 IKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASS----ERARRHAEQERDELADEISN 1754
Cdd:pfam19220 166 RERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEqaerERAEAQLEEAVEAHRAERAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1755 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQ------ 1828
Cdd:pfam19220 246 LRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraelee 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1829 -----NKDLKSKLQELEGSVKS-------------KFKASIAALEAKILQLEEQLEQEAKERAAA 1875
Cdd:pfam19220 326 raemlTKALAAKDAALERAEERiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1094-1775 |
1.98e-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: 46.35 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1094 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNnalkQLRELQAQLAELQEDLESEKAARNKAE 1173
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHL----REELHRRN----QLQPDPAKTKALQTVIEMKDTKISSLE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1174 KLKRDLSEELEALKTELEdtLDTTAAQQELRSkreqevAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEqakrv 1253
Cdd:pfam10174 247 RNIRDLEDEVQMLKTNGL--LHTEDREEEIKQ------MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLE----- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1254 kgnleknkqTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVkgeLADRTHKIQteldnvsclled 1333
Cdd:pfam10174 314 ---------TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESF---LNKKTKQLQ------------ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1334 aekkgiKLTKDVSSLESQLQDTQELLQEETRqKLNLssrirqleeeknnlleqqeeeeesrknLEKQLATLQAQLVETKK 1413
Cdd:pfam10174 370 ------DLTEEKSTLAGEIRDLKDMLDVKER-KINV---------------------------LQKKIENLQEQLRDKDK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1414 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDlmvDLDHQRQIVSNLEKKQKKFDQMLA 1493
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1494 EEKTISARYAEERDRAEAEAREKDTKALSMARALDealEAKEEFERLNKQLraemedlisskddvgKNVHELEKSKRTLE 1573
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE---QKKEECSKLENQL---------------KKAHNAEEAVRTNP 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1574 QQVEemRTQLEELEDELQATEDAKLRLEVnmqamkaqfDRDLQA-RDEQNEekKRALVKQVREMEAELEDERKQRALAVA 1652
Cdd:pfam10174 555 EIND--RIRLLEQEVARYKEESGKAQAEV---------ERLLGIlREVENE--KNDKDKKIAELESLTLRQMKEQNKKVA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1653 AKKKLEMDLK------DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL- 1725
Cdd:pfam10174 622 NIKHGQQEMKkkgaqlLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRk 701
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558686 1726 QLQEDLASSERARRHAEQERDELADEISNSASGK-------AALLDEKRRLEARIAQ 1775
Cdd:pfam10174 702 QLEEILEMKQEALLAAISEKDANIALLELSSSKKkktqeevMALKREKDRLVHQLKQ 758
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1612-1735 |
2.09e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1612 DRDLQARDEQNEEKKRALVKQVREMEAELEDE---RKQRALAVAAKKKLEMDLKDVEAQIEAANK------ARDEAIKQL 1682
Cdd:COG1566 78 PTDLQAALAQAEAQLAAAEAQLARLEAELGAEaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqqELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 688558686 1683 RKLQAQMKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAEILQLQEDLASSE 1735
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREE-EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
881-1360 |
2.09e-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: 46.27 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 881 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLVAKKQELEE 957
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 958 IlHDLESRVeeeeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKL-QLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1036
Cdd:pfam05557 199 I-PELEKEL-------ERLREHNKHLNENIENKLLLKEEVEDLKRKLeREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1037 KLLEDRVGE-MTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDE 1115
Cdd:pfam05557 271 TGLNLRSPEdLSRRIEQLQQREIVLKEENS-------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1116 L--KIQLAKKEEE-LQAVLARGDEEVAQKN---NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTE 1189
Cdd:pfam05557 344 LqrRVLLLTKERDgYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1190 LedTLDTTAAQQELRSKREQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEqakrvkgnLEKNKQTLESDNK 1269
Cdd:pfam05557 424 L--QALRQQESLADPSYSKEEVDSLRRKLET--------LELERQR----LREQKNELE--------MELERRCLQGDYD 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1270 ELTNEVKSLQQ-AKSESEHKRKKLEAQLQEVMARfsegekvkgeLADRTHKIQTELDNVSCL----LEDAEKKGIKLTKD 1344
Cdd:pfam05557 482 PKKTKVLHLSMnPAAEAYQQRKNQLEKLQAEIER----------LKRLLKKLEDDLEQVLRLpettSTMNFKEVLDLRKE 551
|
490
....*....|....*.
gi 688558686 1345 VSSLESQLQDTQELLQ 1360
Cdd:pfam05557 552 LESAELKNQRLKEVFQ 567
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1434-1678 |
2.15e-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: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1434 KDMEVTSQKLEEKAIAfdklEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKTISAryaeERDRAEAEA 1513
Cdd:NF012221 1552 KQDDAAQNALADKERA----EADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1514 REKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIssKDDVGKnvhELEKSKRTLEQQVEEMRTQLE----ELEDE 1589
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQE---QLDDAKKISGKQLADAKQRHVdnqqKVKDA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1590 LQATEDAKLRLEVNMQAMKAQFDrdlQARDEQNEEKKRALVKQVREMEAElederkQRALAVAAKKKLEMDlKDVEAQIE 1669
Cdd:NF012221 1691 VAKSEAGVAQGEQNQANAEQDID---DAKADAEKRKDDALAKQNEAQQAE------SDANAAANDAQSRGE-QDASAAEN 1760
|
....*....
gi 688558686 1670 AANKARDEA 1678
Cdd:NF012221 1761 KANQAQADA 1769
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1095-1249 |
2.28e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1095 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEK 1174
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDL----QDSVANLRASLSAAEAERSRLQALLAELA---GAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1175 LKRDLSEELEALKTELEDTLDTTAA-QQELRSKREQeVAELKKAIDD-ETRNHESQ--IQEMRQRHGTALEEISEQLEQ 1249
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDAsEKRDRESQakIADLGRRLNVALAQRVQELNR 194
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1393-1601 |
2.44e-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: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1393 SRKNLEKQLATLQAQ------LVETKKKLEDDVgalEGLEEVKRK--LQK-DMEVTSQKLEEKaiafdkLEKTKNRLQQE 1463
Cdd:pfam15066 340 SNLYLEKKVKELQMKitkqqvFVDIINKLKENV---EELIEDKYNviLEKnDINKTLQNLQEI------LANTQKHLQES 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1464 lddlmvdldhqrqivsnleKKQKKFDQMlaEEKTISARYAEERDRAEAEAREKDtKALSMARALDEALEAKE-EFERLnK 1542
Cdd:pfam15066 411 -------------------RKEKETLQL--ELKKIKVNYVHLQERYITEMQQKN-KSVSQCLEMDKTLSKKEeEVERL-Q 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1543 QLRAEMEDLISSKDDVgknvheLEKSKRTLEQQVEEMRTQLEELEDE-LQATEDAKLRLE 1601
Cdd:pfam15066 468 QLKGELEKATTSALDL------LKREKETREQEFLSLQEEFQKHEKEnLEERQKLKSRLE 521
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1654-1835 |
2.51e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1654 KKKLEMDLKDVEAqieAANKARDEAIKQL---------RKLQAQ-MKDYQRELEE----ARTSRDEIFTQSKE-----NE 1714
Cdd:PRK10929 25 EKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEprsvpPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1715 KKLKSLEAEILQLQEDLAssERARRhAEQERDElADEISNSASGKAALLDEKRRL----EARI-AQLEEELEEEQSNMEL 1789
Cdd:PRK10929 102 MSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688558686 1790 LNDRFRKTTMQVDTLntELagersaAQKSENARQQLERQNKDLKSK 1835
Cdd:PRK10929 178 LQAESAALKALVDEL--EL------AQLSANNRQELARLRSELAKK 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1086-1314 |
2.68e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1086 QELEKAKRKLD------AETTDLQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQKNNALkQLRELQAQLAELQ 1159
Cdd:PRK11281 63 QDLEQTLALLDkidrqkEETEQLKQQLAQAPAKLRQAQ-------AELEALKDDNDEETRETLSTL-SLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1160 EDLESekaarnkaekLKRDLSE---ELEALKTELEDtldttaAQQEL--RSKREQEVAELKKAIDDETRNHESQIQEMRQ 1234
Cdd:PRK11281 135 DQLQN----------AQNDLAEynsQLVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1235 RHGTALEEISEQLEQakrvkgNLEKNKQTLESDNKELtnEVKSLQQAKSESE---------HKRKKL------EAQLQEV 1299
Cdd:PRK11281 199 AEQALLNAQNDLQRK------SLEGNTQLQDLLQKQR--DYLTARIQRLEHQlqllqeainSKRLTLsektvqEAQSQDE 270
|
250
....*....|....*
gi 688558686 1300 MARFSEGEKVKGELA 1314
Cdd:PRK11281 271 AARIQANPLVAQELE 285
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1585-1857 |
3.25e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1585 ELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElederkqrALAVAAKKKLEMDLKDV 1664
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAEARAAKDKDAVAA--------ALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1665 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskENEKKlKSLEAEIlqlqedlassERAR-RHAEQ 1743
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAA------------ADPKK-AAVAAAI----------ARAKaKKAAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1744 ErDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmqvdtlnTELAGERSAAQKSENARQ 1823
Cdd:PRK05035 565 Q-AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA---------VAAAIARAKAKKAEQQAN 634
|
250 260 270
....*....|....*....|....*....|....
gi 688558686 1824 QLERQNKDLKsklqelegsvKSKFKASIAALEAK 1857
Cdd:PRK05035 635 AEPEEPVDPR----------KAAVAAAIARAKAR 658
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
948-1324 |
3.54e-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: 45.45 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 948 LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK----------LQLEKVTAEA---- 1013
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKylllqkqleqLQEENFRLETardd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1014 ---KIKKMEEDILLLEDQNSKFLK---EKKLLED----------RVGEMTSQLAEEEEKAKNLG----KVKNKQEMMM-- 1071
Cdd:pfam05622 85 yriKCEELEKEVLELQHRNEELTSlaeEAQALKDemdilressdKVKKLEATVETYKKKLEDLGdlrrQVKLLEERNAey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1072 ----VDLEERLKKEEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNN---A 1144
Cdd:pfam05622 165 mqrtLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTlreT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1145 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLseeleaLKTELEDTLdttaaqqeLRSKREQEVAELKKAIDDETRn 1224
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI------MPAEIREKL--------IRLQHENKMLRLGQEGSYRER- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1225 hesqiqemrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE-------SEHKRKKLEAQLQ 1297
Cdd:pfam05622 306 ---------------LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLE 370
|
410 420
....*....|....*....|....*..
gi 688558686 1298 EVMARFSEGEKVKGELADRTHKIQTEL 1324
Cdd:pfam05622 371 KLHEAQSELQKKKEQIEELEPKQDSNL 397
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1492-1648 |
3.61e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1492 LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED----LISSKDDVGKNVHELEK 1567
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1568 SKRTLEQQVEEMRTQLEELE------DELQATEDAKLRLEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELE 1641
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEkkeeelEELIEEQLQELERISGLTAEEAK----EILLEKVEEEARHEAAVLIKEIEEEAK 183
|
....*..
gi 688558686 1642 DERKQRA 1648
Cdd:PRK12704 184 EEADKKA 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
914-1247 |
3.80e-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: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 914 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQ--SLQNEKKkmqsHIQDLE 991
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELE----RLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 992 EQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknlgkvknkqemmm 1071
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--------------- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1072 vDLEERLKKEEKTRQELEKAKRkldaettdLQDQIAELQAQIDELKIQLAKKEEELQ----AVLARGDEEVAQKNNALKQ 1147
Cdd:COG4913 750 -LLEERFAAALGDAVERELREN--------LEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLAL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1148 LRELQAQ-LAELQEDLESEKAARNKAEK--LKRDLSEELEALKTELE---DTL------DTTAAQQELRSKREQEVAELK 1215
Cdd:COG4913 821 LDRLEEDgLPEYEERFKELLNENSIEFVadLLSKLRRAIREIKERIDplnDSLkripfgPGRYLRLEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|..
gi 688558686 1216 KAIDDETRNHESQIQEMRQRHGTALEEISEQL 1247
Cdd:COG4913 901 QELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
980-1361 |
4.18e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 980 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVT----------------------AEAKIKKMEEDILLLEDQNSK--FLKE 1035
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLPVNDELEKVKklnltgqseekfeewrqkwdeiVTNSLPDIEEQLFEAEELNDKfrFRKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1036 KKLLedrvGEMTSQLAEEEEKAKNLgkvknKQEMM-MVDLEERLKKE-EKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1113
Cdd:PRK04778 104 KHEI----NEIESLLDLIEEDIEQI-----LEELQeLLESEEKNREEvEQLKDLYRELRKSLLANRFSFGPALDELEKQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1114 DELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDT 1193
Cdd:PRK04778 175 ENLEEEFSQFVELTES----GDYVEAR-----EILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1194 ---LDTTAAQQELRSKREQeVAELKKAID----DETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEKNKQTLES 1266
Cdd:PRK04778 246 gyhLDHLDIEKEIQDLKEQ-IDENLALLEeldlDEAEEKNEEIQE-------RIDQLYDILEREVKARKYVEKNSDTLPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1267 D-------NKELTNEVKSLQQAK--SESE-HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK 1336
Cdd:PRK04778 318 FlehakeqNKELKEEIDRVKQSYtlNESElESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK 397
|
410 420
....*....|....*....|....*
gi 688558686 1337 KGIKLTKDVSSLESQLQDTQELLQE 1361
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREKLER 422
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1111-1221 |
4.53e-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: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1111 AQIDELKIQLAKKEEELQAVLARGDEEVAQKnnalkqLRELQAQLAELQEDLESEKaARNKAEKlkrDLSEELEALKTEL 1190
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALK-ARWEAEK---ELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 688558686 1191 EDTLDTTAAQQELRSKREQEVAELKKAIDDE 1221
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1078-1378 |
4.73e-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: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1078 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAqlae 1157
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTR---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1158 lQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQElrskreqevaelkkaiddetrNHESQIQEMrQRHg 1237
Cdd:pfam15905 137 -VNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE---------------------GMEGKLQVT-QKN- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1238 taLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLeAQLQEVMArfsegekvkgELADRT 1317
Cdd:pfam15905 193 --LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDI-AQLEELLK----------EKNDEI 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1318 HKIQTELDNVSCLLEdaekkgiKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEE 1378
Cdd:pfam15905 260 ESLKQSLEEKEQELS-------KQIKDLNEKCKLLEsEKEELLREYEEKEQTLNAELEELKE 314
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1613-1822 |
5.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1613 RDLQARDEQNEEKKRALVKQVREMEAELEDerkqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1692
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1693 QRELEEARTSRD--EIFTQSKENEKKLKSLEA----------EILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1760
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESFSDFLDRLSAlskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1761 ALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENAR 1822
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1075-1295 |
5.40e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1075 EERLKKEEKTRQEleKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQ 1154
Cdd:PRK05035 459 QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1155 LAELQEDLESEKA-----ARNKAEKLKR-----DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRN 1224
Cdd:PRK05035 537 KQAAAAADPKKAAvaaaiARAKAKKAAQqaanaEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1225 HESQIQEMR-QRHGTALEEISEQLEQAK--RVKGNLEKNK-----QTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1295
Cdd:PRK05035 617 VAAAIARAKaKKAEQQANAEPEEPVDPRkaAVAAAIARAKarkaaQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
893-1191 |
5.57e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 893 DEELIKVKERQVKVENELVEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLVAKkqELEEILHDLESRVEE 968
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklRSYLPKLNPLREEKKKVSVKSLEELIK--DVEEELEKIEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 969 EEERNQSLQNEKKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDIllledqnsKFLKEKKLLEDRVGEMTS 1048
Cdd:PRK05771 105 LEEEISELENEIKELEQEIE----------------RLEPW------GNFDLDL--------SLLLGFKYVSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1049 QLAEEEEKAKNLGKV----KNKQEMMMV---------DLEERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDE 1115
Cdd:PRK05771 155 DKLEELKLESDVENVeyisTDKGYVYVVvvvlkelsdEVEEELKKLGFERLELE-EEGTPSELIREIKEELEEIEKERES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1116 LK---IQLAKKEEELQAVLARGDEEVAQKNNALKQLRE------LQA-----QLAELQEDLesEKAARNKAEKLKRDLSE 1181
Cdd:PRK05771 234 LLeelKELAKKYLEELLALYEYLEIELERAEALSKFLKtdktfaIEGwvpedRVKKLKELI--DKATGGSAYVEFVEPDE 311
|
330
....*....|
gi 688558686 1182 ELEALKTELE 1191
Cdd:PRK05771 312 EEEEVPTKLK 321
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1039-1123 |
6.12e-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: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1039 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqEMMMVDLEERLK----------KEEKTRQELEKAKRKLDAETTDLQDQIAE 1108
Cdd:cd23165 11 LNARLHELKEELKAKKKELENLEDASD--ELELADDDEPVPykigevfvhlSLEEAQERLEKAKEELEEEIEKLEEEIDE 88
|
90
....*....|....*
gi 688558686 1109 LQAQIDELKIQLAKK 1123
Cdd:cd23165 89 IEEEMKELKVQLYAK 103
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1002-1202 |
6.74e-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: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1002 QKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqemmMVDLEERLKKE 1081
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA----------LTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1082 EKTR-QELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARgdEEVAQKNNALKQLR---------EL 1151
Cdd:pfam04012 88 ALAEkKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTSLgslstssatDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 688558686 1152 QAQLAELQEDLESEKAARNKAEKlKRDLSEELEALKTELEDTLDTTAAQQE 1202
Cdd:pfam04012 166 FERIEEKIEEREARADAAAELAS-AVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1070-1209 |
6.97e-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: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1070 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLR 1149
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLA-------TERSARREAEAELE 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1150 ELQAQLAELQEDLESEKAARnkaEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ 1209
Cdd:pfam09787 118 RLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQ 174
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1720-1858 |
7.24e-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: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1720 LEAEILQLQEDLASSERARRHAEQERD---ELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1796
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1797 TTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS---KLQELEGSVKSKFKASIAALEAKI 1858
Cdd:pfam00529 136 GGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1228-1379 |
7.34e-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: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1228 QIQEMR----QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1303
Cdd:pfam10168 540 ATQVFReeylKKHDLAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1304 -------SEGEKvkgELADRTHKIQTELDNVSCLLEDAEKK------------GIKLTKDVSSLESQLQDTQELLQEETR 1364
Cdd:pfam10168 620 nsqlpvlSDAER---EMKKELETINEQLKHLANAIKQAKKKmnyqryqiaksqSIRKKSSLSLSEKQRKTIKEILKQLGS 696
|
170
....*....|....*
gi 688558686 1365 QKLNLSSRIRQLEEE 1379
Cdd:pfam10168 697 EIDELIKQVKDINKH 711
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1068-1202 |
7.80e-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: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1068 EMMMVDLEERLKKE--EKTRQELEKAKRKLDAETTDLQD------------QIAELQAQIDELKIQLAKKEEELQAVLAR 1133
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1134 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLkrdlsEELEALKTEL---EDTLDTTAAQQE 1202
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1564-1749 |
8.95e-04 |
|
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: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1564 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDE 1643
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1644 RKQRALAVAAKKKLEmdlkdveaqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARTSRDEIFTQSKENEKKLKSLEAE 1723
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 688558686 1724 ILQLQEDLASSERARRHAEQERDELA 1749
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1678-1965 |
9.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1678 AIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAE---QERDELADEISN 1754
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1755 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttmqvdtlntelAGERSAAQKSENARQQLERQNKDLKS 1834
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1835 KLQELEgSVKSKFKASIAALEAKIlqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANsRM 1914
Cdd:PRK03918 308 ELREIE-KRLSRLEEEINGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-EL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 688558686 1915 KQLKRQLeeaeeeatrANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1965
Cdd:PRK03918 375 ERLKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1048-1186 |
1.02e-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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1048 SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEEL 1127
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAA 607
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1128 QAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1186
Cdd:COG3096 608 QDALERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1647-1856 |
1.07e-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: 43.51 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1647 RALAVAAKKKLEMDLKD-----VEAQIEAANKARDEA---IKQLRKLQAQMKDYQRELEEARTSRDEIFTQ--SKENEKK 1716
Cdd:cd22656 101 DDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAakvVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1717 LKSLEAEILQLQEDLAsserarRHAEQERDELADEISNsasgkaalLDEKRRLEARIaqleeeleeeQSNMELLNDrfrk 1796
Cdd:cd22656 181 IKDLQKELEKLNEEYA------AKLKAKIDELKALIAD--------DEAKLAAALRL----------IADLTAADT---- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1797 ttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEA 1856
Cdd:cd22656 233 ---DLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
896-1126 |
1.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 896 LIKVKERQVKVENELVEMERKH--QQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERN 973
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 974 QSLQNEKKKMQShiqdleeqldeeEAARQKLQLEKVTAEAK--------------IKKMEEDILLLEDQNSKFLKEKKLL 1039
Cdd:PHA02562 251 EDPSAALNKLNT------------AAAKIKSKIEQFQKVIKmyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1040 EDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ 1119
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKIS----TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
....*..
gi 688558686 1120 LAKKEEE 1126
Cdd:PHA02562 395 KSELVKE 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1292-1641 |
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 688558686 1292 LEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKgikLTKDVSSLESQLQDTQELLQEETRQKLNLSS 1371
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE---LESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1372 RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE------DDVGALEGLEEVKRK-LQKDMEVTSQKLE 1444
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkeraKKAGAQRKEEEAERKqLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1445 EKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1524
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1525 RALDEALEAKEEFERLNKQL--------------RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1590
Cdd:pfam07888 269 RTQAELHQARLQAAQLTLQLadaslalregrarwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVEL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1591 QATEDAKL----RLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELE 1641
Cdd:pfam07888 349 GREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
979-1181 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 979 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVtaEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAK 1058
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1059 NLgkvknKQEMMMVDLEERLKKEEKTRQElekakrkldaettDLQDQIAELQAQIDELKIQLAKKE---EELQAVLargd 1135
Cdd:pfam06160 309 EL-----KEELERVQQSYTLNENELERVR-------------GLEKQLEELEKRYDEIVERLEEKEvaySELQEEL---- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 688558686 1136 eevaqkNNALKQLRELQAQLAELQEDLES----EKAARNKAEKLKRDLSE 1181
Cdd:pfam06160 367 ------EEILEQLEEIEEEQEEFKESLQSlrkdELEAREKLDEFKLELRE 410
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1082-1368 |
1.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1082 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQED 1161
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1162 LESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE 1241
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1242 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHkRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ 1321
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 688558686 1322 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN 1368
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1642-1832 |
1.39e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1642 DERKQRALAVAAKKKLEMDLK---DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN----- 1713
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrq 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1714 -EKKLKSLEAEILQLQEDLAS-----------SERARR---HAEQERDELADEISNSASGKAALLDEKR-RLEARIAQle 1777
Cdd:PRK11281 126 lESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQAEQAL-- 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1778 eeleeeqsnMELLNDrFRKTTMQVDTLNTELaGERSAAQKSENArQQLERQNKDL 1832
Cdd:PRK11281 204 ---------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQLQLL 246
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1113-1295 |
1.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1113 IDELKIQLAKKEEELQAvlargdEEVAQKNNALKQLRELQAQ--LAELQEDLESE-KAARNKAEKLKRDLSEELEALKTE 1189
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1190 LEDTLDTTA---AQQELRSKREQEVAELKKaiddetrnhesQIQEMRQRHGTALEEISE-QLEQAKRVKgnLEKNKQTLE 1265
Cdd:PRK12704 102 LELLEKREEeleKKEKELEQKQQELEKKEE-----------ELEELIEEQLQELERISGlTAEEAKEIL--LEKVEEEAR 168
|
170 180 190
....*....|....*....|....*....|
gi 688558686 1266 SDNKELTNEVKslQQAKSESEHKRKKLEAQ 1295
Cdd:PRK12704 169 HEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1033-1704 |
1.51e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1033 LKEKKLLEDRVGEMTSQLAE----------EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL 1102
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSEleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1103 QDQIAELQAQIDELKiQLAKKEEELQAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1182
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1183 LEALkteledTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISeqleqakRVKGNLEK 1259
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAG 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1260 NKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE--GEKVKGELA--DRTHKIQTELDNVSCLLEdae 1335
Cdd:PRK04863 728 LEDCPE-DLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpEVPLFGRAAreKRIEQLRAEREELAERYA--- 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1336 kkgiKLTKDVSSLESQLQDTQELLQ-----------EETRQKLNlsSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1404
Cdd:PRK04863 804 ----TLSFDVQKLQRLHQAFSRFIGshlavafeadpEAELRQLN--RRRVELERALADHESQEQQQRSQLEQAKEGLSAL 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1405 QAQLVETKKKLEDDVGalEGLEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQ---QELDDLMVDLDHQRQIVSNL 1481
Cdd:PRK04863 878 NRLLPRLNLLADETLA--DRVEEIREQL-DEAEEAKRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDA 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1482 ekKQKKFDqmlaeektisarYAEERDRAEAEAREKDTKALSMARALDEALEAK-EEFERLNKQLRAEMEDLISSKDDVGK 1560
Cdd:PRK04863 955 --KQQAFA------------LTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1561 NVHELEKSKRTLEQQVEEMRTQLEELedELQATEDAklrlevnmqAMKAQFDRD-LQARDEQNEEKKRALVKQVREMEAE 1639
Cdd:PRK04863 1021 VLASLKSSYDAKRQMLQELKQELQDL--GVPADSGA---------EERARARRDeLHARLSANRSRRNQLEKQLTFCEAE 1089
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1640 LEDERKQralavaaKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-----EEARTSRD 1704
Cdd:PRK04863 1090 MDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELaylsaDELRSMSD 1152
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
929-1335 |
1.58e-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: 43.30 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 929 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshiqdleeqldeeeaarqklqlek 1008
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT----------------------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1009 vtaeakikkmeedillLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEE--------KAKnlgKVKNKQEMMMVDLEERLkk 1080
Cdd:pfam06160 137 ----------------LLANRFSYGPAIDELEKQLAEIEEEFSQFEEltesgdylEAR---EVLEKLEEETDALEELM-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1081 eEKTRQELEKAKRKLDAETTDLQDQIAELQAQ---IDELKI-----QLAKKEEELQAVLARGDEEVAQKNNalkqlRELQ 1152
Cdd:pfam06160 196 -EDIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVdkeiqQLEEQLEENLALLENLELDEAEEAL-----EEIE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1153 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---ID 1219
Cdd:pfam06160 270 ERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlNENELERVRglEKQLEELEKRydeIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1220 DETRNHE---SQIQEMrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKseSEHKRKKLEAQL 1296
Cdd:pfam06160 350 ERLEEKEvaySELQEE-------LEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL--REIKRLVEKSNL 420
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 688558686 1297 ----QEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1335
Cdd:pfam06160 421 pglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQ 463
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1053-1597 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1053 EEEKAKNLGKVKNKQEMMMVDL----EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ 1128
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1129 A-----------VLARGDEEVAQKNNALKQlRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELE 1191
Cdd:pfam07111 215 AqvtlveslrkyVGEQVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQPS 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1192 DTLD---TTAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1268
Cdd:pfam07111 294 DSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1269 ---KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKK--GIK-LT 1342
Cdd:pfam07111 373 msaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKgLM 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1343 KDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeeSRKNLEKQLATLQAQLvETKKKLEDDVGAL 1422
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER------------NRLDAELQLSAHLIQQ-EVGRAREQGEAER 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1423 EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSnlekkqKKFDQMLAEEKTISARY 1502
Cdd:pfam07111 520 QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYG------QALQEKVAEVETRLREQ 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1503 AEERDRAEAEAREKDTKALSMARALDEalEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR----TLEQQVEE 1578
Cdd:pfam07111 594 LSDTKRRLNEARREQAKAVVSLRQIQH--RATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLL 671
|
570
....*....|....*....
gi 688558686 1579 MRTQLEELEDELQATEDAK 1597
Cdd:pfam07111 672 SRYKQQRLLAVLPSGLDKK 690
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1073-1228 |
1.73e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.29 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1073 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLREL 1151
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAAL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558686 1152 QAQLAELQEDLESeKAARNKAEKLKRDL-SEELEALKTELEdtldttAAQQELRSKREQEVAELKKAIDDETRNHESQ 1228
Cdd:pfam12795 162 KAQIDMLEQELLS-NNNRQDLLKARRDLlTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1458-1892 |
1.86e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.97 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1458 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeEKTISARYAEERDRAEAEAREKDTKALsMARALDEALEAKEEF 1537
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRARLLLLALAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1538 ERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQA 1617
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1618 RDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE 1697
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1698 EARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLE 1777
Cdd:COG5278 326 AALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1778 EELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAK 1857
Cdd:COG5278 406 AAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
410 420 430
....*....|....*....|....*....|....*
gi 688558686 1858 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQ 1892
Cdd:COG5278 486 EAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1682-1845 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1682 LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEisnsasgKAA 1761
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-------KDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1762 LLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEG 1841
Cdd:pfam07888 120 LLAQRAAHEARIRE--------------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
....
gi 688558686 1842 SVKS 1845
Cdd:pfam07888 186 ELRS 189
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1623-1896 |
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 688558686 1623 EEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTS 1702
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1703 RDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1782
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1783 EQSNMELLNDRFRKTTMQ-VDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQL 1861
Cdd:COG4372 190 KEANRNAEKEEELAEAEKlIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270
....*....|....*....|....*....|....*
gi 688558686 1862 EEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDE 1896
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1564-1775 |
1.92e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1564 ELEKSKRTLEQQVEEMRTQLEELED-ELQATEDAKLRLEVNMQAmkaqfdrdlqardeqNEEKKRALVKQVREMeaeL-E 1641
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLS---------------NAEKLREALQEALEA---LsG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1642 DERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE---------EARTSR--------- 1703
Cdd:COG0497 238 GEGGALDLLGQALRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdperleevEERLALlrrlarkyg 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1704 ---DEIFTQSKENEKKLKSLEAeilqLQEDLASSERARRHAEQERDELADEISNsASGKAAlldekRRLEARIAQ 1775
Cdd:COG0497 317 vtvEELLAYAEELRAELAELEN----SDERLEELEAELAEAEAELLEAAEKLSA-ARKKAA-----KKLEKAVTA 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
881-1066 |
2.11e-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: 42.83 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 881 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK----HQQLLEEKNILAEQLQA--------------ETELFAEAE 942
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 943 EMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeQLDEEEAARQKLQLEKVTAEAKIKKMEEDI 1022
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 688558686 1023 LLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1066
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1549-1723 |
2.11e-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: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1549 EDLISSKDDvGKNVHELEkSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRA 1628
Cdd:pfam09787 24 EKLIASLKE-GSGVEGLD-SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1629 LVKQV---REMEAEL-----------EDERKQRALAVAAKKKLEMDLKDVEAQIEA---ANKARDEAIKQLRKLQAQMKD 1691
Cdd:pfam09787 102 LATERsarREAEAELerlqeelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQ 181
|
170 180 190
....*....|....*....|....*....|..
gi 688558686 1692 YQRELEEARTSRDEIFTQSKENEKKLKSLEAE 1723
Cdd:pfam09787 182 KQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1032-1187 |
2.15e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1032 FLKEKKLLEDRvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELqa 1111
Cdd:PRK12705 24 LLKKRQRLAKE-AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1112 qiDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQ---LRELQAQ---LAELQEDLESEKAARNKAEKLKRDLSEELEA 1185
Cdd:PRK12705 101 --DNLENQLEEREKALSARELELEELEKQLDNELYRvagLTPEQARkllLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
..
gi 688558686 1186 LK 1187
Cdd:PRK12705 179 QN 180
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1076-1185 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1076 ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEELQAvlARGDEEVAQKNNALKQLRELQAQL 1155
Cdd:COG2268 220 NREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAE--ANAEREVQRQLEIAEREREIELQE 296
|
90 100 110
....*....|....*....|....*....|...
gi 688558686 1156 AELQEDLESEKA---ARNKAEKLKRDLSEELEA 1185
Cdd:COG2268 297 KEAEREEAELEAdvrKPAEAEKQAAEAEAEAEA 329
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1336-1601 |
2.64e-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: 42.11 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1336 KKGIKLTKDVSSLESQlqdTQELLQEETRQklnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKL 1415
Cdd:pfam15905 66 QKNLKESKDQKELEKE---IRALVQERGEQ----DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1416 EDDVGALEGLEEVKRKLQKDMEVTS--QKLEEKA-IAFDKLEKTKNRLQQelddLMVDLDHQRQIVSNLEKKQKKFDQML 1492
Cdd:pfam15905 139 ELLKAKFSEDGTQKKMSSLSMELMKlrNKLEAKMkEVMAKQEGMEGKLQV----TQKNLEHSKGKVAQLEEKLVSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1493 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtl 1572
Cdd:pfam15905 215 IEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK--- 291
|
250 260
....*....|....*....|....*....
gi 688558686 1573 EQQVEEMRTQLEELEDELQATEDaKLRLE 1601
Cdd:pfam15905 292 EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1036-1199 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1036 KKLLEDRVGEMTSQLAEEEEKAKnlgKVKNKqemmMVDLEERLKKEEKTRQELEKA-KRKLDAETTDL-QDQIAELQAQI 1113
Cdd:cd22656 116 KKTIKALLDDLLKEAKKYQDKAA---KVVDK----LTDFENQTEKDQTALETLEKAlKDLLTDEGGAIaRKEIKDLQKEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1114 DELK----IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLK---RDLSEELEAL 1186
Cdd:cd22656 189 EKLNeeyaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIG---PAIPALEKLQgawQAIATDLDSL 265
|
170
....*....|...
gi 688558686 1187 KTELEDTLDTTAA 1199
Cdd:cd22656 266 KDLLEDDISKIPA 278
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1523-1651 |
2.81e-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: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1523 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVgknVHELEKSKRTLEQQVEEMRTQLEELEDEL---QATEDAKLR 1599
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQ---VERLEAEVEELEAELEEKDERIERLERELseaRSEERREIR 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1600 LEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAV 1651
Cdd:COG2433 463 KDREISRLDREIER-LERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1081-1213 |
2.87e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1081 EEKTRQELEKAKrKLDAE-TTDLQDQIAELQAqidELKIQLAKKEEELQAVLARGDEEvaqknNALKQLRELQAQLAELQ 1159
Cdd:PTZ00491 642 DERTRDSLQKSV-QLAIEiTTKSQEAAARHQA---ELLEQEARGRLERQKMHDKAKAE-----EQRTKLLELQAESAAVE 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1160 ---------------EDLESE---KAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1213
Cdd:PTZ00491 713 ssgqsraealaeaeaRLIEAEaevEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD 784
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1238-1736 |
2.91e-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: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1238 TALEEISEQLEQAKRVKGNLEKN-------KQTLESDNKELTNEVKSLQQAKSESEHKRKKleaQLQEVMARFSEgEKVK 1310
Cdd:pfam15818 7 TSLLEALEELRMRREAETQYEEQigkiiveTQELKWQKETLQNQKETLAKQHKEAMAVFKK---QLQMKMCALEE-EKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1311 GELADRTHkiQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQdTQELLQEETRQKLNlssrirQLEEEKNNLLEQQEEE 1390
Cdd:pfam15818 83 YQLATEIK--EKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQ-LHLLAKEDHHKQLN------EIEKYYATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1391 EESRKNLEKQLA---TLQAQLVETKKKLEDDVGAL-EGLEEVKRKLQKDmEVTSQ-KLEEKAIAFDKLEKTKNRLQQELD 1465
Cdd:pfam15818 154 KENHGKLEQNVQeaiQLNKRLSALNKKQESEICSLkKELKKVTSDLIKS-KVTCQyKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1466 -DLMVDLDHQRQIVSNLEKKQKKFdqmlaeektISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERlnKQL 1544
Cdd:pfam15818 233 mELELNKKINEEITHIQEEKQDII---------ISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQR--EKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1545 RAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrdlqarDEQNEE 1624
Cdd:pfam15818 302 KENEEKFLNLQN-------EHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQ--------KKFEED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1625 KKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQReLEeaRTSRD 1704
Cdd:pfam15818 367 KKFQNVPEVNNENSEMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQV-LE--KSFKN 443
|
490 500 510
....*....|....*....|....*....|..
gi 688558686 1705 EIFTQSKENEKKLKSLEAEILQLQEDLASSER 1736
Cdd:pfam15818 444 EIDTSVPQDKNQSEISLSKTLCTDKDLISQGQ 475
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1657-1827 |
2.93e-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: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1657 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQ---RELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLAs 1733
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1734 seRARRHAEQE---RDELADEISNSASGKAALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELag 1810
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL-- 200
|
170
....*....|....*..
gi 688558686 1811 ersaaqksENARQQLER 1827
Cdd:pfam00529 201 --------KLAKLDLER 209
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1163-1380 |
2.95e-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: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1163 ESEKAARNKAEKLKRdlSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNhESQIQEMRQRHGTALEE 1242
Cdd:TIGR00927 637 EAEHTGERTGEEGER--PTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEG-EGEIEAKEADHKGETEA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1243 ISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGEL-ADRTHKIQ 1321
Cdd:TIGR00927 713 EEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIqAGEDGEMK 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1322 TElDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1380
Cdd:TIGR00927 793 GD-EGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1087-1187 |
3.42e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1087 ELEKAKRKLDAETTDLQ---DQIAELQAQIDELKiQLAKK----EEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1159
Cdd:COG0497 276 ELEEAASELRRYLDSLEfdpERLEEVEERLALLR-RLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAE 354
|
90 100 110
....*....|....*....|....*....|....
gi 688558686 1160 EDLEsEKAA------RNKAEKLKRDLSEELEALK 1187
Cdd:COG0497 355 AELL-EAAEklsaarKKAAKKLEKAVTAELADLG 387
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1075-1254 |
3.65e-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: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1075 EERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKI------QLAKKEEEL---QAVLARGDEEVaqknnal 1145
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIkdkQEKLMRRCKKV------- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1146 kqLRELQAQLAELqedLESEkaarnkaeklkRDLSEELEALKTELEdTLDttAAQQELRSKREQEVAELKKAIDDETRN- 1224
Cdd:pfam10168 616 --LQRLNSQLPVL---SDAE-----------REMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSIRKKSs 676
|
170 180 190
....*....|....*....|....*....|....*.
gi 688558686 1225 ------HESQIQEMRQRHGtalEEISEQLEQAKRVK 1254
Cdd:pfam10168 677 lslsekQRKTIKEILKQLG---SEIDELIKQVKDIN 709
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
980-1376 |
3.91e-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: 42.15 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 980 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVTA----------------------EAKIKKMEEDILLLEDQNSK--FLKE 1035
Cdd:pfam06160 5 RKKIYKEIDELEERKNELMNLPVQEELSKVKKlnltgetqekfeewrkkwddivTKSLPDIEELLFEAEELNDKyrFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1036 KKLLEdrvgEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ-------IAE 1108
Cdd:pfam06160 85 KKALD----EIEELLDDIEEDIKQILE----------ELDELLESEEKNREEVEELKDKYRELRKTLLANrfsygpaIDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1109 LQAQIDELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALK- 1187
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTES----GDYLEAR-----EVLEKLEEETDALEELMEDIPPL---YEELKTELPDQLEELKe 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1188 --TELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEK 1259
Cdd:pfam06160 219 gyREMEeegyalEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1260 NKQTLESD-------NKELTNEVKSLQQ----AKSESEHKR------KKLEAQLQEVMARFSEGEKVKGELADRTHKIQT 1322
Cdd:pfam06160 292 NLPEIEDYlehaeeqNKELKEELERVQQsytlNENELERVRglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILE 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 688558686 1323 ELDNVsclledaEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1376
Cdd:pfam06160 372 QLEEI-------EEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1345-1565 |
4.03e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1345 VSSLESQLqDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEG 1424
Cdd:PHA02562 190 IDHIQQQI-KTYNKNIEEQRKK---NGENIARKQNKYDELVEEA------KTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1425 LEEVKRKLQKDME----------------VTSQKLEEKAiafDKLEKTKNR---LQQELDDLMVDLDHQRQIVSNLEKKQ 1485
Cdd:PHA02562 260 LNTAAAKIKSKIEqfqkvikmyekggvcpTCTQQISEGP---DRITKIKDKlkeLQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1486 KKFDQMLAEEKTISARYAEERDRAeaeareKDTKALsMARALDEALEAKEEFERLNKQLraemEDLISSKDDVGKNVHEL 1565
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKA------KKVKAA-IEELQAEFVDNAEELAKLQDEL----DKIVKTKSELVKEKYHR 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1422-1931 |
4.14e-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: 42.26 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1422 LEGLEEVKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISAR 1501
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHG----KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1502 YaeerdraeaearekdtkalsmaRALDEALEAKEEFERLNKQLRAEMEDLISSKddvgkNVHELEKSKRTLEQQVEEMRT 1581
Cdd:TIGR00618 245 L----------------------TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1582 QLEELEDELQATEDAKLRLEVNMQAM-KAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKK---L 1657
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1658 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1737
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1738 RRHAEQERDELADEISNSASGKAALLDEKRRLEARIAqleeELEEEQSNMELLNDRFRKTTMQVdTLNTELAGERSAAQK 1817
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1818 SENARQQLERQNKDLKSKLQELE---GSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1894
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510
....*....|....*....|....*....|....*..
gi 688558686 1895 DERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRA 1931
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1036-1218 |
4.27e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1036 KKLLEDRVGEMTSQLAE-EEEKAKNLGKVKnKQEMMMVDLEERLKK-EEKTRQELEKA-----------KRKLDAETTDL 1102
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEaRQALAQVIANQK-RLERQLEELEAEAEKwEEKARLALEKGredlarealerKAELEAQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1103 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNAlkqlrELQAQLAELQEDLESEKAAR--NKAEKLKRDLS 1180
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-----KAQEKVNEALSGIDSDDATSalERMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 688558686 1181 EELEALKT-ELEDTLDTTAAQQELRSKREQEVAELKKAI 1218
Cdd:COG1842 179 ARAEAAAElAAGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1662-1766 |
4.87e-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: 39.34 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1662 KDVEAQIEAANKARDEAIKQLrklqaqmKDYQRELEEARTSRDEIFTQSKENEKKLKslEAEILQLQEDLASS-ERARRH 1740
Cdd:cd06503 33 EKIAESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAE 103
|
90 100
....*....|....*....|....*.
gi 688558686 1741 AEQERDELADEISNSASGKAALLDEK 1766
Cdd:cd06503 104 IEQEKEKALAELRKEVADLAVEAAEK 129
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1036-1187 |
4.92e-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: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1036 KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD----AETTDLQDQIAELQA 1111
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1112 QIDELKIQLAKKEEELQAVlargdEEVAQKNNALKQlrELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALK 1187
Cdd:smart00787 219 EIMIKVKKLEELEEELQEL-----ESKIEDLTNKKS--ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1624-1919 |
4.99e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1624 EKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1703
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1704 DEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKaALLDEKRRLEARIAQLEEELEEE 1783
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1784 QSNMELLNdRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKAsIAALEAKILqlee 1863
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK-ADELHEEII---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1864 qleqeakeraAANKIVRRTEKKLKEVFMQVEDERRHADQyKEQMEKANSRMKQLKR 1919
Cdd:COG1340 234 ----------ELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1525-1959 |
5.01e-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: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1525 RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELqatedaklrlEVNM 1604
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDEL----------EKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1605 QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQ-RALAVAAKKKLEMDLKDVEA---QIEAANKA--RDEA 1678
Cdd:pfam06160 156 AEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyrEMEEEGYAleHLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1679 IKQLRKLQAQMKDYQRELEEARTsrdeiftqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1758
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLEL---------DEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1759 KAALLDEKRRLeariaqleeeleeeQSNMELLND---RFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1835
Cdd:pfam06160 307 NKELKEELERV--------------QQSYTLNENeleRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1836 LQELEGSVKsKFKASIAALEakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKAN 1911
Cdd:pfam06160 373 LEEIEEEQE-EFKESLQSLR--------------KDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVS 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 688558686 1912 SRMKQLKRQLeeaeeeatraNASR---RKLQRELDDATEASEGLSREVNTL 1959
Cdd:pfam06160 436 DEIEDLADEL----------NEVPlnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1034-1190 |
5.01e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1034 KEKKL--LEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKakrkLDAEttdLQDQIAELQA 1111
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQA----LLAE---LAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558686 1112 QIDELKIQLAkkeeELQAVLARgdeevaqknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTEL 1190
Cdd:PRK09039 117 RAGELAQELD----SEKQVSAR----------ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1555-1718 |
5.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1555 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaKLRLEVNMQAmkaqfdrdlqardEQNEEKKRALVkqvr 1634
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE--KLKEELEEKK-------------EKLQEEEDKLL---- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1635 emeAELEDERKQRalavaakkklemdlkdveaqIEAANKARDEAIKQLRKLQA---------QMKDYQRELEEARTSRDE 1705
Cdd:PRK00409 569 ---EEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKggyasvkahELIEARKRLNKANEKKEK 625
|
170
....*....|...
gi 688558686 1706 IFTQSKENEKKLK 1718
Cdd:PRK00409 626 KKKKQKEKQEELK 638
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1062-1185 |
5.45e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1062 KVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQK 1141
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS---FERLAELRDELAELE-------EELEALKARWEAEKELI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 688558686 1142 NNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1185
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1613-1748 |
5.75e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1613 RDLQARDEQNEEKKRALVKQVREMEAELEDERkqralavaakkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1692
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEE----------------IRRLEEQVERLEAEVEELEAELEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558686 1693 QRELEEARTSRDEiftqSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDEL 1748
Cdd:COG2433 447 ERELSEARSEERR----EIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1085-1187 |
5.85e-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: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1085 RQELEKAKRKLDAETTDLQDQIAELQAQIDELkIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLES 1164
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAY-AAAQAALATAQKELA--NAQAQALQTAQNNLATAQAALANAEARLAK 336
|
90 100
....*....|....*....|...
gi 688558686 1165 EKAArnkAEKLKRDLSEELEALK 1187
Cdd:TIGR04320 337 AKEA---LANLNADLAKKQAALD 356
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1268-1497 |
5.96e-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: 41.55 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1268 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG-----EKVKGELADRTHKIQTELDNVSC---------LLED 1333
Cdd:pfam05667 249 LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSsttdtGLTKGSRFTHTEKLQFTNEAPAAtsspptkveTEEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1334 AEKKGiklTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQlVETKK 1413
Cdd:pfam05667 329 LQQQR---EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEEL--------------EELKEQNEELEKQ-YKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1414 KLeddVGALEGLEEVKRKLQKDMEVTSQKLEE-------------------KAIAFDKLEKTKNRLQ--QELDDLMvdld 1472
Cdd:pfam05667 391 KT---LDLLPDAEENIAKLQALVDASAQRLVElagqwekhrvplieeyralKEAKSNKEDESQRKLEeiKELREKI---- 463
|
250 260
....*....|....*....|....*
gi 688558686 1473 hqRQIVSNLEKKQKKFDQMLAEEKT 1497
Cdd:pfam05667 464 --KEVAEEAKQKEELYKQLVAEYER 486
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1534-1686 |
6.15e-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: 40.82 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1534 KEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA--TEDAKLRLEVNMQAMKAQF 1611
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDllTDEGGAIARKEIKDLQKEL 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558686 1612 DrdlQARDEQNEEKKRALvKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeaankarDEAIKQLRKLQ 1686
Cdd:cd22656 189 E---KLNEEYAAKLKAKI-DELKALIADDEAKLAAALRLIADLTAADTDLDNLLALI-------GPAIPALEKLQ 252
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1504-1753 |
6.74e-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: 40.40 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1504 EERDRAEAEAREKDTKalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKskrtLEQQVEEMRTQL 1583
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEE----AEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1584 EELEDELQATEDAKLRLEVNMQAMKAqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKD 1663
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKE--------IAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1664 V-------EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskenEKKLKSLEAEILQLQEDLASSER 1736
Cdd:pfam00261 153 VgnnlkslEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFA--------------ERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|....*..
gi 688558686 1737 ARRHAEQERDELADEIS 1753
Cdd:pfam00261 219 KYKAISEELDQTLAELN 235
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1201-1463 |
7.07e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1201 QELRSKREQEVAELK--KAIDDETRN--HESQIQEMRQRHGTA-LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTnEV 1275
Cdd:pfam15905 59 LELKKKSQKNLKESKdqKELEKEIRAlvQERGEQDKRLQALEEeLEKVEAKLNAAVREKTSLSASVASLEKQLLELT-RV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1276 KSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDT 1355
Cdd:pfam15905 138 NELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1356 QELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1435
Cdd:pfam15905 218 KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
250 260
....*....|....*....|....*...
gi 688558686 1436 MEVTSQKLEEkaiafdKLEKTKNRLQQE 1463
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 ... |
1081-1191 |
7.08e-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: 38.04 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1081 EEKTRQELEKAKRkldaettdlqDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQE 1160
Cdd:pfam16516 1 EELKRKEMEKVYK----------DEIDCLQAQLQAAEEALAAKQREIDEL----KQEIAQKEEDLETISVLKAQAEVYRS 66
|
90 100 110
....*....|....*....|....*....|.
gi 688558686 1161 DLESEKAARNKAEKLKRDLSEELEALKTELE 1191
Cdd:pfam16516 67 DFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
886-1220 |
7.17e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 886 EEEMQAKDEELIKVKERQVKVENELVE--------MERKHQQLLEEKNILAEQLQAETELFAEAEEMRA-RLVAKKQELE 956
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINksineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 957 EILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarqklqlekvtaeakIKKMEEDILLLEDQNSKFLKEK 1036
Cdd:PRK01156 569 SWLNALAVISLIDIETNRSRSNEIKKQLNDL---------------------------ESRLQEIEIGFPDDKSYIDKSI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1037 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvdleeRLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL 1116
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKID--------NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1117 KIQLAKKEEELQAVLARgdeevaqknnalkqLRELQAQLAELQEDLESEKaarnKAEKLKRDLSEELEALKTELEDTLDT 1196
Cdd:PRK01156 694 KANRARLESTIEILRTR--------------INELSDRINDINETLESMK----KIKKAIGDLKRLREAFDKSGVPAMIR 755
|
330 340
....*....|....*....|....
gi 688558686 1197 TAAQQELRSKREQEVAELKKAIDD 1220
Cdd:PRK01156 756 KSASQAMTSLTRKYLFEFNLDFDD 779
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1569-1723 |
7.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1569 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFDRDLQARDEQNEEKKRALVKQVREMEAELED 1642
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1643 ERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEAR-TSRDEIFTQSKENEKKLKs 1719
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEeEARHEAAVLIKEIEEEAK- 183
|
....
gi 688558686 1720 LEAE 1723
Cdd:PRK12704 184 EEAD 187
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1505-1748 |
7.64e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1505 ERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEmedlisskdDVGKNVHELEKSKRTLEQQVEEmRTQLE 1584
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKS-ISSLK 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1585 E--LEDELQATEdaklrlevnmqaMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEM-DL 1661
Cdd:COG5022 899 LvnLELESEIIE------------LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVEsKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1662 KDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqsKENEKKLKSLEAEILQLQ--EDLASSERARR 1739
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL----QESTKQLKELPVEVAELQsaSKIISSESTEL 1042
|
....*....
gi 688558686 1740 HAEQERDEL 1748
Cdd:COG5022 1043 SILKPLQKL 1051
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1231-1552 |
8.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1231 EMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1310
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1311 GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknNLLEQQEEE 1390
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1391 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1470
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1471 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1550
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
..
gi 688558686 1551 LI 1552
Cdd:COG4372 335 LL 336
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
881-1182 |
8.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 881 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 960
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 961 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1040
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1041 DRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQL 1120
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558686 1121 AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1182
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1662-1766 |
9.65e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.62 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1662 KDVEAQIEAANKARDEAikqlrklQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKslEAEILQLQEDLAS-SERARRH 1740
Cdd:COG0711 34 EKIADGLAEAERAKEEA-------EAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAE 104
|
90 100
....*....|....*....|....*.
gi 688558686 1741 AEQERDELADEISNSASGKAALLDEK 1766
Cdd:COG0711 105 IEQERAKALAELRAEVADLAVAIAEK 130
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1635-1728 |
9.96e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558686 1635 EMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLR-KLQAQMKDYQRELEEARTSRDEIFT--QSK 1711
Cdd:cd16269 195 EKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKeKMEEERENLLKEQERALESKLKEQEalLEE 274
|
90
....*....|....*..
gi 688558686 1712 ENEKKLKSLEAEILQLQ 1728
Cdd:cd16269 275 GFKEQAELLQEEIRSLK 291
|
|
| |
